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...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4053435?pdf=render |
| _version_ | 1819135612803874816 |
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| author | Eric J Ryndock Michael J Conway Samina Alam Sana Gul Sheeba Murad Neil D Christensen Craig Meyers |
| author_facet | Eric J Ryndock Michael J Conway Samina Alam Sana Gul Sheeba Murad Neil D Christensen Craig Meyers |
| author_sort | Eric J Ryndock |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-22T10:21:51Z |
| format | Article |
| id | doaj.art-87c6602cc77c4429bf49ec94819dce47 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-22T10:21:51Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-87c6602cc77c4429bf49ec94819dce472022-12-21T18:29:37ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0196e9948810.1371/journal.pone.0099488Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability.Eric J RyndockMichael J ConwaySamina AlamSana GulSheeba MuradNeil D ChristensenCraig MeyersHuman 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.http://europepmc.org/articles/PMC4053435?pdf=render |
| spellingShingle | Eric J Ryndock Michael J Conway Samina Alam Sana Gul Sheeba Murad Neil D Christensen Craig Meyers Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability. PLoS ONE |
| title | Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability. |
| title_full | Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability. |
| title_fullStr | Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability. |
| title_full_unstemmed | Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability. |
| title_short | Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability. |
| title_sort | roles for human papillomavirus type 16 l1 cysteine residues 161 229 and 379 in genome encapsidation and capsid stability |
| url | http://europepmc.org/articles/PMC4053435?pdf=render |
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