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Positively charged synthetic peptides from structural proteins of papillomaviruses abrogate human papillomavirus infectivity
Author(s) -
Bousarghin Latifa,
Touzé Antoine,
Yvonnet Bernard,
Coursaget Pierre
Publication year - 2004
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.20114
Subject(s) - capsid , infectivity , transfection , peptide , virology , human papillomavirus , virus , glycoprotein , biology , receptor , chemistry , papillomaviridae , viral entry , microbiology and biotechnology , cell culture , viral replication , biochemistry , genetics , medicine , cervical cancer , cancer
Human papillomavirus (HPV) virus‐like particles (VLP) and synthetic peptides corresponding to positively‐charged sequences of the major and minor capsid proteins were tested for their efficacy in inhibiting the infectivity of HPV 31 pseudovirions by blocking virus entry into cells. A greater than 80% reduction of transfection was observed with one HPV‐31 peptide at a concentration of 10 μg/ml. Moreover, the blocking was not type‐specific since similar reduction in transfection was observed with peptides from other HPV types at a concentration of 60 μg/ml. This concentration was non‐toxic for the cells. These findings indicate that some of the positively‐charged sequences of the L1 and L2 HPV capsid proteins of papillomavirus are compounds that might be locally active against sexually transmitted papillomavirus. The findings provide further evidence that cellular glycosamino‐glycans (GAGs) are functional receptors for HPVs. J. Med. Virol. 73:474–480, 2004. © 2004 Wiley‐Liss, Inc.