Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability

Human papillomavirus (HPV) capsids are formed through a network of inter- and intra-pentameric hydrophobic interactions and disulfide bonds. 72 pentamers of the major capsid protein, L1, and an unknown amount of the minor capsid protein, L2, form the structure of the capsid. There are 12 conserved L...

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Bibliographic Details
Published in:PloS one 2014-06, Vol.9 (6), p.e99488-e99488
Main Authors: Ryndock, Eric J, Conway, Michael J, Alam, Samina, Gul, Sana, Murad, Sheeba, Christensen, Neil D, Meyers, Craig
Format: Article
Language:English
Subjects:
Biology and Life Sciences
Capsid
Capsid protein
Capsids
Chemical bonds
Cysteine
Cysteine - genetics
Cystine
Deoxyribonucleic acid
Disulfide bonds
DNA
Encapsidation
Endonuclease
Genome, Viral
Genomes
Genomic Instability
Genomics
Human papillomavirus
Hydrophobicity
Immunology
Infections
Life cycle engineering
Life cycles
Medicine
Mutation
Papillomaviridae - genetics
Papillomavirus
Papillomavirus infections
Protein structure
Proteins
Residues
Serine
Structure-function relationships
Studies
Thiols
Virion
Virions
Virology
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Summary:Human papillomavirus (HPV) capsids are formed through a network of inter- and intra-pentameric hydrophobic interactions and disulfide bonds. 72 pentamers of the major capsid protein, L1, and an unknown amount of the minor capsid protein, L2, form the structure of the capsid. There are 12 conserved L1 cysteine residues in HPV16. While C175, C185, and C428 have been implicated in the formation of a critical inter-pentameric disulfide bond, no structural or functional roles have been firmly attributed to any of the other conserved cysteine residues. Here, we show that substitution of cysteine residues C161, C229, and C379 for serine hinders the accumulation of endonuclease-resistant genomes as virions mature within stratifying and differentiating human epithelial tissue. C229S mutant virions form, but are non-infectious. These studies add detail to the differentiation-dependent assembly and maturation that occur during the HPV16 life cycle in human tissue.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0099488