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Review

Use of attenuated paramyxoviruses for cancer therapy

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Pages 1275-1302 | Published online: 09 Jan 2014

References

  • Parato KA, Senger D, Forsyth PA, Bell JC. Recent progress in the battle between oncolytic viruses and tumours. Nat. Rev. Cancer5, 965–976 (2005).
  • Nemunaitis J, Khuri F, Ganly I et al. Phase II trial of intratumoral administration of ONYX-015, a replication-selective adenovirus, in patients with refractory head and neck cancer. J. Clin. Oncol.19, 289–298 (2001).
  • Nemunaitis J, Ganly I, Khuri F et al. Selective replication and oncolysis in p53 mutant tumors with ONYX-015, an E1B-55-kD gene-deleted adenovirus, in patients with advanced head and neck cancer: a Phase II trial. Cancer Res.60, 6359–6366 (2000).
  • Ganly I, Kirn D, Eckhardt G et al. A Phase I study of ONYX-015, an E1B attenuated adenovirus, administered intratumorally to patients with recurrent head and neck cancer. Clin. Cancer Res.6, 798–806 (2000).
  • Khuri FR, Nemunaitis J, Ganly I et al. A controlled trial of intratumoral ONYX-015, a selectively-replicating adenovirus, in combination with cisplatin and 5-fluorouracil in patients with recurrent head and neck cancer. Nat. Med.6, 879–885 (2000).
  • Vasey PA, Shulman LN, Campos S et al. Phase I trial of intraperitoneal injection of the E1B-55-kD-gene-deleted adenovirus ONYX-015 (dl1520) given on days 1 through 5 every 3 weeks in patients with recurrent/refractory epithelial ovarian cancer. J. Clin. Oncol.20, 1562–1569 (2002).
  • Habib NA, Sarraf CE, Mitry RR et al. E1B-deleted adenovirus (dl1520) gene therapy for patients with primary and secondary liver tumors. Hum. Gene Ther.12, 219–226 (2001).
  • Reid T, Galanis E, Abbruzzese J et al. Hepatic arterial infusion of a replication-selective oncolytic adenovirus (dl1520): Phase II viral, immunologic, and clinical endpoints. Cancer Res.62, 6070–6079 (2002).
  • Mulvihill S, Warren R, Venook A et al. Safety and feasibility of injection with an E1B-55 kDa gene-deleted, replication-selective adenovirus (ONYX-015) into primary carcinomas of the pancreas: a Phase I trial. Gene Ther.8, 308–315 (2001).
  • Hamid O, Varterasian ML, Wadler S et al. Phase II trial of intravenous CI-1042 in patients with metastatic colorectal cancer. J. Clin. Oncol.21, 1498–1504 (2003).
  • Hecht JR, Bedford R, Abbruzzese JL et al. A Phase I/II trial of intratumoral endoscopic ultrasound injection of ONYX-015 with intravenous gemcitabine in unresectable pancreatic carcinoma. Clin. Cancer Res.9, 555–561 (2003).
  • Freytag SO, Khil M, Stricker H et al. Phase I study of replication-competent adenovirus-mediated double suicide gene therapy for the treatment of locally recurrent prostate cancer. Cancer Res.62, 4968–4976 (2002).
  • Freytag SO, Stricker H, Pegg J et al. Phase I study of replication-competent adenovirus-mediated double-suicide gene therapy in combination with conventional-dose three-dimensional conformal radiation therapy for the treatment of newly diagnosed, intermediate- to high-risk prostate cancer. Cancer Res.63, 7497–7506 (2003).
  • DeWeese TL, van der Poel H, Li S et al. A Phase I trial of CV706, a replication-competent, PSA selective oncolytic adenovirus, for the treatment of locally recurrent prostate cancer following radiation therapy. Cancer Res.61, 7464–7472 (2001).
  • Yu W, Fang H. Clinical trials with oncolytic adenovirus in China. Curr. Cancer Drug Targets7, 141–148 (2007).
  • Xia ZJ, Chang JH, Zhang L et al. [Phase III randomized clinical trial of intratumoral injection of E1B gene-deleted adenovirus (H101) combined with cisplatin-based chemotherapy in treating squamous cell cancer of head and neck or esophagus.]. Ai Zheng23, 1666–1670 (2004).
  • Lu W, Zheng S, Li XF et al. Intra-tumor injection of H101, a recombinant adenovirus, in combination with chemotherapy in patients with advanced cancers: a pilot Phase II clinical trial. World J. Gastroenterol.10, 3634–3638 (2004).
  • Xu RH, Yuan ZY, Guan ZZ et al. [Phase II clinical study of intratumoral H101, an E1B deleted adenovirus, in combination with chemotherapy in patients with cancer]. Ai Zheng22, 1307–1310 (2003).
  • Benjamin R, Helman L, Meyers P, Reaman G. A Phase I/II dose escalation and activity study of intravenous injections of OCaP1 for subjects with refractory osteosarcoma metastatic to lung. Hum. Gene Ther.12, 1591–1593 (2001).
  • Small EJ, Carducci MA, Burke JM et al. A Phase I trial of intravenous CG7870, a replication-selective, prostate-specific antigen-targeted oncolytic adenovirus, for the treatment of hormone-refractory, metastatic prostate cancer. Mol. Ther.14, 107–117 (2006).
  • Nemunaitis J, Tong AW, Nemunaitis M et al. A Phase I study of telomerase-specific replication competent oncolytic adenovirus (telomelysin) for various solid tumors. Mol. Ther.18, 429–434 (2010).
  • Chang J, Zhao X, Wu X et al. A Phase I study of KH901, a conditionally replicating granulocyte-macrophage colony-stimulating factor: armed oncolytic adenovirus for the treatment of head and neck cancers. Cancer Biol. Ther.8, 676–682 (2009).
  • Li JL, Liu HL, Zhang XR et al. A Phase I trial of intratumoral administration of recombinant oncolytic adenovirus overexpressing HSP70 in advanced solid tumor patients. Gene Ther.16, 376–382 (2009).
  • Freytag SO, Movsas B, Aref I et al. Phase I trial of replication-competent adenovirus-mediated suicide gene therapy combined with IMRT for prostate cancer. Mol. Ther.15, 1016–1023 (2007).
  • Barton KN, Stricker H, Brown SL et al. Phase I study of noninvasive imaging of adenovirus-mediated gene expression in the human prostate. Mol. Ther.16, 1761–1769 (2008).
  • Markert JM, Medlock MD, Rabkin SD et al. Conditionally replicating herpes simplex virus mutant, G207 for the treatment of malignant glioma: results of a Phase I trial. Gene Ther.7, 867–874 (2000).
  • Markert JM, Liechty PG, Wang W et al. Phase Ib trial of mutant herpes simplex virus G207 inoculated pre- and post-tumor resection for recurrent GBM. Mol. Ther.17, 199–207 (2009).
  • Hu JC, Coffin RS, Davis CJ et al. A Phase I study of OncoVEXGM-CSF, a second-generation oncolytic herpes simplex virus expressing granulocyte macrophage colony-stimulating factor. Clin. Cancer Res.12, 6737–6747 (2006).
  • Fong Y, Kim T, Bhargava A et al. A herpes oncolytic virus can be delivered via the vasculature to produce biologic changes in human colorectal cancer. Mol. Ther.17, 389–394 (2009).
  • Varghese S, Rabkin SD. Oncolytic herpes simplex virus vectors for cancer virotherapy. Cancer Gene Ther.9, 967–978 (2002).
  • Mace AT, Ganly I, Soutar DS, Brown SM. Potential for efficacy of the oncolytic herpes simplex virus 1716 in patients with oral squamous cell carcinoma. Head Neck30, 1045–1051 (2008).
  • Harrow S, Papanastassiou V, Harland J et al. HSV1716 injection into the brain adjacent to tumour following surgical resection of high-grade glioma: safety data and long-term survival. Gene Ther.11, 1648–1658 (2004).
  • Mastrangelo MJ, Maguire HC Jr, Eisenlohr LC et al. Intratumoral recombinant GM-CSF-encoding virus as gene therapy in patients with cutaneous melanoma. Cancer Gene Ther.6, 409–422 (1999).
  • Park BH, Hwang T, Liu TC et al. Use of a targeted oncolytic poxvirus, JX-594, in patients with refractory primary or metastatic liver cancer: a Phase I trial. Lancet Oncol.9, 533–542 (2008).
  • Marshall JL, Hoyer RJ, Toomey MA et al. Phase I study in advanced cancer patients of a diversified prime-and-boost vaccination protocol using recombinant vaccinia virus and recombinant nonreplicating Avipox virus to elicit anti-carcinoembryonic antigen immune responses. J. Clin. Oncol.18, 3964–3973 (2000).
  • Eder JP, Kantoff PW, Roper K et al. A Phase I trial of a recombinant vaccinia virus expressing prostate-specific antigen in advanced prostate cancer. Clin. Cancer Res.6, 1632–1638 (2000).
  • Zhang Q, Yu YA, Wang E et al. Eradication of solid human breast tumors in nude mice with an intravenously injected light-emitting oncolytic vaccinia virus. Cancer Res.67, 10038–10046 (2007).
  • Kaufman HL, Taback B, Sherman W et al. Phase II trial of Modified Vaccinia Ankara (MVA) virus expressing 5T4 and high dose interleukin-2 (IL-2) in patients with metastatic renal cell carcinoma. J. Transl. Med.7, 2 (2009).
  • Harrop R, Connolly N, Redchenko I et al. Vaccination of colorectal cancer patients with modified vaccinia Ankara delivering the tumor antigen 5T4 (TroVax) induces immune responses which correlate with disease control: a Phase I/II trial. Clin. Cancer Res.12, 3416–3424 (2006).
  • Reddy PS, Burroughs KD, Hales LM et al. Seneca Valley virus, a systemically deliverable oncolytic picornavirus, and the treatment of neuroendocrine cancers. J. Natl Cancer Inst.99, 1623–1633 (2007).
  • Csatary LK, Eckhardt S, Bukosza I et al. Attenuated veterinary virus vaccine for the treatment of cancer. Cancer Detect. Prev.17, 619–627 (1993).
  • Csatary LK, Gosztonyi G, Szeberenyi J et al. MTH-68/H oncolytic viral treatment in human high-grade gliomas. J. Neurooncol.67, 83–93 (2004).
  • Freeman AI, Zakay-Rones Z, Gomori JM et al. Phase I/II trial of intravenous NDV-HUJ oncolytic virus in recurrent glioblastoma multiforme. Mol. Ther.13, 221–228 (2006).
  • Hotte SJ, Lorence RM, Hirte HW et al. An optimized clinical regimen for the oncolytic virus PV701. Clin. Cancer Res.13, 977–985 (2007).
  • Laurie SA, Bell JC, Atkins HL et al. A Phase 1 clinical study of intravenous administration of PV701, an oncolytic virus, using two-step desensitization. Clin. Cancer Res.12, 2555–2562 (2006).
  • Lorence RM, Roberts MS, O’Neil JD et al. Phase 1 clinical experience using intravenous administration of PV701, an oncolytic Newcastle disease virus. Curr. Cancer Drug Targets7, 157–167 (2007).
  • Pecora AL, Rizvi N, Cohen GI et al. Phase I trial of intravenous administration of PV701, an oncolytic virus, in patients with advanced solid cancers. J. Clin. Oncol.20, 2251–2266 (2002).
  • Galanis E, Hartmann LC, Cliby WA et al. Phase I trial of intraperitoneal administration of an oncolytic measles virus strain engineered to express carcinoembryonic antigen for recurrent ovarian cancer. Cancer Res.70, 875–882 (2010).
  • Heinzerling L, Kunzi V, Oberholzer PA, Kundig T, Naim H, Dummer R. Oncolytic measles virus in cutaneous T-cell lymphomas mounts antitumor immune responses in vivo and targets interferon-resistant tumor cells. Blood106, 2287–2294 (2005).
  • Oncolytics Biotech releases REOLYSIN Phase I clinical trial results. Expert Rev. Anti Cancer Ther.2, 139 (2002).
  • Asada T. Treatment of human cancer with mumps virus. Cancer34, 1907–1928 (1974).
  • Okuno Y, Asada T, Yamanishi K et al. Studies on the use of mumps virus for treatment of human cancer. Biken J.21, 37–49 (1978).
  • Shimizu Y, Hasumi K, Okudaira Y, Yamanishi K, Takahashi M. Immunotherapy of advanced gynecologic cancer patients utilizing mumps virus. Cancer Detect. Prev.12, 487–495 (1988).
  • Sato M, Urade M, Sakuda M et al. Attenuated mumps virus therapy of carcinoma of the maxillary sinus. Int. J. Oral Surg.8, 205–211 (1979).
  • Iwasaki M, Takeda M, Shirogane Y et al. The matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein. J. Virol.83, 10374–10383 (2009).
  • Lamb R, Parks GD. Paramyxoviridae: the viruses and their replication. In: Fields Virology. Knipe D (Ed.). Lippincott Williams & Wilkins, PA, USA, 1449–1496 (2007).
  • Radecke F, Spielhofer P, Schneider H et al. Rescue of measles viruses from cloned DNA. EMBO J.14, 5773–5784 (1995).
  • Peeters BP, de Leeuw OS, Koch G, Gielkens AL. Rescue of Newcastle disease virus from cloned cDNA: evidence that cleavability of the fusion protein is a major determinant for virulence. J. Virol.73, 5001–5009 (1999).
  • Clarke DK, Sidhu MS, Johnson JE, Udem SA. Rescue of mumps virus from cDNA. J. Virol.74, 4831–4838 (2000).
  • Reichard KW, Lorence RM, Cascino CJ et al. Newcastle disease virus selectively kills human tumor cells. J. Surg. Res.52, 448–453 (1992).
  • Esolen LM, Park SW, Hardwick JM, Griffin DE. Apoptosis as a cause of death in measles virus-infected cells. J. Virol.69, 3955–3958 (1995).
  • Myers R, Greiner S, Harvey M et al. Oncolytic activities of approved mumps and measles vaccines for therapy of ovarian cancer. Cancer Gene Ther.12, 593–599 (2005).
  • Chattopadhyay S, Marques JT, Yamashita M et al. Viral apoptosis is induced by IRF-3-mediated activation of Bax. EMBO J.29(10), 1762–1773 (2010).
  • Anderson BD, Nakamura T, Russell SJ, Peng KW. High CD46 receptor density determines preferential killing of tumor cells by oncolytic measles virus. Cancer Res.64, 4919–4926 (2004).
  • Schirrmacher V, Fournier P. Newcastle disease virus: a promising vector for viral therapy, immune therapy, and gene therapy of cancer. Methods Mol. Biol.542, 565–605 (2009).
  • Yan YF, Chen X, Zhu Y, Wu JG, Dong CY. Selective cytolysis of tumor cells by mumps virus S79. Intervirology48, 292–296 (2005).
  • Cutts FT, Markowitz LE. Successes and failures in measles control. J. Infect. Dis.170(Suppl. 1), S32–S41 (1994).
  • Griffin D. Measles virus. In: Fields Virology. Knipe D (Ed.). Lippincott Williams & Wilkins, PA, USA, 1551–1586 (2007).
  • Kaplan LJ, Daum RS, Smaron M, McCarthy CA. Severe measles in immunocompromised patients. JAMA267, 1237–1241 (1992).
  • Palumbo P, Hoyt L, Demasio K, Oleske J, Connor E. Population-based study of measles and measles immunization in human immunodeficiency virus-infected children. Pediatr. Infect. Dis. J.11, 1008–1014 (1992).
  • Angel JB, Walpita P, Lerch RA et al. Vaccine-associated measles pneumonitis in an adult with AIDS. Ann. Intern. Med.129, 104–106 (1998).
  • Permar SR, Moss WJ, Ryon JJ et al. Prolonged measles virus shedding in human immunodeficiency virus-infected children, detected by reverse transcriptase-polymerase chain reaction. J. Infect. Dis.183, 532–538 (2001).
  • American Academy of Pediatrics. Committee on Infectious Diseases and Committee on Pediatric AIDS. Measles immunization in HIV-infected children. Pediatrics103, 1057–1060 (1999).
  • Hilleman MR. Current overview of the pathogenesis and prophylaxis of measles with focus on practical implications. Vaccine20, 651–665 (2001).
  • Enders JF, Peebles TC. Propagation in tissue cultures of cytopathogenic agents from patients with measles. Proc. Soc. Exp. Biol. Med.86, 277–286 (1954).
  • Griffin DE, Pan CH. Measles: old vaccines, new vaccines. Curr. Top. Microbiol. Immunol.330, 191–212 (2009).
  • Enders G. Chapter 59. Paramyxoviruses. In: Medical Microbiology. Baron S (Ed.). The University of Texas Medical Branch at Galveston, TX, USA (1996).
  • Hviid A, Rubin S, Muhlemann K. Mumps. Lancet371, 932–944 (2008).
  • Carbone K, Rubin S. Mumps virus. In: Fields Virology. Knipe D (Ed.). Lippincott-Raven Publishers, PA, USA, 1527–1550 (2007).
  • Fullerton KE, Reef SE. Commentary: ongoing debate over the safety of the different mumps vaccine strains impacts mumps disease control. Int. J. Epidemiol.31, 983–984 (2002).
  • Alexander DJ. Newcastle Disease. Kluwer Academic, Boston, MA, USA (1988).
  • Nagai Y, Klenk HD, Rott R. Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology72, 494–508 (1976).
  • Morrison T, McQuain C, Sergel T, McGinnes L, Reitter J. The role of the amino terminus of F1 of the Newcastle disease virus fusion protein in cleavage and fusion. Virology193, 997–1000 (1993).
  • Ogasawara T, Gotoh B, Suzuki H et al. Expression of factor X and its significance for the determination of paramyxovirus tropism in the chick embryo. EMBO J.11, 467–472 (1992).
  • de Leeuw OS, Hartog L, Koch G, Peeters BP. Effect of fusion protein cleavage site mutations on virulence of Newcastle disease virus: non-virulent cleavage site mutants revert to virulence after one passage in chicken brain. J. Gen. Virol.84, 475–484 (2003).
  • Garten W, Berk W, Nagai Y, Rott R, Klenk HD. Mutational changes of the protease susceptibility of glycoprotein F of Newcastle disease virus: effects on pathogenicity. J. Gen. Virol.50, 135–147 (1980).
  • Toyoda T, Sakaguchi T, Imai K et al. Structural comparison of the cleavage-activation site of the fusion glycoprotein between virulent and avirulent strains of Newcastle disease virus. Virology158, 242–247 (1987).
  • Charan S, Mahajan VM, Agarwal LP. Newcastle disease virus antibodies in human sera. Indian J. Med. Res.73, 303–307 (1981).
  • Miller LT, Yates VJ. Reactions of human sera to avian adenoviruses and Newcastle disease virus. Avian Dis.15, 781–788 (1971).
  • Russell SJ. RNA viruses as virotherapy agents. Cancer Gene Ther.9, 961–966 (2002).
  • Nakamura T, Russell SJ. Oncolytic measles viruses for cancer therapy. Expert Opin. Biol. Ther.4, 1685–1692 (2004).
  • Naik S, Russell SJ. Engineering oncolytic viruses to exploit tumor specific defects in innate immune signaling pathways. Expert Opin. Biol. Ther.9, 1163–1176 (2009).
  • Takeuchi O, Akira S. Innate immunity to virus infection. Immunol. Rev.227, 75–86 (2009).
  • Le Bon A, Tough DF. Links between innate and adaptive immunity via type I interferon. Curr. Opin. Immunol.14, 432–436 (2002).
  • Darnell JE Jr, Kerr IM, Stark GR. Jak–STAT pathways and transcriptional activation in response to IFNs and other extracellular signaling proteins. Science264, 1415–1421 (1994).
  • Haller O, Kochs G. Interferon-induced mx proteins: dynamin-like GTPases with antiviral activity. Traffic3, 710–717 (2002).
  • Rebouillat D, Hovanessian AG. The human 2´,5´-oligoadenylate synthetase family: interferon-induced proteins with unique enzymatic properties. J. Interferon Cytokine Res.19, 295–308 (1999).
  • Proud CG. PKR: a new name and new roles. Trends Biochem. Sci.20, 241–246 (1995).
  • McCormack SJ, Thomis DC, Samuel CE. Mechanism of interferon action: identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2α protein kinase. Virology188, 47–56 (1992).
  • Samuel CE. Mechanism of interferon action: phosphorylation of protein synthesis initiation factor eIF-2 in interferon-treated human cells by a ribosome-associated kinase processing site specificity similar to hemin-regulated rabbit reticulocyte kinase. Proc. Natl Acad. Sci. USA76, 600–604 (1979).
  • Toth AM, Zhang P, Das S, George CX, Samuel CE. Interferon action and the double-stranded RNA-dependent enzymes ADAR1 adenosine deaminase and PKR protein kinase. Prog. Nucleic Acid Res. Mol. Biol.81, 369–434 (2006).
  • McAllister CS, Toth AM, Zhang P, Devaux P, Cattaneo R, Samuel CE. Mechanisms of protein kinase PKR-mediated amplification of β interferon induction by C protein-deficient measles virus. J. Virol.84, 380–386 (2010).
  • Clemens MJ, Elia A. The double-stranded RNA-dependent protein kinase PKR: structure and function. J. Interferon Cytokine Res.17, 503–524 (1997).
  • Clemens MJ. PKR – a protein kinase regulated by double-stranded RNA. Int. J. Biochem. Cell Biol.29, 945–949 (1997).
  • Balachandran S, Kim CN, Yeh WC, Mak TW, Bhalla K, Barber GN. Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signaling. EMBO J.17, 6888–6902 (1998).
  • Takaoka A, Hayakawa S, Yanai H et al. Integration of interferon-α/β signalling to p53 responses in tumour suppression and antiviral defence. Nature424, 516–523 (2003).
  • Chen Q, Gong B, Mahmoud-Ahmed AS et al. Apo2L/TRAIL and Bcl-2-related proteins regulate type I interferon-induced apoptosis in multiple myeloma. Blood98, 2183–2192 (2001).
  • Colamonici OR, Domanski P, Platanias LC, Diaz MO. Correlation between interferon (IFN) α resistance and deletion of the IFN α/β genes in acute leukemia cell lines suggests selection against the IFN system. Blood80, 744–749 (1992).
  • Xu B, Grander D, Sangfelt O, Einhorn S. Primary leukemia cells resistant to α-interferon in vitro are defective in the activation of the DNA-binding factor interferon-stimulated gene factor 3. Blood84, 1942–1949 (1994).
  • Abril E, Mendez RE, Garcia A et al. Characterization of a gastric tumor cell line defective in MHC class I inducibility by both α- and γ-interferon. Tissue Antigens47, 391–398 (1996).
  • Sun WH, Pabon C, Alsayed Y et al. Interferon-α resistance in a cutaneous T-cell lymphoma cell line is associated with lack of STAT1 expression. Blood91, 570–576 (1998).
  • Whibley C, Pharoah PD, Hollstein M. p53 polymorphisms: cancer implications. Nat. Rev. Cancer9, 95–107 (2009).
  • Fontana JM, Bankamp B, Rota PA Inhibition of interferon induction and signaling by paramyxoviruses. Immunol. Rev.225, 46–67 (2008).
  • Childs K, Stock N, Ross C et al. MDA-5, but not RIG-I, is a common target for paramyxovirus V proteins. Virology359, 190–200 (2007).
  • Nakatsu Y, Takeda M, Ohno S, Shirogane Y, Iwasaki M, Yanagi Y. Measles virus circumvents the host interferon response by different actions of the C and V proteins. J. Virol.82, 8296–8306 (2008).
  • Pfaller CK, Conzelmann KK. Measles virus V protein is a decoy substrate for IκB kinase α and prevents Toll-like receptor 7/9-mediated interferon induction. J. Virol.82, 12365–12373 (2008).
  • Huang Z, Krishnamurthy S, Panda A, Samal SK. Newcastle disease virus V protein is associated with viral pathogenesis and functions as an a interferon antagonist. J. Virol.77, 8676–8685 (2003).
  • Palosaari H, Parisien JP, Rodriguez JJ, Ulane CM, Horvath CM. STAT protein interference and suppression of cytokine signal transduction by measles virus V protein. J. Virol.77, 7635–7644 (2003).
  • Ramachandran A, Parisien JP, Horvath CM. STAT2 is a primary target for measles virus V protein-mediated α/β interferon signaling inhibition. J. Virol.82, 8330–8338 (2008).
  • Randall RE, Goodbourn S. Interferons and viruses: an interplay between induction, signalling, antiviral responses and virus countermeasures. J. Gen. Virol.89, 1–47 (2008).
  • Yokota S, Saito H, Kubota T, Yokosawa N, Amano K, Fujii N. Measles virus suppresses interferon-α signaling pathway: suppression of Jak1 phosphorylation and association of viral accessory proteins, C and V, with interferon-α receptor complex. Virology306, 135–146 (2003).
  • Cruz CD, Palosaari H, Parisien JP et al. Measles virus V protein inhibits p53 family member p73. J. Virol.80, 5644–5650 (2006).
  • Toth AM, Devaux P, Cattaneo R, Samuel CE. Protein kinase PKR mediates the apoptosis induction and growth restriction phenotypes of C protein-deficient measles virus. J. Virol.83, 961–968 (2009).
  • Fournier P, Zeng J, Schirrmacher V. Two ways to induce innate immune responses in human PBMCs: paracrine stimulation of IFN-α responses by viral protein or dsRNA. Int. J. Oncol.23, 673–680 (2003).
  • Puri M, Lemon K, Duprex WP, Rima BK, Horvath CM. A point mutation, E95D, in the mumps virus V protein disengages STAT3 targeting from STAT1 targeting. J. Virol.83, 6347–6356 (2009).
  • Ohno S, Ono N, Takeda M, Takeuchi K, Yanagi Y. Dissection of measles virus V protein in relation to its ability to block α/β interferon signal transduction. J. Gen. Virol.85, 2991–2999 (2004).
  • Haralambieva I, Iankov I, Hasegawa K, Harvey M, Russell SJ, Peng KW. Engineering oncolytic measles virus to circumvent the intracellular innate immune response. Mol. Ther.15, 588–597 (2007).
  • Meng X, Nakamura T, Okazaki T et al. Enhanced antitumor effects of an engineered measles virus Edmonston strain expressing the wild-type N, P, L genes on human renal cell carcinoma. Mol. Ther.18, 544–551 (2010).
  • Tenoever BR, Servant MJ, Grandvaux N, Lin R, Hiscott J. Recognition of the measles virus nucleocapsid as a mechanism of IRF-3 activation. J. Virol.76, 3659–3669 (2002).
  • Takeda M, Ohno S, Tahara M et al. Measles viruses possessing the polymerase protein genes of the Edmonston vaccine strain exhibit attenuated gene expression and growth in cultured cells and SLAM knock-in mice. J. Virol.82, 11979–11984 (2008).
  • Peng KW, Frenzke M, Myers R et al. Biodistribution of oncolytic measles virus after intraperitoneal administration into IFNAR-CD46Ge transgenic mice. Hum. Gene Ther.14, 1565–1577 (2003).
  • Hale BG, Randall RE, Ortin J, Jackson D. The multifunctional NS1 protein of influenza A viruses. J. Gen. Virol.89, 2359–2376 (2008).
  • Mibayashi M, Martinez-Sobrido L, Loo YM et al. Inhibition of retinoic acid-inducible gene I-mediated induction of β interferon by the NS1 protein of influenza A virus. J. Virol.81, 514–524 (2007).
  • Wang X, Li M, Zheng H et al. Influenza A virus NS1 protein prevents activation of NF-κB and induction of α/β interferon. J. Virol.74, 11566–11573 (2000).
  • Zamarin D, Martinez-Sobrido L, Kelly K et al. Enhancement of oncolytic properties of recombinant newcastle disease virus through antagonism of cellular innate immune responses. Mol. Ther.17, 697–706 (2009).
  • Krishnamurthy S, Takimoto T, Scroggs RA, Portner A. Differentially regulated interferon response determines the outcome of Newcastle disease virus infection in normal and tumor cell lines. J. Virol.80, 5145–5155 (2006).
  • Fiola C, Peeters B, Fournier P, Arnold A, Bucur M, Schirrmacher V. Tumor selective replication of Newcastle disease virus: association with defects of tumor cells in antiviral defence. Int. J. Cancer119, 328–338 (2006).
  • Park MS, Garcia-Sastre A, Cros JF, Basler CF, Palese P. Newcastle disease virus V protein is a determinant of host range restriction. J. Virol.77, 9522–9532 (2003).
  • Prestwich RJ, Harrington KJ, Pandha HS, Vile RG, Melcher AA, Errington F. Oncolytic viruses: a novel form of immunotherapy. Expert Rev. Anti Cancer Ther.8, 1581–1588 (2008).
  • Matzinger P. Tolerance, danger, and the extended family. Annu. Rev. Immunol.12, 991–1045 (1994).
  • Gallucci S, Matzinger P. Danger signals: SOS to the immune system. Curr. Opin. Immunol.13, 114–119 (2001).
  • Lokuta MA, Maher J, Noe KH, Pitha PM, Shin ML, Shin HS. Mechanisms of murine RANTES chemokine gene induction by Newcastle disease virus. J. Biol. Chem.271, 13731–13738 (1996).
  • Zeng J, Fournier P, Schirrmacher V. Induction of interferon-α and tumor necrosis factor-related apoptosis-inducing ligand in human blood mononuclear cells by hemagglutinin–neuraminidase but not F protein of Newcastle disease virus. Virology297, 19–30 (2002).
  • Washburn B, Schirrmacher V. Human tumor cell infection by Newcastle Disease Virus leads to upregulation of HLA and cell adhesion molecules and to induction of interferons, chemokines and finally apoptosis. Int. J. Oncol.21, 85–93 (2002).
  • Bai L, Koopmann J, Fiola C, Fournier P, Schirrmacher V. Dendritic cells pulsed with viral oncolysates potently stimulate autologous T cells from cancer patients. Int. J. Oncol.21, 685–694 (2002).
  • Rogge L, Barberis-Maino L, Biffi M et al. Selective expression of an interleukin-12 receptor component by human T helper 1 cells. J. Exp. Med.185, 825–831 (1997).
  • Jarahian M, Watzl C, Fournier P et al. Activation of natural killer cells by newcastle disease virus hemagglutinin–neuraminidase. J. Virol.83, 8108–8121 (2009).
  • Bai L, Beckhove P, Feuerer M et al. Cognate interactions between memory T cells and tumor antigen-presenting dendritic cells from bone marrow of breast cancer patients: bidirectional cell stimulation, survival and antitumor activity in vivo. Int. J. Cancer103, 73–83 (2003).
  • Sato K, Hida S, Takayanagi H et al. Antiviral response by natural killer cells through TRAIL gene induction by IFN-α/β. Eur. J. Immunol.31, 3138–3146 (2001).
  • Schirrmacher V, Bai L, Umansky V, Yu L, Xing Y, Qian Z. Newcastle disease virus activates macrophages for anti-tumor activity. Int. J. Oncol.16, 363–373 (2000).
  • Umansky V, Shatrov VA, Lehmann V, Schirrmacher V. Induction of NO synthesis in macrophages by Newcastle disease virus is associated with activation of nuclear factor-κ B. Int. Immunol.8, 491–498 (1996).
  • Washburn B, Weigand MA, Grosse-Wilde A et al. TNF-related apoptosis-inducing ligand mediates tumoricidal activity of human monocytes stimulated by Newcastle disease virus. J. Immunol.170, 1814–1821 (2003).
  • Ertel C, Millar NS, Emmerson PT, Schirrmacher V, von Hoegen P. Viral hemagglutinin augments peptide-specific cytotoxic T cell responses. Eur. J. Immunol.23, 2592–2596 (1993).
  • Karcher J, Dyckhoff G, Beckhove P et al. Antitumor vaccination in patients with head and neck squamous cell carcinomas with autologous virus-modified tumor cells. Cancer Res.64, 8057–8061 (2004).
  • Liang W, Wang H, Sun TM et al. Application of autologous tumor cell vaccine and NDV vaccine in treatment of tumors of digestive tract. World J. Gastroenterol.9, 495–498 (2003).
  • Schneider T, Gerhards R, Kirches E, Firsching R. Preliminary results of active specific immunization with modified tumor cell vaccine in glioblastoma multiforme. J. Neurooncol.53, 39–46 (2001).
  • Steiner HH, Bonsanto MM, Beckhove P et al. Antitumor vaccination of patients with glioblastoma multiforme: a pilot study to assess feasibility, safety, and clinical benefit. J. Clin. Oncol.22, 4272–4281 (2004).
  • Cassel WA, Murray DR. Treatment of stage II malignant melanoma patients with a Newcastle disease virus oncolysate. Nat. Immun. Cell Growth Reg.7, 351–352 (1988).
  • Batliwalla FM, Bateman BA, Serrano D et al. A 15-year follow-up of AJCC stage III malignant melanoma patients treated postsurgically with Newcastle disease virus (NDV) oncolysate and determination of alterations in the CD8 T cell repertoire. Mol. Med.4, 783–794 (1998).
  • Wallack MK, Sivanandham M, Balch CM et al. Surgical adjuvant active specific immunotherapy for patients with stage III melanoma: the final analysis of data from a Phase III, randomized, double-blind, multicenter vaccinia melanoma oncolysate trial. J. Am. Coll. Surg.187, 69–77; discussion 77–79 (1998).
  • Ockert D, Schirrmacher V, Beck N et al. Newcastle disease virus-infected intact autologous tumor cell vaccine for adjuvant active specific immunotherapy of resected colorectal carcinoma. Clin. Cancer Res.2, 21–28 (1996).
  • Schlag P, Manasterski M, Gerneth T et al. Active specific immunotherapy with Newcastle-disease-virus-modified autologous tumor cells following resection of liver metastases in colorectal cancer. First evaluation of clinical response of a Phase II-trial. Cancer Immunol. Immunother.35, 325–330 (1992).
  • Takeda M, Tahara M, Hashiguchi T et al. A human lung carcinoma cell line supports efficient measles virus growth and syncytium formation via a SLAM- and CD46-independent mechanism. J. Virol.81, 12091–12096 (2007).
  • Leonard VH, Sinn PL, Hodge G et al. Measles virus blind to its epithelial cell receptor remains virulent in rhesus monkeys but cannot cross the airway epithelium and is not shed. J. Clin. Invest.118, 2448–2458 (2008).
  • Tatsuo H, Ono N, Tanaka K, Yanagi Y. SLAM (CDw150) is a cellular receptor for measles virus. Nature406, 893–897 (2000).
  • Aversa G, Carballido J, Punnonen J et al. SLAM and its role in T cell activation and Th cell responses. Immunol. Cell Biol.75, 202–205 (1997).
  • Punnonen J, Cocks BG, Carballido JM et al. Soluble and membrane-bound forms of signaling lymphocytic activation molecule (SLAM) induce proliferation and Ig synthesis by activated human B lymphocytes. J. Exp. Med.185, 993–1004 (1997).
  • Dorig RE, Marcil A, Chopra A, Richardson CD. The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell75, 295–305 (1993).
  • Leonard VH, Hodge G, Reyes-Del Valle J, McChesney MB, Cattaneo R. Signaling lymphocytic activation molecule (SLAM, CD150)-blind measles virus is attenuated and induces strong adaptive immune responses in rhesus monkeys. J. Virol. DOI:10.1128/JVI.02304-09 (2010) (Epub ahead of print).
  • Nielsen L, Blixenkrone-Moller M, Thylstrup M, Hansen NJ, Bolt G. Adaptation of wild-type measles virus to CD46 receptor usage. Arch. Virol.146, 197–208 (2001).
  • Hsu EC, Sarangi F, Iorio C et al. A single amino acid change in the hemagglutinin protein of measles virus determines its ability to bind CD46 and reveals another receptor on marmoset B cells. J. Virol.72, 2905–2916 (1998).
  • Xie M, Tanaka K, Ono N et al. Amino acid substitutions at position 481 differently affect the ability of the measles virus hemagglutinin to induce cell fusion in monkey and marmoset cells co-expressing the fusion protein. Arch. Virol.144, 1689–1699 (1999).
  • Riley-Vargas RC, Gill DB, Kemper C, Liszewski MK, Atkinson JP. CD46, expanding beyond complement regulation. Trends Immunol.25, 496–503 (2004).
  • Seya T, Hara T, Matsumoto M, Akedo H. Quantitative analysis of membrane cofactor protein (MCP) of complement. High expression of MCP on human leukemia cell lines, which is down-regulated during cell differentiation. J. Immunol.145, 238–245 (1990).
  • Ong HT, Timm MM, Greipp PR et al. Oncolytic measles virus targets high CD46 expression on multiple myeloma cells. Exp. Hematol.34, 713–720 (2006).
  • Bjorge L, Hakulinen J, Wahlstrom T, Matre R, Meri S. Complement-regulatory proteins in ovarian malignancies. Int. J. Cancer70, 14–25 (1997).
  • Varsano S, Rashkovsky L, Shapiro H, Ophir D, Mark-Bentankur T. Human lung cancer cell lines express cell membrane complement inhibitory proteins and are extremely resistant to complement-mediated lysis; a comparison with normal human respiratory epithelium in vitro, and an insight into mechanism(s) of resistance. Clin. Exp. Immunol.113, 173–182 (1998).
  • Blok VT, Daha MR, Tijsma OM, Weissglas MG, van den Broek LJ, Gorter A. A possible role of CD46 for the protection in vivo of human renal tumor cells from complement-mediated damage. Lab. Invest.80, 335–344 (2000).
  • Simpson KL, Jones A, Norman S, Holmes CH. Expression of the complement regulatory proteins decay accelerating factor (DAF, CD55), membrane cofactor protein (MCP, CD46) and CD59 in the normal human uterine cervix and in premalignant and malignant cervical disease. Am. J. Pathol.151, 1455–1467 (1997).
  • Murray KP, Mathure S, Kaul R et al. Expression of complement regulatory proteins – CD 35, CD 46, CD 55, and CD 59 – in benign and malignant endometrial tissue. Gynecol. Oncol.76, 176–182 (2000).
  • Kinugasa N, Higashi T, Nouso K et al. Expression of membrane cofactor protein (MCP, CD46) in human liver diseases. Br. J. Cancer80, 1820–1825 (1999).
  • Juhl H, Helmig F, Baltzer K et al. Frequent expression of complement resistance factors CD46, CD55, and CD59 on gastrointestinal cancer cells limits the therapeutic potential of monoclonal antibody 17-1A. J. Surg. Oncol.64, 222–230 (1997).
  • Gorter A, Blok VT, Haasnoot WH, Ensink NG, Daha MR, Fleuren GJ. Expression of CD46, CD55, and CD59 on renal tumor cell lines and their role in preventing complement-mediated tumor cell lysis. Lab. Invest.74, 1039–1049 (1996).
  • Thorsteinsson L, O’Dowd GM, Harrington PM, Johnson PM. The complement regulatory proteins CD46 and CD59, but not CD55, are highly expressed by glandular epithelium of human breast and colorectal tumour tissues. APMIS106, 869–878 (1998).
  • Oglesby TJ, Allen CJ, Liszewski MK, White DJ, Atkinson JP. Membrane cofactor protein (CD46) protects cells from complement-mediated attack by an intrinsic mechanism. J. Exp. Med.175, 1547–1551 (1992).
  • Liszewski MK, Atkinson JP. Membrane cofactor protein. Curr. Top. Microbiol. Immunol.178, 45–60 (1992).
  • Jurianz K, Ziegler S, Garcia-Schuler H et al. Complement resistance of tumor cells: basal and induced mechanisms. Mol. Immunol.36, 929–939 (1999).
  • Grote D, Russell SJ, Cornu TI et al. Live attenuated measles virus induces regression of human lymphoma xenografts in immunodeficient mice. Blood97, 3746–3754 (2001).
  • Peng KW, TenEyck CJ, Galanis E, Kalli KR, Hartmann LC, Russell SJ. Intraperitoneal therapy of ovarian cancer using an engineered measles virus. Cancer Res.62, 4656–4662 (2002).
  • Phuong LK, Allen C, Peng KW et al. Use of a vaccine strain of measles virus genetically engineered to produce carcinoembryonic antigen as a novel therapeutic agent against glioblastoma multiforme. Cancer Res.63, 2462–2469 (2003).
  • Grote D, Cattaneo R, Fielding AK. Neutrophils contribute to the measles virus-induced antitumor effect: enhancement by granulocyte macrophage colony-stimulating factor expression. Cancer Res.63, 6463–6468 (2003).
  • Dingli D, Peng KW, Harvey ME et al. Image-guided radiovirotherapy for multiple myeloma using a recombinant measles virus expressing the thyroidal sodium iodide symporter. Blood103, 1641–1646 (2004).
  • Msaouel P, Iankov ID, Allen C et al. Noninvasive imaging and radiovirotherapy of prostate cancer using an oncolytic measles virus expressing the sodium iodide symporter. Mol. Ther.12, 2041–2048 (2009).
  • Msaouel P, Iankov ID, Allen C et al. Engineered measles virus as a novel oncolytic therapy against prostate cancer. Prostate69, 82–91 (2009).
  • Peng KW, Ahmann GJ, Pham L, Greipp PR, Cattaneo R, Russell SJ. Systemic therapy of myeloma xenografts by an attenuated measles virus. Blood98, 2002–2007 (2001).
  • Kolakofsky LR. Paramyxoviridae: the Viruses and their Replication. Lippincott Williams & Wilkins, PA, USA (2001).
  • Varki A. Sialic acids. In: Essentials of Glycobiology. Varki A (Ed.). Cold Springs Harbor Laboratory Press, NY, USA, 195–210 (1999).
  • Varki A. Glycosylation changes in cancer. In: Essentials of Glycobiology, Second Ed. Cold Springs Harbor Laboratory Press, New York, NY, USA, 537–550 (1999).
  • Varki NM, Varki A. Diversity in cell surface sialic acid presentations: implications for biology and disease. Lab. Invest.87, 851–857 (2007).
  • Puhlmann J, Puehler F, Mumberg D, Boukamp P, Beier R. Rac1 is required for oncolytic NDV replication in human cancer cells and establishes a link between tumorigenesis and sensitivity to oncolytic virus. Oncogene29, 2205–2216 (2010).
  • Lorence RM, Katubig BB, Reichard KW et al. Complete regression of human fibrosarcoma xenografts after local Newcastle disease virus therapy. Cancer Res.54, 6017–6021 (1994).
  • Reichard K, Cascino CJ, Peeples ME, Walter RJ, Reyers HM. N-myc oncogene enhances the sensitivity of neuroblastoma to killing by Newcastle disease virus. Surg. Forum603–606 (1992).
  • Santer UV, DeSantis R, Hard KJ et al. N-linked oligosaccharide changes with oncogenic transformation require sialylation of multiantennae. Eur. J. Biochem.181, 249,–260 (1989).
  • Lorence RM, Roberts MS, Groene WS, Rabin H. Replication-Competent, Oncolytic Newcastle Disease Virus for Cancer Therapy. Karger, Basel, Switzerland (2001).
  • Nakamura T, Peng KW, Harvey M et al. Rescue and propagation of fully retargeted oncolytic measles viruses. Nat. Biotechnol.23, 209–214 (2005).
  • Hasegawa K, Pham L, O’Connor MK et al. Dual therapy of ovarian cancer using measles viruses expressing carcinoembryonic antigen and sodium iodide symporter. Clin. Cancer Res.12, 1868–1875 (2006).
  • Ungerechts G, Springfeld C, Frenzke ME et al. An immunocompetent murine model for oncolysis with an armed and targeted measles virus. Mol. Ther.15, 1991–1997 (2007).
  • Paraskevakou G, Allen C, Nakamura T et al. Epidermal growth factor receptor (EGFR)-retargeted measles virus strains effectively target EGFR- or EGFRvIII expressing gliomas. Mol. Ther.15, 677–686 (2007).
  • Allen C, Vongpunsawad S, Nakamura T et al. Retargeted oncolytic measles strains entering via the EGFRvIII receptor maintain significant antitumor activity against gliomas with increased tumor specificity. Cancer Res.66, 11840–11850 (2006).
  • Ungerechts G, Springfeld C, Frenzke ME et al. Lymphoma chemovirotherapy: CD20-targeted and convertase-armed measles virus can synergize with fludarabine. Cancer Res.67, 10939–10947 (2007).
  • Nakamura T, Peng KW, Vongpunsawad S et al. Antibody-targeted cell fusion. Nat. Biotechnol.22, 331–336 (2004).
  • Liu C, Hasegawa K, Russell SJ, Sadelain M, Peng KW. Prostate-specific membrane antigen retargeted measles virotherapy for the treatment of prostate cancer. Prostate69, 1128–1141 (2009).
  • Jing Y, Tong C, Zhang J et al. Tumor and vascular targeting of a novel oncolytic measles virus retargeted against the urokinase receptor. Cancer Res.69, 1459–1468 (2009).
  • Allen C, Paraskevakou G, Iankov I et al. Interleukin-13 displaying retargeted oncolytic measles virus strains have significant activity against gliomas with improved specificity. Mol. Ther.16, 1556–1564 (2008).
  • Bian H, Fournier P, Moormann R, Peeters B, Schirrmacher V. Selective gene transfer in vitro to tumor cells via recombinant Newcastle disease virus. Cancer Gene Ther.12, 295–303 (2005).
  • Bian H, Fournier P, Peeters B, Schirrmacher V. Tumor-targeted gene transfer in vivo via recombinant Newcastle disease virus modified by a bispecific fusion protein. Int. J. Oncol.27, 377–384 (2005).
  • Bian H, Wilden H, Fournier P, Peeters B, Schirrmacher V. In vivo efficacy of systemic tumor targeting of a viral RNA vector with oncolytic properties using a bispecific adapter protein. Int. J. Oncol.29, 1359–1369 (2006).
  • Peng KW, Facteau S, Wegman T, O’Kane D, Russell SJ. Non-invasive in vivo monitoring of trackable viruses expressing soluble marker peptides. Nat. Med.8, 527–531 (2002).
  • Ura Y, Ochi Y, Hamazu M, Ishida M, Nakajima K, Watanabe T. Studies on circulating antibody against carcinoembryonic antigen (CEA) and CEA-like antigen in cancer patients. Cancer Lett.25, 283–295 (1985).
  • Dadachova E, Carrasco N. The Na/I symporter (NIS): imaging and therapeutic applications. Semin. Nucl. Med.34, 23–31 (2004).
  • Mazzaferri EL, Kloos RT. Clinical review 128, current approaches to primary therapy for papillary and follicular thyroid cancer. J. Clin. Endocrinol. Metab.86, 1447–1463 (2001).
  • Dingli D, Kemp BJ, O’Connor MK et al. Combined I-124 positron emission tomography/computed tomography imaging of NIS gene expression in animal models of stably transfected and intravenously transfected tumor. Mol. Imaging Biol.8, 16–23 (2006).
  • Carlson SK, Classic KL, Hadac EM et al.In vivo quantitation of intratumoral radioisotope uptake using micro-single photon emission computed tomography/computed tomography. Mol. Imaging Biol.8, 324–332 (2006).
  • Sharkey RM, Motta-Hennessy C, Pawlyk D, Siegel JA, Goldenberg DM. Biodistribution and radiation dose estimates for yttrium- and iodine-labeled monoclonal antibody IgG and fragments in nude mice bearing human colonic tumor xenografts. Cancer Res.50, 2330–2336 (1990).
  • Press OW, Appelbaum FR, Eary JF, Bernstein ID. Radiolabeled antibody therapy of lymphomas. Important Adv. Oncol.157–171 (1995).
  • Penheiter AR, Wegman TR, Classic KL et al. Sodium iodide symporter (NIS)-mediated radiovirotherapy for pancreatic cancer. AJR Am. J. Roentgenol.195, 341–349 (2010).
  • Li H, Peng KW, Dingli D, Kratzke RA, Russell SJ. Oncolytic measles viruses encoding interferon β and the thyroidal sodium iodide symporter gene for mesothelioma virotherapy. Cancer Gene Ther.17(8), 550–558 (2010).
  • Carlson SK, Classic KL, Hadac EM et al. Quantitative molecular imaging of viral therapy for pancreatic cancer using an engineered measles virus expressing the sodium-iodide symporter reporter gene. AJR Am. J. Roentgenol.192, 279–287 (2009).
  • Blechacz B, Splinter PL, Greiner S et al. Engineered measles virus as a novel oncolytic viral therapy system for hepatocellular carcinoma. Hepatology44, 1465–1477 (2006).
  • Heel KA, Hall JC. Peritoneal defences and peritoneum-associated lymphoid tissue. Br. J. Surg.83, 1031–1036 (1996).
  • Fisher K. Striking out at disseminated metastases: the systemic delivery of oncolytic viruses. Curr. Opin. Mol. Ther.8, 301–313 (2006).
  • Douglas JT, Kim M, Sumerel LA, Carey DE, Curiel DT. Efficient oncolysis by a replicating adenovirus (ad) in vivo is critically dependent on tumor expression of primary ad receptors. Cancer Res.61, 813–817 (2001).
  • Jain RK. Delivery of molecular medicine to solid tumors: lessons from in vivo imaging of gene expression and function. J. Control. Release74, 7–25 (2001).
  • Yun CO. Overcoming the extracellular matrix barrier to improve intratumoral spread and therapeutic potential of oncolytic virotherapy. Curr. Opin. Mol. Ther.10, 356–361 (2008).
  • Sauthoff H, Hu J, Maca C et al. Intratumoral spread of wild-type adenovirus is limited after local injection of human xenograft tumors: virus persists and spreads systemically at late time points. Hum. Gene Ther.14, 425–433 (2003).
  • Emadi A, Jones RJ, Brodsky RA. Cyclophosphamide and cancer: golden anniversary. Nat. Rev. Clin. Oncol.6, 638–647 (2009).
  • Chen TL, Kennedy MJ, Anderson LW et al. Nonlinear pharmacokinetics of cyclophosphamide and 4-hydroxycyclophosphamide/aldophosphamide in patients with metastatic breast cancer receiving high-dose chemotherapy followed by autologous bone marrow transplantation. Drug Metab. Dispos.25, 544–551 (1997).
  • Sladek NE, Kollander R, Sreerama L, Kiang DT. Cellular levels of aldehyde dehydrogenases (ALDH1A1 and ALDH3A1) as predictors of therapeutic responses to cyclophosphamide-based chemotherapy of breast cancer: a retrospective study. Rational individualization of oxazaphosphorine-based cancer chemotherapeutic regimens. Cancer Chemother. Pharmacol.49, 309–321 (2002).
  • Gordon MY, Goldman JM, Gordon-Smith EC. 4-hydroperoxycyclophosphamide inhibits proliferation by human granulocyte-macrophage colony-forming cells (GM-CFC) but spares more primitive progenitor cells. Leuk. Res.9, 1017–1021 (1985).
  • Jones RJ, Barber JP, Vala MS et al. Assessment of aldehyde dehydrogenase in viable cells. Blood85, 2742–2746 (1995).
  • Sharkis SJ, Santos GW, Colvin M. Elimination of acute myelogenous leukemic cells from marrow and tumor suspensions in the rat with 4-hydroperoxycyclophosphamide. Blood55, 521–523 (1980).
  • Russell SJ, Peng KW. Measles virus for cancer therapy. Curr. Top. Microbiol. Immunol.330, 213–241 (2009).
  • Aisenberg AC, Davis C. The thymus and recovery from cyclophosphamide-induced tolerance to sheep erythrocytes. J. Exp. Med.128, 35–46 (1968).
  • Myers RM, Greiner SM, Harvey ME et al. Preclinical pharmacology and toxicology of intravenous MV-NIS, an oncolytic measles virus administered with or without cyclophosphamide. Clin. Pharmacol. Ther.82, 700–710 (2007).
  • Russell SJ, Peng KW. The utility of cells as vehicles for oncolytic virus therapies. Curr. Opin. Mol. Ther.10, 380–386 (2008).
  • Willmon C, Harrington K, Kottke T, Prestwich R, Melcher A, Vile R. Cell carriers for oncolytic viruses: Fed Ex for cancer therapy. Mol. Ther.17, 1667–1676 (2009).
  • Munguia A, Ota T, Miest T, Russell SJ. Cell carriers to deliver oncolytic viruses to sites of myeloma tumor growth. Gene Ther.15, 797–806 (2008).
  • Liu C, Russell SJ, Peng KW. Systemic therapy of disseminated myeloma in passively immunized mice using measles virus-infected cell carriers. Mol. Ther.18(6), 1155–1164 (2010).
  • Peng KW, Dogan A, Vrana J et al. Tumor-associated macrophages infiltrate plasmacytomas and can serve as cell carriers for oncolytic measles virotherapy of disseminated myeloma. Am. J. Hematol.84, 401–407 (2009).
  • Zhu YD, Heath J, Collins J et al. Experimental measles. II. Infection and immunity in the rhesus macaque. Virology233, 85–92 (1997).
  • Helin E, Salmi AA, Vanharanta R, Vainionpaa R. Measles virus replication in cells of myelomonocytic lineage is dependent on cellular differentiation stage. Virology253, 35–42 (1999).
  • Esolen LM, Ward BJ, Moench TR, Griffin DE. Infection of monocytes during measles. J. Infect. Dis.168, 47–52 (1993).
  • Gresser I, Chany C. Isolation of measles virus from the washed leucocytic fraction of blood. Proc. Soc. Exp. Biol. Med.113, 695–698 (1963).
  • Karp CL, Wysocka M, Wahl LM et al. Mechanism of suppression of cell-mediated immunity by measles virus. Science273, 228–231 (1996).
  • Nakayama T, Mori T, Yamaguchi S et al. Detection of measles virus genome directly from clinical samples by reverse transcriptase-polymerase chain reaction and genetic variability. Virus Res.35, 1–16 (1995).
  • Roscic-Mrkic B, Schwendener RA, Odermatt B et al. Roles of macrophages in measles virus infection of genetically modified mice. J. Virol.75, 3343–3351 (2001).
  • Salonen R, Ilonen J, Salmi A. Measles virus infection of unstimulated blood mononuclear cells in vitro: antigen expression and virus production preferentially in monocytes. Clin. Exp. Immunol.71, 224–228 (1988).
  • Forthal DN, Aarnaes S, Blanding J, de la Maza L, Tilles JG. Degree and length of viremia in adults with measles. J. Infect. Dis.166, 421–424 (1992).
  • Sakaguchi M, Yoshikawa Y, Yamanouchi K, Sata T, Nagashima K, Takeda K. Growth of measles virus in epithelial and lymphoid tissues of cynomolgus monkeys. Microbiol. Immunol.30, 1067–1073 (1986).
  • Mrkic B, Odermatt B, Klein MA, Billeter MA, Pavlovic J, Cattaneo R. Lymphatic dissemination and comparative pathology of recombinant measles viruses in genetically modified mice. J. Virol.74, 1364–1372 (2000).
  • Mrkic B, Pavlovic J, Rulicke T et al. Measles virus spread and pathogenesis in genetically modified mice. J. Virol.72, 7420–7427 (1998).
  • Kemper C, Leung M, Stephensen CB et al. Membrane cofactor protein (MCP; CD46) expression in transgenic mice. Clin. Exp. Immunol.124, 180–189 (2001).
  • Iankov ID, Blechacz B, Liu C et al. Infected cell carriers: a new strategy for systemic delivery of oncolytic measles viruses in cancer virotherapy. Mol. Ther.15, 114–122 (2007).
  • Ong HT, Hasegawa K, Dietz AB, Russell SJ, Peng KW. Evaluation of T cells as carriers for systemic measles virotherapy in the presence of antiviral antibodies. Gene Ther.14, 324–333 (2007).
  • Mader EK, Maeyama Y, Lin Y et al. Mesenchymal stem cell carriers protect oncolytic measles viruses from antibody neutralization in an orthotopic ovarian cancer therapy model. Clin. Cancer Res.15, 7246–7255 (2009).
  • Pollard JW. Tumour-educated macrophages promote tumour progression and metastasis. Nat. Rev. Cancer4, 71–78 (2004).
  • Kidd S, Spaeth E, Klopp A, Andreeff M, Hall B, Marini FC. The (in) auspicious role of mesenchymal stromal cells in cancer: be it friend or foe. Cytotherapy10, 657–667 (2008).
  • Giordano A, Galderisi U, Marino IR. From the laboratory bench to the patient’s bedside: an update on clinical trials with mesenchymal stem cells. J. Cell Physiol.211, 27–35 (2007).
  • Inai T, Mancuso M, Hashizume H et al. Inhibition of vascular endothelial growth factor (VEGF) signaling in cancer causes loss of endothelial fenestrations, regression of tumor vessels, and appearance of basement membrane ghosts. Am. J. Pathol.165, 35–52 (2004).
  • Hobbs SK, Monsky WL, Yuan F et al. Regulation of transport pathways in tumor vessels: role of tumor type and microenvironment. Proc. Natl Acad. Sci. USA95, 4607–4612 (1998).
  • Baluk P, Hashizume H, McDonald DM. Cellular abnormalities of blood vessels as targets in cancer. Curr. Opin. Genet. Dev.15, 102–111 (2005).
  • Maeda H, Wu J, Sawa T, Matsumura Y, Hori K. Tumor vascular permeability and the EPR effect in macromolecular therapeutics: a review. J. Control. Release65, 271–284 (2000).
  • Russell SJ, Peng KW. Viruses as anticancer drugs. Trends Pharmacol. Sci.28, 326–333 (2007).
  • Ong HT, Trejo TR, Pham LD, Oberg AL, Russell SJ, Peng KW. Intravascularly administered RGD-displaying measles viruses bind to and infect neovessel endothelial cells in vivo. Mol. Ther.17, 1012–1021 (2009).
  • Tucker GC. Integrins: molecular targets in cancer therapy. Curr. Oncol. Rep.8, 96–103 (2006).
  • Jin H, Varner J. Integrins: roles in cancer development and as treatment targets. Br. J. Cancer90, 561–565 (2004).
  • Hallak LK, Merchan JR, Storgard CM, Loftus JC, Russell SJ. Targeted measles virus vector displaying echistatin infects endothelial cells via α(v)β3 and leads to tumor regression. Cancer Res.65, 5292–5300 (2005).
  • Vigil A, Park MS, Martinez O et al. Use of reverse genetics to enhance the oncolytic properties of Newcastle disease virus. Cancer Res.67, 8285–8292 (2007).
  • Li J, Melanson VR, Mirza AM, Iorio RM. Decreased dependence on receptor recognition for the fusion promotion activity of L289A-mutated newcastle disease virus fusion protein correlates with a monoclonal antibody-detected conformational change. J. Virol.79, 1180–1190 (2005).
  • Altomonte J, Marozin S, Schmid RM, Ebert O. Engineered newcastle disease virus as an improved oncolytic agent against hepatocellular carcinoma. Mol. Ther.18, 275–284 (2009).
  • Zamarin D, Vigil A, Kelly K, Garcia-Sastre A, Fong Y. Genetically engineered Newcastle disease virus for malignant melanoma therapy. Gene Ther.16, 796–804 (2009).
  • Sule NS, Nerurkar RP, Kamath S. Interleukin-2 as a therapeutic agent. J. Assoc. Physicians India49, 897–900 (2001).
  • Boyman O, Surh CD, Sprent J. Potential use of IL-2/anti-IL-2 antibody immune complexes for the treatment of cancer and autoimmune disease. Expert Opin. Biol. Ther.6, 1323–1331 (2006).
  • Jin P, Wang E, Provenzano M, Stroncek D, Marincola FM. Gene expression signatures of interleukin-2 in vivo and in vitro and their relation to anticancer therapy. Crit. Rev. Immunol.27, 437–448 (2007).
  • Parker WB, Allan PW, Shaddix SC et al. Metabolism and metabolic actions of 6-methylpurine and 2-fluoroadenine in human cells. Biochem. Pharmacol.55, 1673–1681 (1998).
  • Breitbach CJ, Paterson JM, Lemay CG et al. Targeted inflammation during oncolytic virus therapy severely compromises tumor blood flow. Mol. Ther.15, 1686–1693 (2007).
  • Morikawa K, Kamegaya S, Yamazaki M, Mizuno D. Hydrogen peroxide as a tumoricidal mediator of murine polymorphonuclear leukocytes induced by a linear β-1,3-D-glucan and some other immunomodulators. Cancer Res.45, 3482–3486 (1985).
  • Pericle F, Kirken RA, Epling-Burnette PK, Blanchard DK, Djeu JY. Direct killing of interleukin-2-transfected tumor cells by human neutrophils. Int. J. Cancer66, 367–373 (1996).
  • Learn DB, Thomas EL. Inhibition of tumor cell glutamine uptake by isolated neutrophils. J. Clin. Invest.82, 789–796 (1988).
  • Prados MD, Levin V. Biology and treatment of malignant glioma. Semin. Oncol.27, 1–10 (2000).
  • Wong ET, Hess KR, Gleason MJ et al. Outcomes and prognostic factors in recurrent glioma patients enrolled onto Phase II clinical trials. J. Clin. Oncol.17, 2572–2578 (1999).
  • Msaouel P, Dispenzieri A, Galanis E. Clinical testing of engineered oncolytic measles virus strains in the treatment of cancer: an overview. Curr. Opin. Mol. Ther.11, 43–53 (2009).

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