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Basic Characteristics of Mutations
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Mutation Site
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C379S |
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Mutation Site Sentence
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Establishment of Productive HPV16 C161S, C229S, and C379S Cell Lines |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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L1 |
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Standardized Encoding Gene
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L1
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Genotype/Subtype
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HPV16 |
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Viral Reference
|
-
|
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Functional Impact and Mechanisms
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Disease
|
-
|
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Immune
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- |
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Target Gene
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-
|
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Clinical and Epidemiological Correlations
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Clinical Information
|
- |
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Treatment
|
- |
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Location
|
- |
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Literature Information
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|
PMID
|
24918586
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Title
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Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability
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Author
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Ryndock EJ,Conway MJ,Alam S,Gul S,Murad S,Christensen ND,Meyers C
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Journal
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PloS one
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Journal Info
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2014 Jun 11;9(6):e99488
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Abstract
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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.
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Sequence Data
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-
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