73
Views
7
CrossRef citations to date
0
Altmetric
Review

Bioactive molecules of Taenia solium metacestode, a causative agent of neurocysticercosis

, , , &
Pages 691-707 | Published online: 09 Jan 2014

References

  • Liu YM, Bair MJ, Chang WH, Lin SC, Chan YJ. Acute pancreatitis caused by tapeworm in the biliary tract. Am. J. Trop. Med. Hyg.73, 377–380 (2005).
  • Gilman RH, Del Brutto OH, Garcia HH, Martinez M. The Cysticercosis Working Group in Peru. Prevalence of taeniosis among patients with neurocysticercosis is related to severity of infection. Neurology55, 1062 (2000).
  • Verastegui M, Gilman RH, Garcia HH et al. Prevalence of antibodies to unique Taenia solium oncosphere antigens in taeniasis and human and porcine cysticercosis. Am. J. Trop. Med. Hyg.69, 438–444 (2003).
  • Lescano AG, Garcia HH, Gilman RH et al. Swine cysticercosis hotspots surrounding Taenia solium tapeworm carriers. Am. J. Trop. Med. Hyg.76, 376–383 (2007).
  • Lescano AG, Garcia HH, Gilman RH et al.Taenia solium cysticercosis hotspots surrounding tapeworm carriers: clustering on human seroprevalence but not on seizures. PLoS Negl. Trop. Dis.3, e371 (2009).
  • Mahanty S, Garcia HH; The Cysticercosis Working Group in Perú. Cysticercosis and neurocysticercosis as pathogens affecting the nervous system. Prog. Neurobiol.91(2), 172–184 (2010).
  • Sotelo J, Guerrero V, Rubio F. Neurocysticercosis: a new classification based on active and inactive forms: a study of 753 cases. Arch. Intern. Med.145, 442–445 (1985).
  • Del Brutto OH, Sotelo J, Roman GC. Neurocysticercosis: A Clinical Handbook. Del Brutto OH, Sotelo J, Roman GC (Eds). Swets and Zeitlinger Publishers, Lisse, The Netherlands (1998).
  • Chung JY, Bahk YY, Huh S, Kang SY, Kong Y, Cho SY. A recombinant 10-kDa protein of Taenia solium metacestodes specific to active neurocysticercosis. J. Infect. Dis.180, 1307–1315 (1999).
  • Meyer A, Dua T, Ma J, Saxena A, Birbeck G. Global disparities in the epilepsy treatment gap: a systematic review. WHO Bulletin88, 260–266 (2010).
  • Gonzalez AE, Cama V, Gilman RH et al. Prevalence and comparison of serologic assays, necropsy, and tongue examination for the diagnosis of porcine cysticercosis in Peru. Am. J. Trop. Med. Hyg.43, 94–99 (1990).
  • Onah DN, Chiejina SN. Taenia solium cysticercosis and human taeniasis in the Nsukka area of Enugu State, Nigeria. Ann. Trop. Med. Parasitol.89, 399–407 (1995).
  • Phiri IK, Ngowi H, Afonso S et al. The emergence of Taenia solium cysticercosis in Eastern and Southern Africa as a serious agricultural problem and public health risk. Acta Trop.87, 13–23 (2003).
  • White AC Jr. Neurocysticercosis: updates on epidemiology, pathogenesis, diagnosis, and management. Ann. Rev. Med.51, 187–206 (2000).
  • Garcia HH, Del Brutto OH, Nash TE, White AC Jr, Tsang VC, Gilman RH. New concepts in the diagnosis and management of neurocysticercosis (Taenia solium). Am. J. Trop. Med. Hyg.72, 3–9 (2005).
  • Singhi P, Singhi S. Neurocysticercosis in children. Indian J. Pediatr.76, 537–545 (2009).
  • Sciutto E, Fragoso G, Fleury A et al.Taenia solium disease in humans and pigs: an ancient parasitosis disease rooted in developing countries and emerging as a major health problem of global dimensions. Microbes Infect.2, 1875–1890 (2000).
  • Sotelo J, Del Brutto OH. Brain cysticercosis. Arch. Med. Res.31, 3–14 (2000).
  • Esquivel A, Diaz-Otero F, Gimenez-Roldan S. Growing frequency of neurocysticercosis in Madrid (Spain). Neurologia20, 116–120 (2005).
  • Sorvillo FJ, DeGiorgio C, Waterman SH. Deaths from cysticercosis, United States. Emerg. Infect. Dis.13, 230–235 (2007).
  • Chang KH, Han MH. MRI of CNS parasitic diseases. J. Magn. Reson. Imaging8, 297–307 (1998).
  • Patel R, Jha S, Yadav RK. Pleomorphism of the clinical manifestations of neurocysticercosis. Trans. R. Soc. Trop. Med. Hyg.100, 134–141 (2006).
  • Kim SI, Kang SY, Cho SY, Hwang ES, Cha CY. Purification of cystic fluid antigen of Taenia solium metacestodes by affinity chromatography using monoclonal antibody and its antigenic characterization. Korean J. Parasitol.24, 145–158 (1986).
  • Cho SY, Kim SI, Kang SY, Kong Y. Biochemical properties of a purified protein in cystic fluid of Taenia solium metacestodes. Korean J. Parasitol.26, 87–94 (1988).
  • Tsang VC, Brand JA, Boyer AE. An enzyme-linked immunoelectrotransfer blot assay and glycoprotein antigens for diagnosing human cysticercosis (Taenia solium). J. Infect. Dis.159, 50–59 (1989).
  • Yang HJ, Chung JY, Yun DH et al. Immunoblot analysis of a 10 kDa antigen in cyst fluid of Taenia solium metacestodes. Parasite Immunol.20, 483–488 (1998).
  • Ko RC, Ng TF. Specificity of isoelectric focusing-purified antigens in the diagnosis of human cysticercosis. Parasitol Res.84, 565–969 (1998).
  • Ito A, Plancarte A, Ma L et al. Novel antigens for neurocysticercosis: simple method for preparation and evaluation for serodiagnosis. Am. J. Trop. Med. Hyg.59, 291–294 (1998).
  • Sako Y, Nakao M, Ikejima T, Piao XZ, Nakaya K, Ito A. Molecular characterization and diagnostic value of Taenia solium low-molecular-weight antigen genes. J. Clin. Microbiol.38, 4439–4444 (2000).
  • Sato MO, Yamasaki H, Sako Y et al. Evaluation of tongue inspection and serology for diagnosis of Taenia solium cysticercosis in swine. Vet. Parasitol.111, 309–322 (2003).
  • Hancock K, Khan A, Williams FB et al. Characterization of the 8-kilodalton antigens of Taenia solium metacestodes and evaluation of their use in an enzyme-linked immunosorbent assay for serodiagnosis. J. Clin. Microbiol.41, 2577–2586 (2003).
  • Lee EG, Bae YA, Jeong YT et al. Proteomic analysis of a 120 kDa protein complex in cyst fluid of Taenia solium metacestode and preliminary evaluation of its value for the serodiagnosis of neurocysticercosis. Parasitology131, 867–879 (2005).
  • Scheel CM, Khan A, Hancock K et al. Serodiagnosis of neurocysticercosis using synthetic 8-kD proteins: comparison of assay formats. Am. J. Trop. Med. Hyg.73, 771–776 (2005).
  • Sako MO, Sako Y, Nakao M, Yamasaki H, Nakaya K, Ito A. Evaluation of purified Taenia solium glycoproteins and recombinant antigens in the serologic detection of human and swine cysticercosis. J. Infect. Dis.194, 1783–1790 (2006).
  • Bueno EC, Scheel CM, Vaz AJ et al. Application of synthetic 8-kD and recombinant GP50 antigens in the diagnosis of neurocysticercosis by enzyme-linked immunosorbent assay. Am. J. Trop. Med. Hyg.72, 278–283 (2005).
  • Lee EG, Kim SH, Bae YA et al. A hydrophobic ligand binding protein of the Taenia solium metacestode mediates uptake of the host lipid: implication for the maintenance of parasitic cellular homeostasis. Proteomics7, 4016–4030 (2007).
  • Ferrer E, Bonay P, Foster-Cuevas M et al. Molecular cloning and characterisation of Ts8B1, Ts8B2 and Ts8B3, three new members of the Taenia solium metacestode 8 kDa diagnostic antigen family. Mol. Biochem. Parasitol.152, 90–100 (2007).
  • Bae YA, Jeong YT, Chung JY et al. A recombinant chimeric antigen toward a standardized serodiagnosis of Taenia solium neurocysticercosis. Proteomics Clin. Appl.2, 1596–1610 (2008).
  • Deckers N, Dorny P. Immunodiagnosis of Taenia solium taeniosis/cysticercosis. Trends Parasitol.26, 137–144 (2010).
  • Sikasunge CS, Phiri IK, Johansen MV, Willingham AL 3rd, Leifsson PS. Host-cell apoptosis in Taenia solium-induced brain granulomas in naturally infected pigs. Parasitology135, 1237–1242 (2008).
  • Alvarez JI, Rivera J, Teale JM. Differential release and phagocytosis of tegument glycoconjugates in neurocysticercosis: implications for immune evasion strategies. PLoS Negl. Trop. Dis.9, e218 (2008).
  • Vaca-Paniagua F, Torres-Rivera A, Parra-Unda R, Landa A. Taenia solium:antioxidant metabolism enzymes as targets for cestocidal drugs and vaccines. Curr. Top. Med. Chem.8, 393–399 (2008).
  • Lee EG, Lee MY, Chung JY et al. Feasibility of baculovirus-expressed recombinant 10-kDa antigen in the serodiagnosis of Taenia solium neurocysticercosis. Trans. R. Soc. Trop. Med. Hyg.99, 919–926 (2005).
  • Serpa JA, Yancey LS, White AC Jr. Advances in the diagnosis and management of neurocysticercosis. Expert Rev. Anti Infect. Ther.4, 1051–1061 (2006).
  • Greene RM, Hancock K, Wilkins PP, Tsang VC. Taenia solium: molecular cloning and serologic evaluation of 14- and 18-kDa related, diagnostic antigens. J. Parasitol.86, 1001–1007 (2000).
  • Hancock K, Pattabhi S, Greene RM et al. Characterization and cloning of GP50, a Taenia solium antigen diagnostic for cysticercosis. Mol. Biochem. Parasitol.133, 115–124 (2004).
  • Hancock K, Pattabhi S, Whitfield FW et al. Characterization and cloning of T24, a Taenia solium antigen diagnostic for cysticercosis. Mol. Biochem. Parasitol.147, 109–117 (2006).
  • Restrepo BI, Obregon-Henao A, Mesa M et al. Characterisation of the carbohydrate components of Taenia solium metacestode glycoprotein antigens. Int. J. Parasitol.30, 689–696 (2000).
  • Obregón-Henao A, Gil DL, Gómez DI, Sanzón F, Teale JM, Restrepo BI. The role of N-linked carbohydrates in the antigenicity of Taenia solium metacestode glycoproteins of 12, 16 and 18 kD. Mol. Biochem. Parasitol.114, 209–215 (2001).
  • Villota GE, Gomez DI, Volcy M et al. Similar diagnostic performance for neurocysticercosis of three glycoprotein preparations from Taenia solium metacestodes. Am. J. Trop. Med. Hyg.68, 276–280 (2003).
  • Deckers N, Saerens D, Kanobana K et al. Nanobodies, a promising tool for species-specific diagnosis of Taenia solium cysticercosis. Int. J. Parasitol.39, 625–633 (2009).
  • Greene RM, Wilkins PP, Tsang VC. Diagnostic glycoproteins of Taenia solium cysts share homologous 14- and 18-kDa subunits. Mol. Biochem. Parasitol.99, 257–261 (1999).
  • Haslam SM, Restrepo BI, Obergon-Henao A, Teale JM, Morris HR, Dell A. Structural characterization of the N-linked glycans from Taenia solium metacestodes. Mol. Biochem. Parasitol.126, 103–107 (2003).
  • Handali S, Klarman M, Gaspard AN et al. Multiantigen print immunoassay for comparison of diagnostic antigens for Taenia solium cysticercosis and taeniasis. Clin. Vaccine Immunol.17, 68–72 (2010).
  • Cho SY, Kong Y, Kim SI, Kang SY. Measurement of 150 kDa protein of Taenia solium metacestodes by antibody-sandwich ELISA in cerebrospinal fluid of neurocysticercosis patients. Korean J. Parasitol.30, 299–307 (1992).
  • Gao YJ, Yan HL, Ding FX, Lu YM, Sun SH. Annexin B1 at the host–parasite interface of the Taenia solium cysticercus: secreted and associated with inflammatory reaction. Acta Trop.101, 192–199 (2007).
  • Yan HL, Xue G, Mei Q, Ding FX, Wang YZ, Sun SH. Calcium-dependent proapoptotic effect of Taenia solium metacestodes annexin B1 on human eosinophils: a novel strategy to prevent host immune response. Int. J. Biochem. Cell. Biol.40, 2151–2163 (2008).
  • Vibanco-Perez N, Jimenez L, Merchant MT, Landa A. Characterization of glutathione-S transferase of Taenia solium. J. Parasitol.85, 448–453 (1999).
  • Vibanco-Perez N, Jimenez L, Mendoza-Hernandez G, Landa A. Characterization of a recombinant µ-class glutathione S-transferase from Taenia solium. Parasitol. Res.88, 398–404 (2002).
  • Plancarte A, Rendon JL, Landa A. Purification, characterization and kinetic properties of the Taenia solium glutathione S-transferase isoform 26.5 kDa. Parasitol. Res.93, 137–144 (2004).
  • Nguyen HA, Bae YA, Lee EG et al. A novel σ-like glutathione transferase of Taenia solium metacestode. Int. J. Parasitol.40, 1097–1106 (2010).
  • Nava G, Robert L, Plancarte A. Characterization of Taenia solium cysticerci microsomal glutathione S-transferase activity. Parasitol. Res.101, 1373–1381 (2007).
  • Castellanos-González A, Jimenez L, Landa A. Cloning, production and characterisation of a recombinant Cu/Zn superoxide dismutase from Taenia solium. Int. J. Parasitol.32, 1175–1182 (2002).
  • Molina-López J, Jiménez L, Ochoa-Sánchez A, Landa A. Molecular cloning and characterization of a 2-Cys peroxiredoxin from Taenia solium. J. Parasitol.92, 796–802 (2006).
  • Vaca-Paniagua F, Parra-Unda R, Landa A. Characterization of one typical 2-Cys peroxiredoxin gene of Taenia solium and Taenia crassiceps. Parasitol. Res.105, 781–787 (2009).
  • Rodríguez-Contreras D, Skelly PJ, Landa A, Shoemaker CB, Laclette JP. Molecular and functional characterization and tissue localization of 2 glucose transporter homologues (TGTP1 and TGTP2) from the tapeworm Taenia solium. Parasitology117, 579–588 (1998).
  • Montero E, Gonzalez LM, Bonay P et al.Taenia solium: identification and preliminary characterization of a lipid binding protein with homology to the SEC14 catalytic domain. Exp. Parasitol.116, 191–200 (2007).
  • Plancarte A, Flisser A, Gauci CG, Lightowlers MW. Vaccination against Taenia solium cysticercosis in pigs using native and recombinant oncosphere antigens. Int. J. Parasitol.29, 643–647 (1999).
  • Lightowlers MW, Gauci CG, Chow C et al. Molecular and genetic characterisation of the host-protective oncosphere antigens of taeniid cestode parasites. Int. J. Parasitol.33, 1207–1217 (2003).
  • Mayta H, Hancock K, Levine MZ et al. Characterization of a novel Taenia solium oncosphere antigen. Mol. Biochem. Parasitol.156, 154–161 (2007).
  • Flisser A, Gauci CG, Zoli A et al. Induction of protection against porcine cysticercosis by vaccination with recombinant oncosphere antigens. Infect. Immun.72, 5292–5297 (2004).
  • Gonzalez AE, Gauci CG, Barber D et al. Vaccination of pigs to control human neurocysticercosis. Am. J. Trop. Med. Hyg.72, 837–839 (2005).
  • Zheng Y, Cai X, Zhang D, Jing Z. Genetic variability of the 45W gene family between Chinese and Mexican Taenia solium. Am. J. Trop. Med. Hyg.78, 946–948 (2008).
  • Assana E, Kyngdon CT, Gauci CG et al. Elimination of Taenia solium transmission to pigs in a field trial of the TSOL18 vaccine in Cameroon. Int. J. Parasitol.40, 515–519 (2010).
  • Marshall W, Lightowlers MW. Eradication of Taenia solium cysticercosis: a role for vaccination of pigs. Int. J. Parasitol. DOI: 10.1016/j.ijpara.2010.05.001 (2010) (Epub ahead of print).
  • Kyngdon CT, Gauci CG, Rolfe RA et al. In vitro oncosphere-killing assays to determine immunity to the larvae of Taenia pisiformis, Taenia ovis, Taenia saginata, and Taenia solium. J. Parasitol.92, 273–281 (2006).
  • Verastegui M, Gilman RH, Garcia HH et al. Prevalence of antibodies to unique Taenia solium oncosphere antigens in taeniasis and human and porcine cysticercosis. Am. J. Trop. Med. Hyg.69, 438–444 (2003).
  • Guo A, Jin Z, Zheng Y et al. Induction of protection against porcine cysticercosis in growing pigs by DNA vaccination. Vaccine25, 170–175 (2007).
  • Sciutto E, Rosas G, Hernández M et al. Improvement of the synthetic tri-peptide vaccine (S3Pvac) against porcine Taenia solium cysticercosis in search of a more effective, inexpensive and manageable vaccine. Vaccine25, 1368–1378 (2007).
  • Santovanez SJ, Hernandez-Gonzalez A, Chile N et al. Proteomic study of activated Taenia solium oncosphere. Mol. Biochem. Parasitol.171, 32–39 (2010).
  • Flisser A, Woodhouse E, Larralde C. Human cysticercosis: antigens, antibodies and non-responders. Clin. Exp. Immunol.39, 27–37 (1980).
  • Landa A, Laclette JP, Nicholson-Weller A, Shoemaker CB. cDNA cloning and recombinant expression of collagen-binding and complement inhibitor activity of Taenia solium paramyosin (AgB). Mol. Biochem. Parasitol.60, 343–347 (1993).
  • Laclette JP, Shoemaker CB, Richter D et al. Paramyosin inhibits complement C1. J. Immunol.148, 124–128 (1992).
  • Morales J, Velasco T, Tovar V et al.Castration and pregnancy of rural pigs significantly increase the prevalence of naturally acquired Taenia solium cysticercosis. Vet. Parasitol.108, 41–48 (2002).
  • Escobedo G, Camacho-Arroyo I, Hernández-Hernández OT, Ostoa-Saloma P, García-Varela M, Morales-Montor J. Progesterone induces scolex evagination of the human parasite Taenia solium: evolutionary implications to the host-parasite relationship. J. Biomed. Biotechnol DOI: 10.1155/2010/591079 (2010) (Epub ahead of print).
  • White AC Jr, Molinari JL, Pillai AV, Rege AA. Detection and preliminary characterization of Taenia solium metacestode proteases. J. Parasitol,78, 281–287 (1992).
  • Molinari JL, Mejia H, White AC Jr et al. Taenia solium: a cysteine protease secreted by metacestodes depletes human CD4 lymphocytes in vitro. Exp. Parasitol.94, 133–142 (2000).
  • Tato P, Fernández AM, Solano S et al. A cysteine protease from Taenia solium metacestodes induce apoptosis in human CD4+ T-cells. Parasitol. Res.92, 197–204 (2004).
  • Baig S, Damian RT, Molinari JL et al. Purification and characterization of a metacestode cysteine proteinase from Taenia solium involved in the breakdown of human IgG. Parasitology131, 411–416 (2005).
  • Solano S, Cortés IM, Copitin NI, Tato P, Molinari JL. Lymphocyte apoptosis in the inflammatory reaction around Taenia solium metacestodes in porcine cysticercosis. Vet. Parasitol.140, 171–176 (2006).
  • Li AH, Moon SU, Park YK et al. Identification and characterization of a cathepsin L-like cysteine protease from Taenia solium metacestode. Vet. Parasitol.141, 251–259 (2006).
  • Zimic M, Pajuelo M, Rueda D et al. Utility of a protein fraction with cathepsin L-like activity purified from cysticercus fluid of Taenia solium in the diagnosis of human cysticercosis. Am. J. Trop. Med. Hyg.80, 964–970 (2009).
  • Cai GB, Bae YA, Kim SH et al. A membrane-associated metalloprotease of Taenia solium metacestode structurally related to the FACE-1/Ste24p protease family. Int. J. Parasitol.36, 925–935 (2006).
  • Mendlovic F, Carrillo-Farga J, Torres J, Lactle JP, Flisser A. Differential expression of calreticulin in developmental stages of Taenia solium. J. Parasitol.92, 789–795 (2006).
  • Mendlovic F, Ostoa-Saloma P, Solís CF, Martínez-Ocaña J, Flisser A, Laclette JP. Cloning, characterization, and functional expression of Taenia solium calreticulin. J. Parasitol.90, 891–893 (2004).
  • Kim SH, Chung JY, Bae YA et al. Functional identification of a protein inhibitor of neuronal nitric oxide synthase of Taenia solium metacestode. Mol. Biochem. Parasitol.151, 41–51 (2007).
  • Willms K, Shoemaker CB, Skelly PJ, Landa A. Cloning and expression of a Na+, K+-ATPase α-subunit from Taenia solium (TNaK1a). Mol. Biochem. Parasitol.138, 79–82 (2004).
  • Jiménez L, Vibanco-Pérez N, Navarro L, Landa A. Cloning, expression and characterisation of a recombinant triosephosphate isomerase from Taenia solium. Int. J. Parasitol.30, 1007–1012 (2000).
  • Jeziorski MC, Greenberg RM. Voltage-gated calcium channel subunits from platyhelminths: potential role in praziquantel action. Int. J. Parasitol.36, 625–632 (2006).
  • Garcia HH, Pretell EJ, Gilman RH et al. A trial of antiparasitic treatment to reduce the rate of seizures due to cerebral cysticercosis. N. Engl. J. Med.350, 249–258 (2004).
  • Del Brutto OH, Wadia NH, Dumas M, Cruz M, Tsang VC, Schantz PM. Proposal of diagnostic criteria for human cysticercosis and neurocysticercosis. J. Neurol. Sci.142, 1–6 (1996).
  • McCormick GF. Cysticercosis – review of 230 patients. Bull. Clin. Neurosci.50, 76–101 (1985).
  • Chung JY, Kho WG, Hwang SY et al. Molecular determination of the origin of acephalic cysticercus. Parasitology130, 239–246 (2005).
  • Hauptman JS, Hinrichs C, Mele C, Lee HJ. Radiologic manifestations of intraventricular and subarachnoid racemose neurocysticercosis. Emerg. Radiol.11, 153–157 (2005).
  • Torgovnick J, Onouha A, Arsura E, Sethi NK, Sethi PK. Neuroimage: racemose neurocysticercosis. Clin. Neurol. Neurosurg.110, 97–98 (2008).

Websites

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.