Identification of a neutralization epitope in the VP1 capsid protein of SV40

Abstract Three SV40 escape mutants were identified by selection in the presence of monoclonal antibodies with neutralizing activity. The VP1 amino acid alterations in these mutants were: (1) K73 → E (in loop BC); (2) D77 → E (in loop BC); (3) K171 → R (in loop EF); and (4) Q175 → H (in loop EF). The...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2008-11, Vol.381 (1), p.116-122
Main Authors: Murata, Haruhiko, Teferedegne, Belete, Sheng, Li, Lewis, Andrew M, Peden, Keith
Format: Article
Language:English
Subjects:
Antibodies, Viral - immunology
Antibodies, Viral - metabolism
Capsid Proteins - chemistry
Capsid Proteins - genetics
Capsid Proteins - immunology
Cell Line
Epitope
Epitope Mapping
Epitopes - chemistry
Epitopes - immunology
Humans
Infectious Disease
JC virus
Monoclonal antibody
Mutation - genetics
Neutralization
Neutralization Tests
Phenotype
Polyomavirus
Primates
Simian virus 40
Simian virus 40 - genetics
Simian virus 40 - immunology
SV40
VP1
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Summary:Abstract Three SV40 escape mutants were identified by selection in the presence of monoclonal antibodies with neutralizing activity. The VP1 amino acid alterations in these mutants were: (1) K73 → E (in loop BC); (2) D77 → E (in loop BC); (3) K171 → R (in loop EF); and (4) Q175 → H (in loop EF). These residues are clustered in close proximity to each other on the surface of the native capsid protein, strongly suggesting that they form a conformational epitope directly recognized by the neutralizing antibody. To our knowledge, the present study represents the first experimental mapping of a neutralization epitope of a polyomavirus family member. Structural information regarding the neutralization epitope should be useful for clarifying the extent of cross-reactivity exhibited by the humoral immune response towards related primate polyomaviruses (e.g., SV40, BKV, and JCV).
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2008.07.032