6533b870fe1ef96bd12d077f

RESEARCH PRODUCT

Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines.

Claudia FliggeJ. Robin HarrisIngrid PetzakMartin SappRolf E. Streeck

subject

virusesImmunologyTrimerBiologymedicine.disease_causeMicrobiologycomplex mixturesSerineCapsidVirologyAnimal VirusesmedicineCysteineDisulfidesPapillomaviridaeMutationVirus AssemblyCapsomereVirionvirus diseasesbiochemical phenomena metabolism and nutritionMolecular biologyCapsidInsect ScienceMutationBiophysicsCysteine

description

ABSTRACT We have used viruslike particles (VLPs) of human papillomaviruses to study the structure and assembly of the viral capsid. We demonstrate that mutation of either of two highly conserved cysteines of the major capsid protein L1 to serine completely prevents the assembly of VLPs but not of capsomers, whereas mutation of all other cysteines leaves VLP assembly unaffected. These two cysteines form intercapsomeric disulfides yielding an L1 trimer. Trimerization comprises about half of the L1 molecules in VLPs but all L1 molecules in complete virions. We suggest that trimerization of L1 is indispensable for the stabilization of intercapsomeric contacts in papillomavirus capsids.

yearjournalcountryeditionlanguage
1998-06-17Journal of virology
10.1128/jvi.72.7.6186-6189.1998https://pubmed.ncbi.nlm.nih.gov/9621087