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Deglycosylation effect of the mammalian sperm maturation antigen (SMA2) on serological reaction and acrosome reaction.
MedLine Citation:
PMID:  22824309     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Spermatozoal membrane proteins are considered to possess several immunological unique characteristics as the cell is formed behind the blood-testes barriers. Major goat sperm maturation antigen (SMA2) contains one hexosamine along with mannose, galactose and glucose. In the present study, effects of deglycosylation of SMA2 antigen on immuno-reactivity and the serological activity was investigated. SMA2 glycoantigen showed positive immunoreactivity after treatment with sodium borohydride (NaBH(4)) and moreover this generated a 44kDa protein band which was negative for periodic acid Schiff reagent. Trifluoromethanesulfonic acid (TFMS) caused aggregation and restricted the free mobility of the treated antigen on SDS-PAGE and the protein band generated by TFMS treatment also showed positive immuno-reactivity. The results supported the views that the protein portion retains its immuno-reactivity even after oxidation of the vicinal hydroxyl group of saccharide component of SMA2 antigen. These data suggest that immunodominent epitopes exist on the core protein by which the SMA2 antigen retains its immuno-reactivity even after disruption of the saccharide portion. Additional experiments demonstrate that protein epitopes have a role in capacitation and the acrosome reaction (AR) in presence of antibody which is raised against this protein part of SMA2 using the negative staining of FITC-PSA (fluorescein isothiocyanate-labeled Pisum sativum agglutinin) probe. Altogether these findings indicate that the protein portion of SMA2 might fulfill the serological activity of the antigen as well as the protein epitope affects the acrosome reaction. In view of this property, we propose that the protein portion of SMA2 antigen might be considered as a potential antigenic target for an immune response.
Authors:
Tapasi Das; Tapati Chatterjee
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-7-7
Journal Detail:
Title:  Animal reproduction science     Volume:  -     ISSN:  1873-2232     ISO Abbreviation:  -     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-7-24     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7807205     Medline TA:  Anim Reprod Sci     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2012 Elsevier B.V. All rights reserved.
Affiliation:
Department of Molecular and Human Genetics Division, Indian Institute of Chemical Biology, 4 Raja S.C Mullick Road, Jadavpur, Kolkata 700032, W.B, India.
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