Literature DB >> 1718315

Identification of linear epitopes of the BPV-1 L1 protein recognized by sera of infected or immunized animals.

A B Jenson1, P Lim, S Ghim, L Cowsert, C Olson, L Y Lim, C Farquhar, W Pilacinski.   

Abstract

Sera from cattle that had been inoculated with BPV-1 virions or with recombinant L1 proteins and serum from a rabbit that had been immunized with SDS-denatured virions were evaluated for their reactivity with 466 overlapping synthetic peptides corresponding to 95% of the BPV-1 L1 protein. The late serological response of cattle to both intact virions and recombinant L1 proteins exhibited a similar profile of reactivity with approximately 70% (7 of 10) of L1 antigenic sites. However, the L1 serological response of the rabbit to SDS-denatured virions exhibited a significant difference from bovine serum antibodies in the profile of epitopes recognized, including a relative lack of response to major bovine epitopes located between L1 amino acids (AAs) 300-400. Importantly, only the sera from animals inoculated/immunized with intact virions was capable of neutralizing BPV-1 infectivity of murine C127 cells, suggesting that nonlinear epitopes are important for papillomavirus neutralization.

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Year:  1991        PMID: 1718315     DOI: 10.1159/000163684

Source DB:  PubMed          Journal:  Pathobiology        ISSN: 1015-2008            Impact factor:   4.342


  2 in total

Review 1.  Multiplicity of uses of monoclonal antibodies that define papillomavirus linear immunodominant epitopes.

Authors:  A B Jenson; M C Jenson; L Cowsert; S J Ghim; J P Sundberg
Journal:  Immunol Res       Date:  1997-02       Impact factor: 2.829

2.  Characterization of HPV16 L1 loop domains in the formation of a type-specific, conformational epitope.

Authors:  Vanessa A Olcese; Yan Chen; Richard Schlegel; Hang Yuan
Journal:  BMC Microbiol       Date:  2004-07-19       Impact factor: 4.465

  2 in total

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