Hostname: page-component-586b7cd67f-tf8b9 Total loading time: 0 Render date: 2024-11-28T16:26:47.387Z Has data issue: false hasContentIssue false
  • English
  • Français

An evaluation of antigen B family of Echinococcus granulosus, its conformational propensity and elucidation of the agretope

Published online by Cambridge University Press:  01 September 2009

D. Bhattacharya ,
D. Pan ,
S. Das ,
A.K. Bera ,
S. Bandyopadhyay  and
S.K. Das
D. Bhattacharya*
Affiliation:
Indian Veterinary Research Institute, Eastern Regional Station, 37-Belgachia Road, Kolkata700 037, India
D. Pan
Affiliation:
Indian Veterinary Research Institute, Eastern Regional Station, 37-Belgachia Road, Kolkata700 037, India
S. Das
Affiliation:
Indian Veterinary Research Institute, Eastern Regional Station, 37-Belgachia Road, Kolkata700 037, India
A.K. Bera
Affiliation:
Indian Veterinary Research Institute, Eastern Regional Station, 37-Belgachia Road, Kolkata700 037, India
S. Bandyopadhyay
Affiliation:
Indian Veterinary Research Institute, Eastern Regional Station, 37-Belgachia Road, Kolkata700 037, India
S.K. Das
Affiliation:
Indian Veterinary Research Institute, Eastern Regional Station, 37-Belgachia Road, Kolkata700 037, India
*
*Fax: +91 3325 565725 E-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

The present communication evaluates the antigen B (AgB) family of bubaline isolates of Echinococcus granulosus with respect to their conformational propensity and also discusses the stretches of agretope. AgB, which is abundantly present in hydatid cyst fluid, is encoded by a gene family, AgB1–AgB5. Hydatidosis is of zoonotic and economic importance in India. Buffaloes serve as the intermediate host. However, to date the AgB family has not been fully analysed. During the present study two different primers used for amplification of AgB1 revealed homology to Echinococcus canadensis (G8) as well as E. granulosus sensu stricto (G1/G2). The sequence of AgB3 is homologous to that of the well-defined species, Echinococcus ortleppi (G5), and the predicted amino acid sequence of AgB4 is homologous to bovine isolates identified earlier. α- and β-amphipathic structures were recorded in all the antigens designated as T-cell receptor sites. The antigenic index of different stretches correlated with hydrophilicity because the hydrophobic residues are not accessible to the cells. In this study, we investigated the binding propensity of AgB to MHC II in order to determine stretches of agretope. Agretopes began with four hydrophilic residues. Two to three additional hydrophilic residues were present in the internal motif. This comparison of AgB and its family of bubaline isolates, with respect to their sequence information, α- and β- amphipathic regions, antigenic index and stretches of agretope is the first such report from India.

Type
Research Papers
Information
Journal of Helminthology , Volume 83 , Issue 3 , September 2009 , pp. 219 - 224
Copyright
Copyright © Cambridge University Press 2008

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Arend, A.C., Zaha, A., Ayala, F.Z. & Haag, K.L. (2004) The Echinococcus granulosus antigen B shows a high degree of genetic variability. Experimental Parasitology 108, 76–80.CrossRefGoogle Scholar
Bowles, J., Blair, D. & McManus, D.P. (1995) A molecular phylogeny of the genus Echinococcus. Parasitology 110, 317–328.CrossRefGoogle ScholarPubMed
Chemale, G., Haag, K.L., Ferreira, H.B. & Zaha, A. (2001) Echinococcus granulosus antigen B is encoded by a gene family. Molecular and Biochemical Parasitology 16, 233–237.CrossRefGoogle Scholar
Delisi, C. & Berzofsky, J.A. (1985) T-cell antigenic sites tend to be amphipathic structures. Proceedings of the National Academy of Sciences, USA 82, 7048–7052.CrossRefGoogle ScholarPubMed
Fernández, V., Ferreira, H.B., Fernández, C., Zaha, A. & Nieto, A. (1996) Molecular characterisation of a novel 8-kDa subunit of Echinococcus granulosus antigen B. Molecular and Biochemical Parasitology 77, 247–250.CrossRefGoogle ScholarPubMed
Goldsby, R.A., Kindt, T.J. & Osborne, B.A. (2000) Kuby immunology. 165 pp. 4th edn.New York, W.H. Freeman and Company.Google Scholar
Haag, K.L., Alves-Junior, L., Zaha, A. & Ayala, F.J. (2004) Contingent, non-neutral evolution in a multicellular parasite: natural selection and gene conversion in the Echinococcus granulosus antigen B gene family. Gene 333, 157–167.CrossRefGoogle Scholar
Haag, K.L., Araújo, A.M., Gottstein, B., Siles-Lucas, M., Thompson, R.C. & Zaha, A. (1999) Breeding systems in Echinococcus granulosus (Cestoda; Taeniidae): selfing or outcrossing? Parasitology 118, 63–71.CrossRefGoogle ScholarPubMed
Kaiser, E.T. & Kézdy, F.J. (1984) Amphiphilic secondary structure: design of peptide hormones. Science 223, 249–255.CrossRefGoogle ScholarPubMed
Lavikainen, A., Lehtinen, M.J., Meri, T., Hirvela-Koski, V. & Meri, S. (2003) Molecular genetic characterization of the Fennoscandian cervid strain, a new genotypic group (G10) of Echinococcus granulosus. Parasitology 127, 207–215.CrossRefGoogle Scholar
Lightowlers, M.W. & Gottstein, B. (1995) Echinococcosis/hydatidosis: antigens, immunological and molecular diagnosis. pp. 355–410in Thompson, R.C.A. & Lymbery, A.J. (Eds) Echinococcus and hydatid disease. Wallingford, Oxon, UK, CAB International.Google Scholar
Nakao, M., McManus, D.P., Schantz, P.M., Craig, P.S. & Ito, A. (2007) A molecular phylogeny of the genus Echinococcus inferred from complete mitochondrial genomes. Parasitology 134, 713–722.CrossRefGoogle ScholarPubMed
Rosenzvit, M.C., Camicia, F., Kamenetzky, L., Muzulin, P.M. & Gutierrez, A.M. (2006) Identification and intra-specific variability analysis of secreted and membrane-bound proteins from Echinococcus granulosus. Parasitology International 55 (Suppl.), S63–S67.CrossRefGoogle ScholarPubMed
Scott, J.C., Stefaniak, J., Pawlowski, Z.S. & McManus, D.P. (1997) Molecular genetic analysis of human cystic hydatid cases from Poland: identification of a new genotype (G9) of Echinococcus granulosus. Parasitology 114, 37–43.CrossRefGoogle ScholarPubMed
Shepherd, J.C., Aitken, A. & McManus, D.P. (1991) A protein secreted in vivo by Echinococcus granulosus inhibits elastase activity and neutrophil chemotaxis. Molecular and Biochemical Parasitology 44, 81–90.CrossRefGoogle ScholarPubMed
Singh, H. & Raghava, G.P. (2001) ProPred: prediction of HLA-DR binding sites. Bioinformatics 17, 1236–1237.CrossRefGoogle ScholarPubMed
Spouge, J.L., Guy, H.R., Cornette, J.L., Margalit, H., Cease, K., Berzofsky, J.A. & DeLisi, C. (1987) Strong conformational propensities enhance T cell antigenicity. Journal of Immunology 138, 204–212.CrossRefGoogle ScholarPubMed
Virgino, V.G., Hernandez, A., Rott, M.B., Monteiro, K.M., Zandonai, A.F., Nieto, A., Zaha, A. & Ferreira, H.B. (2003) A set of recombinant antigens from Echinococcus granulosus with potential for use in the immunodiagnosis of human cystic hydatid disease. Clinical and Experimental Immunology 132, 309–315.CrossRefGoogle Scholar