期刊
JOURNAL OF VIROLOGY
卷 75, 期 16, 页码 7727-7731出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.75.16.7727-7731.2001
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Human papillomavirus capsid assembly requires intercapsomeric disulfide bonds between molecules of the major capsid protein L1. Virions isolated from naturally occurring lesions have a higher degree of cross-linking than virus-like particles (VLPs), which have been generated in eukaryotic expression systems. Here we show that DNA encapsidation into VLPs leads to increased cross-linking between L1 molecules comparable to that seen in virions. A higher trypsin resistance, indicating a tighter association of capsomeres through DNA interaction, accompanies this structural change.
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