Surface plasmon resonance for vaccine design and efficacy studies: recent applications and future trends

References

• Handbook of Surface Plasmon Resonance. Schasfoort RBM, Tudos AJ (Eds). The Royal Society of Chemistry, London, UK (2008).
   Google Scholar
• World Health Organization. AIDS epidemic update: Joint United Nations Programme on HIV/AIDS (UNAIDS) and World Health Organization (WHO). WHO, Geneva, Switzerland (2009).
   Google Scholar
• Rich RL, Myszka DG. Spying on HIV with SPR. Trends Microbiol.11(3), 124–133 (2003).
   PubMed Web of Science ®Google Scholar
• Sharma VA, Kan E, Sun Y et al. Structural characteristics correlate with immune responses induced by HIV envelope glycoprotein vaccines. Virology352(1), 131–144 (2006).
   PubMedGoogle Scholar
• Zolla-Pazner S. Identifying epitopes of HIV-1 that induce protective antibodies. Nat. Rev. Immunol.4(3), 199–210 (2004).
   PubMed Web of Science ®Google Scholar
• McBurney SP, Ross TM. Viral sequence diversity: challenges for AIDS vaccine designs. Expert Rev. Vaccines7(9), 1405–1417 (2008).
   PubMed Web of Science ®Google Scholar
• Kwong PD, Doyle ML, Casper DJ et al. HIV-1 evades antibody-mediated neutralization through conformational masking of receptor-binding sites. Nature420(6916), 678–682 (2002).
   PubMed Web of Science ®Google Scholar
• Haynes BF, Montefiori DC. Aiming to induce broadly reactive neutralizing antibody responses with HIV-1 vaccine candidates. Expert Rev. Vaccines5(4), 579–595 (2006).
   PubMedGoogle Scholar
• Overbaugh J, Rudensey LM. Alterations in potential sites for glycosylation predominate during evolution of the simian immunodeficiency virus envelope gene in macaques. J. Virol.66(10), 5937–5948 (1992).
   PubMedGoogle Scholar
• Wyatt R, Sodroski J. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science280(5371), 1884–1888 (1998).
   PubMed Web of Science ®Google Scholar
• Shan M, Klasse PJ, Banerjee K et al. HIV-1 gp120 mannoses induce immunosuppressive responses from dendritic cells. PLoS Pathog.3(11), e169 (2007).
   PubMed Web of Science ®Google Scholar
• Frey G, Peng H, Rits-Volloch S, Morelli M, Cheng Y, Chen B. A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc. Natl Acad. Sci. USA105(10), 3739–3744 (2008).
   PubMedGoogle Scholar
• Gorny MK, Conley AJ, Karwowska S et al. Neutralization of diverse human immunodeficiency virus type 1 variants by an anti-V3 human monoclonal antibody. J. Virol.66(12), 7538–7542 (1992).
   PubMed Web of Science ®Google Scholar
• Conley AJ, Gorny MK, Kessler JA 2nd et al. Neutralization of primary human immunodeficiency virus type 1 isolates by the broadly reactive anti-V3 monoclonal antibody, 447-52D. J. Virol.68(11), 6994–7000 (1994).
   PubMed Web of Science ®Google Scholar
• Gorny MK, Williams C, Volsky B et al. Human monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus type 1 primary isolates from various clades. J. Virol.76(18), 9035–9045 (2002).
   PubMed Web of Science ®Google Scholar
• Suphaphiphat P, Thitithanyanont A, Paca-Uccaralertkun S, Essex M, Lee TH. Effect of amino acid substitution of the V3 and bridging sheet residues in human immunodeficiency virus type 1 subtype C gp120 on CCR5 utilization. J. Virol.77(6), 3832–3837 (2003).
   PubMedGoogle Scholar
• Haynes BF, Ma B, Montefiori DC et al. Analysis of HIV-1 subtype B third variable region peptide motifs for induction of neutralizing antibodies against HIV-1 primary isolates. Virology345(1), 44–55 (2006).
   PubMedGoogle Scholar
• Mor A, Segal E, Mester B et al. Mimicking the structure of the V3 epitope bound to HIV-1 neutralizing antibodies. Biochemistry48(15), 3288–3303 (2009).
   PubMedGoogle Scholar
• Mester B, Manor R, Mor A et al. HIV-1 peptide vaccine candidates: selecting constrained V3 peptides with highest affinity to antibody 447-52D. Biochemistry48(33), 7867–7877 (2009).
   PubMedGoogle Scholar
• Thali M, Moore JP, Furman C et al. Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding. J. Virol.67(7), 3978–3988 (1993).
   PubMedGoogle Scholar
• Barbas CF 3rd, Bjorling E, Chiodi F et al. Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro. Proc. Natl Acad. Sci. USA89(19), 9339–9343 (1992).
   PubMed Web of Science ®Google Scholar
• Moulard M, Phogat SK, Shu Y et al. Broadly cross-reactive HIV-1-neutralizing human monoclonal Fab selected for binding to gp120–CD4–CCR5 complexes. Proc. Natl Acad. Sci. USA99(10), 6913–6918 (2002).
   PubMed Web of Science ®Google Scholar
• Coutsinos Z, Absi Z, Henin Y, Guillet JG, Launay O. [Designing an effective AIDS vaccine: strategies and current status]. Rev. Med. Intern.29(8), 632–641 (2008).
   PubMedGoogle Scholar
• Girard MP. HIV/AIDS vaccines: heading for new vaccine approaches? Bull. Soc. Pathol. Exot.101(3), 220–226 (2008).
   PubMedGoogle Scholar
• Girard MP, Osmanov SK, Kieny MP. A review of vaccine research and development: the human immunodeficiency virus (HIV). Vaccine24(19), 4062–4081 (2006).
   PubMed Web of Science ®Google Scholar
• Burton DR, Desrosiers RC, Doms RW et al. HIV vaccine design and the neutralizing antibody problem. Nat. Immunol.5(3), 233–236 (2004).
   PubMed Web of Science ®Google Scholar
• Rits-Volloch S, Frey G, Harrison SC, Chen B. Restraining the conformation of HIV-1 gp120 by removing a flexible loop. EMBO J.25(20), 5026–5035 (2006).
   PubMedGoogle Scholar
• Zhang W, Godillot AP, Wyatt R, Sodroski J, Chaiken I. Antibody 17b binding at the coreceptor site weakens the kinetics of the interaction of envelope glycoprotein gp120 with CD4. Biochemistry40(6), 1662–1670 (2001).
   PubMed Web of Science ®Google Scholar
• Zhou T, Xu L, Dey B et al. Structural definition of a conserved neutralization epitope on HIV-1 gp120. Nature445(7129), 732–737 (2007).
   PubMed Web of Science ®Google Scholar
• Zwick MB, Parren PW, Saphire EO et al. Molecular features of the broadly neutralizing immunoglobulin G1 b12 required for recognition of human immunodeficiency virus type 1 gp120. J. Virol.77(10), 5863–5876 (2003).
   PubMed Web of Science ®Google Scholar
• Yang X, Tomov V, Kurteva S et al. Characterization of the outer domain of the gp120 glycoprotein from human immunodeficiency virus type 1. J. Virol.78(23), 12975–12986 (2004).
   PubMed Web of Science ®Google Scholar
• Arthos J, Cicala C, Steenbeke TD et al. Biochemical and biological characterization of a dodecameric CD4–Ig fusion protein: implications for therapeutic and vaccine strategies. J. Biol. Chem.277(13), 11456–11464 (2002).
   PubMed Web of Science ®Google Scholar
• Dey B, Svehla K, Xu L et al. Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced co-receptor binding site. PLoS Pathog.5(5), e1000445 (2009).
   PubMed Web of Science ®Google Scholar
• Zwick MB, Labrijn AF, Wang M et al. Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41. J. Virol.75(22), 10892–10905 (2001).
   PubMed Web of Science ®Google Scholar
• Montero M, van Houten NE, Wang X, Scott JK. The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design. Microbiol. Mol. Biol. Rev.72(1), 54–84 (2008).
   PubMed Web of Science ®Google Scholar
• Bryson S, Julien JP, Hynes RC, Pai EF. Crystallographic definition of the epitope promiscuity of the broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2F5: vaccine design implications. J. Virol.83(22), 11862–11875 (2009).
   PubMedGoogle Scholar
• Menendez A, Chow KC, Pan OC, Scott JK. Human immunodeficiency virus type 1-neutralizing monoclonal antibody 2F5 is multispecific for sequences flanking the DKW core epitope. J. Mol. Biol.338(2), 311–327 (2004).
   PubMed Web of Science ®Google Scholar
• Parker CE, Deterding LJ, Hager-Braun C et al. Fine definition of the epitope on the gp41 glycoprotein of human immunodeficiency virus type 1 for the neutralizing monoclonal antibody 2F5. J. Virol.75(22), 10906–10911 (2001).
   PubMed Web of Science ®Google Scholar
• McGaughey GB, Citron M, Danzeisen RC et al. HIV-1 vaccine development: constrained peptide immunogens show improved binding to the anti-HIV-1 gp41 mAb. Biochemistry42(11), 3214–3223 (2003).
   PubMedGoogle Scholar
• Joyce JG, Hurni WM, Bogusky MJ et al. Enhancement of α-helicity in the HIV-1 inhibitory peptide DP178 leads to an increased affinity for human monoclonal antibody 2F5 but does not elicit neutralizing responses in vitro. Implications for vaccine design. J. Biol. Chem.277(48), 45811–45820 (2002).
   PubMed Web of Science ®Google Scholar
• Coeffier E, Clement JM, Cussac V et al. Antigenicity and immunogenicity of the HIV-1 gp41 epitope ELDKWA inserted into permissive sites of the MalE protein. Vaccine19(7–8), 684–693 (2000).
   PubMed Web of Science ®Google Scholar
• Liao M, Lu Y, Xiao Y, Dierich MP, Chen Y. Induction of high level of specific antibody response to the neutralizing epitope ELDKWA on HIV-1 gp41 by peptide-vaccine. Peptides21(4), 463–468 (2000).
   PubMedGoogle Scholar
• Xiao Y, Zhao Y, Lu Y, Chen YH. Epitope-vaccine induces high levels of ELDKWA-epitope-specific neutralizing antibody. Immunol. Invest.29(1), 41–50 (2000).
   PubMed Web of Science ®Google Scholar
• Eckhart L, Raffelsberger W, Ferko B et al. Immunogenic presentation of a conserved gp41 epitope of human immunodeficiency virus type 1 on recombinant surface antigen of hepatitis B virus. J. Gen. Virol.77(9), 2001–2008 (1996).
   PubMed Web of Science ®Google Scholar
• Muster T, Guinea R, Trkola A et al. Cross-neutralizing activity against divergent human immunodeficiency virus type 1 isolates induced by the gp41 sequence ELDKWAS. J. Virol.68(6), 4031–4034 (1994).
   PubMed Web of Science ®Google Scholar
• Veiga AS, Pattenden LK, Fletcher JM, Castanho MA, Aguilar MI. Interactions of HIV-1 antibodies 2F5 and 4E10 with a gp41 epitope prebound to host and viral membrane model systems. Chembiochem.10(6), 1032–1044 (2009).
   PubMedGoogle Scholar
• Ofek G, Tang M, Sambor A et al. Structure and mechanistic analysis of the anti-human immunodeficiency virus type 1 antibody 2F5 in complex with its gp41 epitope. J. Virol.78(19), 10724–10737 (2004).
   PubMed Web of Science ®Google Scholar
• Grundner C, Mirzabekov T, Sodroski J, Wyatt R. Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins. J. Virol.76(7), 3511–3521 (2002).
   PubMed Web of Science ®Google Scholar
• Maynard JA, Lindquist NC, Sutherland JN et al. Surface plasmon resonance for high-throughput ligand screening of membrane-bound proteins. Biotechnol. J.4(11), 1542–1558 (2009).
   PubMedGoogle Scholar
• Anderluh G, Besenicar M, Kladnik A, Lakey JH, Macek P. Properties of nonfused liposomes immobilized on an L1 Biacore chip and their permeabilization by a eukaryotic pore-forming toxin. Anal. Biochem.344(1), 43–52 (2005).
   PubMedGoogle Scholar
• Kim M, Qiao Z, Yu J, Montefiori D, Reinherz EL. Immunogenicity of recombinant human immunodeficiency virus type 1-like particles expressing gp41 derivatives in a pre-fusion state. Vaccine25(27), 5102–5114 (2007).
   PubMed Web of Science ®Google Scholar
• Alam SM, Morelli M, Dennison SM et al. Role of HIV membrane in neutralization by two broadly neutralizing antibodies. Proc. Natl Acad. Sci. USA106(48), 20234–20239 (2009).
   PubMed Web of Science ®Google Scholar
• Alam SM, McAdams M, Boren D et al. The role of antibody polyspecificity and lipid reactivity in binding of broadly neutralizing anti-HIV-1 envelope human monoclonal antibodies 2F5 and 4E10 to glycoprotein 41 membrane proximal envelope epitopes. J. Immunol.178(7), 4424–4435 (2007).
   PubMed Web of Science ®Google Scholar
• Sanchez-Martinez S, Lorizate M, Katinger H, Kunert R, Nieva JL. Membrane association and epitope recognition by HIV-1 neutralizing anti-gp41 2F5 and 4E10 antibodies. AIDS Res. Hum. Retroviruses22(10), 998–1006 (2006).
   PubMed Web of Science ®Google Scholar
• Haynes BF, Fleming J, St Clair EW et al. Cardiolipin polyspecific autoreactivity in two broadly neutralizing HIV-1 antibodies. Science308(5730), 1906–1908 (2005).
   PubMed Web of Science ®Google Scholar
• Dennison SM, Stewart SM, Stempel KC, Liao HX, Haynes BF, Alam SM. Stable docking of neutralizing human immunodeficiency virus type 1 gp41 membrane-proximal external region monoclonal antibodies 2F5 and 4E10 is dependent on the membrane immersion depth of their epitope regions. J. Virol.83(19), 10211–10223 (2009).
   PubMed Web of Science ®Google Scholar
• Sun ZY, Oh KJ, Kim M et al. HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane. Immunity28(1), 52–63 (2008).
   PubMed Web of Science ®Google Scholar
• Haynes BF, Alam SM. HIV-1 hides an Achilles’ heel in virion lipids. Immunity28(1), 10–12 (2008).
   PubMed Web of Science ®Google Scholar
• Song L, Sun ZY, Coleman KE et al. Broadly neutralizing anti-HIV-1 antibodies disrupt a hinge-related function of gp41 at the membrane interface. Proc. Natl Acad. Sci. USA106(22), 9057–9062 (2009).
   PubMedGoogle Scholar
• Munoz-Barroso I, Durell S, Sakaguchi K, Appella E, Blumenthal R. Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41. J. Cell. Biol.140(2), 315–323 (1998).
   PubMed Web of Science ®Google Scholar
• Dimitrov AS, Louis JM, Bewley CA, Clore GM, Blumenthal R. Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation. Biochemistry44(37), 12471–12479 (2005).
   PubMedGoogle Scholar
• Steger HK, Root MJ. Kinetic dependence to HIV-1 entry inhibition. J. Biol. Chem.281(35), 25813–25821 (2006).
   PubMedGoogle Scholar
• Ofek G, McKee K, Yang Y et al. Relationship between antibody 2F5 neutralization of HIV-1 and hydrophobicity of its heavy chain third complementarity-determining region. J. Virol.84(6), 2955–2962 (2010).
   PubMed Web of Science ®Google Scholar
• Scherer EM, Leaman DP, Zwick MB, McMichael AJ, Burton DR. Aromatic residues at the edge of the antibody combining site facilitate viral glycoprotein recognition through membrane interactions. Proc. Natl Acad. Sci. USA107(4), 1529–1534 (2010).
   PubMedGoogle Scholar
• Wyatt R, Kwong PD, Desjardins E et al. The antigenic structure of the HIV gp120 envelope glycoprotein. Nature393(6686), 705–711 (1998).
   PubMed Web of Science ®Google Scholar
• Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ. Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. J. Biol. Chem.265(18), 10373–10382 (1990).
   PubMed Web of Science ®Google Scholar
• Scanlan CN, Pantophlet R, Wormald MR et al. The broadly neutralizing anti-human immunodeficiency virus type 1 antibody 2G12 recognizes a cluster of a1→2 mannose residues on the outer face of gp120. J. Virol.76(14), 7306–7321 (2002).
   PubMed Web of Science ®Google Scholar
• Trkola A, Purtscher M, Muster T et al. Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1. J. Virol.70(2), 1100–1108 (1996).
   PubMed Web of Science ®Google Scholar
• Burton DR, Stanfield RL, Wilson IA. Antibody vs. HIV in a clash of evolutionary titans. Proc. Natl Acad. Sci. USA102(42), 14943–14948 (2005).
   PubMed Web of Science ®Google Scholar
• Calarese DA, Scanlan CN, Zwick MB et al. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science300(5628), 2065–2071 (2003).
   PubMed Web of Science ®Google Scholar
• Kwong PD, Wilson IA. HIV-1 and influenza antibodies: seeing antigens in new ways. Nat. Immunol.10(6), 573–578 (2009).
   PubMed Web of Science ®Google Scholar
• Menendez A, Calarese DA, Stanfield RL et al. A peptide inhibitor of HIV-1 neutralizing antibody 2G12 is not a structural mimic of the natural carbohydrate epitope on gp120. FASEB J.22(5), 1380–1392 (2008).
   PubMed Web of Science ®Google Scholar
• Wang LX, Ni J, Singh S, Li H. Binding of high-mannose-type oligosaccharides and synthetic oligomannose clusters to human antibody 2G12: implications for HIV-1 vaccine design. Chem. Biol.11(1), 127–134 (2004).
   PubMed Web of Science ®Google Scholar
• Brewer CF, Bhattacharyya L. Specificity of concanavalin A binding to asparagine-linked glycopeptides. A nuclear magnetic relaxation dispersion study. J. Biol. Chem.261(16), 7306–7310 (1986).
   PubMedGoogle Scholar
• Dacheux L, Moreau A, Ataman-Onal Y, Biron F, Verrier B, Barin F. Evolutionary dynamics of the glycan shield of the human immunodeficiency virus envelope during natural infection and implications for exposure of the 2G12 epitope. J. Virol.78(22), 12625–12637 (2004).
   PubMed Web of Science ®Google Scholar
• Pashov A, MacLeod S, Saha R, Perry M, VanCott TC, Kieber-Emmons T. Concanavalin A binding to HIV envelope protein is less sensitive to mutations in glycosylation sites than monoclonal antibody 2G12. Glycobiology15(10), 994–1001 (2005).
   PubMedGoogle Scholar
• Pashov A, Canziani G, Monzavi-Karbassi B et al. Antigenic properties of peptide mimotopes of HIV-1-associated carbohydrate antigens. J. Biol. Chem.280(32), 28959–28965 (2005).
   PubMed Web of Science ®Google Scholar
• Pashov A, Canziani G, Macleod S, Plaxco J, Monzavi-Karbassi B, Kieber-Emmons T. Targeting carbohydrate antigens in HIV vaccine development. Vaccine23(17–18), 2168–2175 (2005).
   PubMedGoogle Scholar
• Pashov AD, Plaxco J, Kaveri SV, Monzavi-Karbassi B, Harn D, Kieber-Emmons T. Multiple antigenic mimotopes of HIV carbohydrate antigens: relating structure and antigenicity. J. Biol. Chem.281(40), 29675–29683 (2006).
   PubMedGoogle Scholar
• Dudkin VY, Orlova M, Geng X, Mandal M, Olson WC, Danishefsky SJ. Toward fully synthetic carbohydrate-based HIV antigen design: on the critical role of bivalency. J. Am. Chem. Soc.126(31), 9560–9562 (2004).
   PubMed Web of Science ®Google Scholar
• Krauss IJ, Joyce JG, Finnefrock AC et al. Fully synthetic carbohydrate HIV antigens designed on the logic of the 2G12 antibody. J. Am. Chem. Soc.129(36), 11042–11044 (2007).
   PubMed Web of Science ®Google Scholar
• Remarque EJ, Faber BW, Kocken CH, Thomas AW. Apical membrane antigen 1: a malaria vaccine candidate in review. Trends Parasitol.24(2), 74–84 (2008).
   PubMed Web of Science ®Google Scholar
• Richie TL, Parekh FK, Alan DTB, Lawrence RS. Malaria. In: Vaccines for Biodefense and Emerging and Neglected Diseases. Academic Press, London, UK, 1309–1364 (2009).
   Google Scholar
• Richards JS, Beeson JG. The future for blood-stage vaccines against malaria. Immunol. Cell. Biol.87(5), 377–390 (2009).
   PubMed Web of Science ®Google Scholar
• Good MF. Vaccine-induced immunity to malaria parasites and the need for novel strategies. Trends Parasitol.21(1), 29–34 (2005).
   PubMed Web of Science ®Google Scholar
• Girard MP, Reed ZH, Friede M, Kieny MP. A review of human vaccine research and development: malaria. Vaccine25(9), 1567–1580 (2007).
   PubMed Web of Science ®Google Scholar
• Plassmeyer ML, Reiter K, Shimp RL Jr et al. Structure of the Plasmodium falciparum circumsporozoite protein, a leading malaria vaccine candidate. J. Biol. Chem.284(39), 26951–26963 (2009).
   PubMed Web of Science ®Google Scholar
• Uthaipibull C, Aufiero B, Syed SE et al. Inhibitory and blocking monoclonal antibody epitopes on merozoite surface protein 1 of the malaria parasite Plasmodium falciparum. J. Mol. Biol.307(5), 1381–1394 (2001).
   PubMed Web of Science ®Google Scholar
• Harris KS, Casey JL, Coley AM et al. Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning. J. Biol. Chem.284(14), 9361–9371 (2009).
   PubMed Web of Science ®Google Scholar
• Igonet S, Vulliez-Le Normand B, Faure G et al. Cross-reactivity studies of an anti-Plasmodium vivax apical membrane antigen 1 monoclonal antibody: binding and structural characterisation. J. Mol. Biol.366(5), 1523–1537 (2007).
   PubMed Web of Science ®Google Scholar
• Henderson KA, Streltsov VA, Coley AM et al. Structure of an IgNAR–AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure15(11), 1452–1466 (2007).
   PubMed Web of Science ®Google Scholar
• Kim SH, Hwang SY, Lee YS, Choi IH, Park SG, Kho WG. Single-chain antibody fragment specific for Plasmodium vivax Duffy binding protein. Clin. Vaccine Immunol.14(6), 726–731 (2007).
   PubMedGoogle Scholar
• Bright RA, Carter DM, Crevar CJ et al. Cross-clade protective immune responses to influenza viruses with H5N1 HA and NA elicited by an influenza virus-like particle. PLoS One3(1), e1501 (2008).
   PubMed Web of Science ®Google Scholar
• Ulmer JB, Valley U, Rappuoli R. Vaccine manufacturing: challenges and solutions. Nat. Biotechnol.24(11), 1377–1383 (2006).
   PubMed Web of Science ®Google Scholar
• Nilsson CE, Abbas S, Bennemo M, Larsson A, Hamalainen MD, Frostell-Karlsson A. A novel assay for influenza virus quantification using surface plasmon resonance. Vaccine28(3), 759–766 (2010).
   PubMed Web of Science ®Google Scholar
• Mahmood K, Bright RA, Mytle N et al. H5N1 VLP vaccine induced protection in ferrets against lethal challenge with highly pathogenic H5N1 influenza viruses. Vaccine26(42), 5393–5399 (2008).
   PubMed Web of Science ®Google Scholar
• Ng AK, Zhang H, Tan K et al. Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design. FASEB J.22(10), 3638–3647 (2008).
   PubMed Web of Science ®Google Scholar
• Wang R, Song A, Levin J et al. Therapeutic potential of a fully human monoclonal antibody against influenza A virus M2 protein. Antiviral Res.80(2), 168–177 (2008).
   PubMed Web of Science ®Google Scholar
• Sui J, Hwang WC, Perez S et al. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat. Struct. Mol. Biol.16(3), 265–273 (2009).
   PubMed Web of Science ®Google Scholar
• Throsby M, van den Brink E, Jongeneelen M et al. Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells. PLoS One3(12), e3942 (2008).
   PubMed Web of Science ®Google Scholar
• Deroo S, Fischer A, Beaupain N et al. Non-immunized natural human heavy chain CDR3 repertoires allow the isolation of high affinity peptides mimicking a human influenza hemagglutinin epitope. Mol. Immunol.45(5), 1366–1373 (2008).
   PubMedGoogle Scholar
• Friguet B, Chaffotte AF, Djavadi-Ohaniance L, Goldberg ME. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods77(2), 305–319 (1985).
   PubMed Web of Science ®Google Scholar
• Tripet B, Kao DJ, Jeffers SA, Holmes KV, Hodges RS. Template-based coiled-coil antigens elicit neutralizing antibodies to the SARS-coronavirus. J. Struct. Biol.155(2), 176–194 (2006).
   PubMedGoogle Scholar
• ter Meulen J, van den Brink EN, Poon LL et al. Human monoclonal antibody combination against SARS coronavirus: synergy and coverage of escape mutants. PLoS Med.3(7), e237 (2006).
   PubMed Web of Science ®Google Scholar
• Prabakaran P, Gan J, Feng Y et al. Structure of severe acute respiratory syndrome coronavirus receptor-binding domain complexed with neutralizing antibody. J. Biol. Chem.281(23), 15829–15836 (2006).
   PubMed Web of Science ®Google Scholar
• Lee JW, Kim K, Jung SH et al. Identification of a domain containing B-cell epitopes in hepatitis C virus E2 glycoprotein by using mouse monoclonal antibodies. J. Virol.73(1), 11–18 (1999).
   PubMedGoogle Scholar
• Tzitzilonis C, Prince SM, Collins RF et al. Structural variation and immune recognition of the P1.2 subtype meningococcal antigen. Proteins62(4), 947–955 (2006).
   PubMedGoogle Scholar
• Park IH, Youn JH, Choi IH, Nahm MH, Kim SJ, Shin JS. Anti-idiotypic antibody as a potential candidate vaccine for Neisseria meningitidis serogroup B. Infect Immun.73(10), 6399–6406 (2005).
   PubMed Web of Science ®Google Scholar
• Cho WC. A future of cancer prevention and cures: highlights of the Centennial Meeting of the American Association for Cancer Research. Ann. Oncol.19(2), 205–211 (2008).
   PubMedGoogle Scholar
• Barr E, Sings HL. Prophylactic HPV vaccines: new interventions for cancer control. Vaccine26(49), 6244–6257 (2008).
   PubMedGoogle Scholar
• Deschuyteneer M, Elouahabi A, Plainchamp D et al. Molecular and structural characterization of the L1 virus-like particles that are used as vaccine antigens in Cervarix™, the AS04-adjuvanted HPV-16 and -18 cervical cancer vaccine. Hum. Vaccines6(5) (2010).
   PubMedGoogle Scholar
• Heimburg-Molinaro J, Almogren A, Morey S et al. Development, characterization, and immunotherapeutic use of peptide mimics of the Thomsen-Friedenreich carbohydrate antigen. Neoplasia11(8), 780–792 (2009).
   PubMed Web of Science ®Google Scholar
• Coelho M, Gauthier P, Pugniere M, Roquet F, Pelegrin A, Navarro-Teulon I. Isolation and characterisation of a human anti-idiotypic scFv used as a surrogate tumour antigen to elicit an anti-HER-2/neu humoral response in mice. Br. J. Cancer90(10), 2032–2041 (2004).
   PubMedGoogle Scholar
• Alvarez-Rueda N, Ladjemi MZ, Behar G et al. A llama single domain anti-idiotypic antibody mimicking HER2 as a vaccine: Immunogenicity and efficacy. Vaccine27(35), 4826–4833 (2009).
   PubMed Web of Science ®Google Scholar
• Cachia PJ, Kao DJ, Hodges RS. Synthetic peptide vaccine development: measurement of polyclonal antibody affinity and cross-reactivity using a new peptide capture and release system for surface plasmon resonance spectroscopy. J. Mol. Recognit.17(6), 540–557 (2004).
   PubMedGoogle Scholar
• Khurana S, Chearwae W, Castellino F et al. Vaccines with MF59 adjuvant expand the antibody repertoire to target protective sites of pandemic avian h5n1 influenza virus. Sci. Transl. Med.2(15), 15ra15 (2010).
   Google Scholar
• Khurana S, Suguitan AL Jr, Rivera Y et al. Antigenic fingerprinting of H5N1 avian influenza using convalescent sera and monoclonal antibodies reveals potential vaccine and diagnostic targets. PLoS Med.6(4), e1000049 (2009).
   PubMed Web of Science ®Google Scholar
• Mire-Sluis AR, Barrett YC, Devanarayan V et al. Recommendations for the design and optimization of immunoassays used in the detection of host antibodies against biotechnology products. J. Immunol. Methods289(1–2), 1–16 (2004).
   PubMed Web of Science ®Google Scholar
• Nechansky A. HAHA – nothing to laugh about. Measuring the immunogenicity (human anti-human antibody response) induced by humanized monoclonal antibodies applying ELISA and SPR technology. J. Pharm. Biomed. Anal.51(1), 252–254 (2010).
   PubMed Web of Science ®Google Scholar
• Torres M, Fernandez-Fuentes N, Fiser A, Casadevall A. Exchanging murine and human immunoglobulin constant chains affects the kinetics and thermodynamics of antigen binding and chimeric antibody autoreactivity. PLoS One2(12), e1310 (2007).
   PubMedGoogle Scholar
• Lofgren JA, Dhandapani S, Pennucci JJ et al. Comparing ELISA and surface plasmon resonance for assessing clinical immunogenicity of panitumumab. J. Immunol.178(11), 7467–7472 (2007).
   PubMed Web of Science ®Google Scholar
• Rich RL, Myszka DG. Survey of the year 2006 commercial optical biosensor literature. J. Mol. Recognit.20(5), 300–366 (2007).
   PubMedGoogle Scholar
• Rich RL, Myszka DG. Survey of the year 2005 commercial optical biosensor literature. J. Mol. Recognit.19(6), 478–534 (2006).
   PubMed Web of Science ®Google Scholar
• Rich RL, Myszka DG. Survey of the year 2003 commercial optical biosensor literature. J. Mol. Recognit.18(1), 1–39 (2005).
   PubMedGoogle Scholar
• Rich RL, Myszka DG. Survey of the year 2004 commercial optical biosensor literature. J. Mol. Recognit.18(6), 431–478 (2005).
   PubMedGoogle Scholar
• Rich RL, Myszka DG. Grading the commercial optical biosensor literature – class of 2008: ‘the mighty binders’. J. Mol. Recognit.23(1), 1–64 (2009).
   Google Scholar
• Metz B, Jiskoot W, Hennink WE, Crommelin DJ, Kersten GF. Physicochemical and immunochemical techniques predict the quality of diphtheria toxoid vaccines. Vaccine22(2), 156–167 (2003).
   PubMed Web of Science ®Google Scholar
• Metz B, Jiskoot W, Mekkes D et al. Quality control of routine, experimental and real-time aged diphtheria toxoids by in vitro analytical techniques. Vaccine25(39–40), 6863–6871 (2007).
   PubMed Web of Science ®Google Scholar
• Leenaars PP, Kersten GF, de Bruijn ML, Hendriksen CF. An in vitro approach in quality control of toxoid vaccines. Vaccine19(17–19), 2729–2733 (2001).
   PubMedGoogle Scholar
• Mandenius CF, Wang R, Alden A et al. Monitoring of influenza virus hemagglutinin in process samples using weak affinity ligands and surface plasmon resonance. Anal. Chim. Acta623(1), 66–75 (2008).
   PubMed Web of Science ®Google Scholar
• Conroy PJ, Hearty S, Leonard P, O’Kennedy RJ. Antibody production, design and use for biosensor-based applications. Semin. Cell. Dev. Biol.20(1), 10–26 (2009).
   PubMed Web of Science ®Google Scholar
• Bravman T, Bronner V, Lavie K, Notcovich A, Papalia GA, Myszka DG. Exploring ‘one-shot’ kinetics and small molecule analysis using the ProteOn XPR36 array biosensor. Anal. Biochem.358(2), 281–288 (2006).
   PubMed Web of Science ®Google Scholar
• Hosse RJ, Tay L, Hattarki MK et al. Kinetic screening of antibody–Im7 conjugates by capture on a colicin E7 DNase domain using optical biosensors. Anal. Biochem.385(2), 346–357 (2009).
   PubMedGoogle Scholar
• Safsten P, Klakamp SL, Drake AW, Karlsson R, Myszka DG. Screening antibody-antigen interactions in parallel using Biacore A100. Anal. Biochem.353(2), 181–190 (2006).
   PubMed Web of Science ®Google Scholar
• Luong JH, Male KB, Glennon JD. Biosensor technology: technology push versus market pull. Biotechnol. Adv.26(5), 492–500 (2008).
   PubMed Web of Science ®Google Scholar
• Havard J, Gillock N, Martin A, Quinn J. An automated surface plasmon resonance-based system. Am. Biotechnol. Lab.27(11), 24–25 (2009).
   Google Scholar
• Boozer C, Kim G, Cong S, Guan H, Londergan T. Looking towards label-free biomolecular interaction analysis in a high-throughput format: a review of new surface plasmon resonance technologies. Curr. Opin. Biotechnol.17(4), 400–405 (2006).
   PubMed Web of Science ®Google Scholar
• Abdiche Y, Malashock D, Pinkerton A, Pons J. Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet. Anal. Biochem.377(2), 209–217 (2008).
   PubMed Web of Science ®Google Scholar
• Abdiche YN, Malashock DS, Pinkerton A, Pons J. Exploring blocking assays using Octet, ProteOn, and Biacore biosensors. Anal. Biochem.386(2), 172–180 (2009).
   PubMed Web of Science ®Google Scholar
• Rich RL, Papalia GA, Flynn PJ et al. A global benchmark study using affinity-based biosensors. Anal. Biochem.386(2), 194–216 (2009).
   PubMed Web of Science ®Google Scholar