Characterization of HPV16 L1 loop domains in the formation of a type-specific, conformational epitopeReport as inadecuate




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BMC Microbiology

, 4:29

First Online: 19 July 2004Received: 09 March 2004Accepted: 19 July 2004

Abstract

BackgroundVirus-like particles VLPs formed by the human papillomavirus HPV L1 capsid protein are currently being tested in clinical trials as prophylactic vaccines against genital warts and cervical cancer. The efficacy of these vaccines is critically dependent upon L1 type-specific conformational epitopes. To investigate the molecular determinants of the HPV16 L1 conformational epitope recognized by monoclonal antibody 16A, we utilized a domain-swapping approach to generate a series of L1 proteins composed of a canine oral papillomavirus COPV L1 backbone containing different regions of HPV16 L1.

ResultsGross domain swaps, which did not alter the ability of L1 to assemble into VLPs, demonstrated that the L1 N-terminus encodes at least a component of the 16A antigenic determinant. Finer epitope mapping, using GST-L1 fusion proteins, mapped the 16A epitope to the L1 variable regions I and possibly II within the N-terminus.

ConclusionsThese results suggest that non-contiguous loop regions of L1 display critical components of a type-specific, conformational epitope.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2180-4-29 contains supplementary material, which is available to authorized users.

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Author: Vanessa A Olcese - Yan Chen - Richard Schlegel - Hang Yuan

Source: https://link.springer.com/article/10.1186/1471-2180-4-29



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