KRISHI
ICAR RESEARCH DATA REPOSITORY FOR KNOWLEDGE MANAGEMENT
(An Institutional Publication and Data Inventory Repository)
"Not Available": Please do not remove the default option "Not Available" for the fields where metadata information is not available
"1001-01-01": Date not available or not applicable for filling metadata infromation
"1001-01-01": Date not available or not applicable for filling metadata infromation
Please use this identifier to cite or link to this item:
http://krishi.icar.gov.in/jspui/handle/123456789/76920
Title: | An evaluation of antigen B family of Echinococcus granulosus, its conformational propensity and elucidation of the agretope |
Other Titles: | Not Available |
Authors: | D Bhattacharya D Pan S Das A K Bera S Bandyopadhyay S K Das |
ICAR Data Use Licennce: | http://krishi.icar.gov.in/PDF/ICAR_Data_Use_Licence.pdf |
Author's Affiliated institute: | Indian Veterinary Research Institute |
Published/ Complete Date: | 1001-01-01 |
Project Code: | Not Available |
Keywords: | Antigen B, Echinicoccus granulosus, Hydatidosis, |
Publisher: | Cambridge University Press |
Citation: | 6 |
Series/Report no.: | Not Available; |
Abstract/Description: | 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. alpha- and beta-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, alpha- and beta- amphipathic regions, antigenic index and stretches of agretope is the first such report from India. |
Description: | Not Available |
ISSN: | Not Available |
Type(s) of content: | Research Paper |
Sponsors: | Not Available |
Language: | English |
Name of Journal: | Journal of Helminthology |
Journal Type: | NAAS |
NAAS Rating: | 7.87 |
Impact Factor: | 1.866 |
Volume No.: | 83(3) |
Page Number: | 219-24 |
Name of the Division/Regional Station: | Eastern Regional Station of IVRI, Kolkata |
Source, DOI or any other URL: | doi: 10.1017/S0022149X0814740X. |
URI: | http://krishi.icar.gov.in/jspui/handle/123456789/76920 |
Appears in Collections: | AS-IVRI-Publication |
Files in This Item:
There are no files associated with this item.
Items in KRISHI are protected by copyright, with all rights reserved, unless otherwise indicated.