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Influence of high hydrostatic pressure on epitope mapping of tobacco mosaic virus coat protein.


ABSTRACT: In this study, we investigated the effect of high hydrostatic pressure (HHP) on tobacco mosaic virus (TMV), a model virus in immunology and one of the most studied viruses to date. Exposure to HHP significantly altered the recognition epitopes when compared to sera from mice immunized with native virus. These alterations were studied further by combining HHP with urea or low temperature and then inoculating the altered virions into Balb-C mice. The antibody titers and cross-reactivity of the resulting sera were determined by ELISA. The antigenicity of the viral particles was maintained, as assessed by using polyclonal antibodies against native virus. The antigenicity of canonical epitopes was maintained, although binding intensities varied among the treatments. The patterns of recognition determined by epitope mapping were cross checked with the prediction algorithms for the TMVcp amino acid sequence to infer which alterations had occurred. These findings suggest that different cleavage sites were exposed after the treatments and this was confirmed by epitope mapping using sera from mice immunized with virus previously exposed to HHP.

SUBMITTER: Ferreira de Lima Neto D 

PROVIDER: S-EPMC3949500 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature

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Influence of high hydrostatic pressure on epitope mapping of tobacco mosaic virus coat protein.

Ferreira de Lima Neto Daniel D   Bonafe Carlos Francisco Sampaio CF   Arns Clarice Weis CW  

Viral immunology 20140301 2


In this study, we investigated the effect of high hydrostatic pressure (HHP) on tobacco mosaic virus (TMV), a model virus in immunology and one of the most studied viruses to date. Exposure to HHP significantly altered the recognition epitopes when compared to sera from mice immunized with native virus. These alterations were studied further by combining HHP with urea or low temperature and then inoculating the altered virions into Balb-C mice. The antibody titers and cross-reactivity of the res  ...[more]

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