Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate.
As HIV-1-encoded envelope protein traverses the secretory pathway, it may be modified with N- and O-linked carbohydrate. When the gp120s of HIV-1 NL4-3, HIV-1 YU2, HIV-1 Bal, HIV-1 JRFL, and HIV-1 JRCSF were expressed as secreted proteins, the threonine at consensus position 499 was found to be O-gl...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2015-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4410959?pdf=render |
| _version_ | 1831768877773619200 |
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| author | Elizabeth Stansell Maria Panico Kevin Canis Poh-Choo Pang Laura Bouché Daniel Binet Michael-John O'Connor Elena Chertova Julian Bess Jeffrey D Lifson Stuart M Haslam Howard R Morris Ronald C Desrosiers Anne Dell |
| author_facet | Elizabeth Stansell Maria Panico Kevin Canis Poh-Choo Pang Laura Bouché Daniel Binet Michael-John O'Connor Elena Chertova Julian Bess Jeffrey D Lifson Stuart M Haslam Howard R Morris Ronald C Desrosiers Anne Dell |
| author_sort | Elizabeth Stansell |
| collection | DOAJ |
| description | As HIV-1-encoded envelope protein traverses the secretory pathway, it may be modified with N- and O-linked carbohydrate. When the gp120s of HIV-1 NL4-3, HIV-1 YU2, HIV-1 Bal, HIV-1 JRFL, and HIV-1 JRCSF were expressed as secreted proteins, the threonine at consensus position 499 was found to be O-glycosylated. For SIVmac239, the corresponding threonine was also glycosylated when gp120 was recombinantly expressed. Similarly-positioned, highly-conserved threonines in the influenza A virus H1N1 HA1 and H5N1 HA1 envelope proteins were also found to carry O-glycans when expressed as secreted proteins. In all cases, the threonines were modified predominantly with disialylated core 1 glycans, together with related core 1 and core 2 structures. Secreted HIV-1 gp140 was modified to a lesser extent with mainly monosialylated core 1 O-glycans, suggesting that the ectodomain of the gp41 transmembrane component may limit the accessibility of Thr499 to glycosyltransferases. In striking contrast to these findings, gp120 on purified virions of HIV-1 Bal and SIV CP-MAC lacked any detectable O-glycosylation of the C-terminal threonine. Our results indicate the absence of O-linked carbohydrates on Thr499 as it exists on the surface of virions and suggest caution in the interpretation of analyses of post-translational modifications that utilize recombinant forms of envelope protein. |
| first_indexed | 2024-12-22T07:10:24Z |
| format | Article |
| id | doaj.art-27d7d92696914ff1a11ff3d9a4512bc0 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-22T07:10:24Z |
| publishDate | 2015-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-27d7d92696914ff1a11ff3d9a4512bc02022-12-21T18:34:32ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01104e012478410.1371/journal.pone.0124784Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate.Elizabeth StansellMaria PanicoKevin CanisPoh-Choo PangLaura BouchéDaniel BinetMichael-John O'ConnorElena ChertovaJulian BessJeffrey D LifsonStuart M HaslamHoward R MorrisRonald C DesrosiersAnne DellAs HIV-1-encoded envelope protein traverses the secretory pathway, it may be modified with N- and O-linked carbohydrate. When the gp120s of HIV-1 NL4-3, HIV-1 YU2, HIV-1 Bal, HIV-1 JRFL, and HIV-1 JRCSF were expressed as secreted proteins, the threonine at consensus position 499 was found to be O-glycosylated. For SIVmac239, the corresponding threonine was also glycosylated when gp120 was recombinantly expressed. Similarly-positioned, highly-conserved threonines in the influenza A virus H1N1 HA1 and H5N1 HA1 envelope proteins were also found to carry O-glycans when expressed as secreted proteins. In all cases, the threonines were modified predominantly with disialylated core 1 glycans, together with related core 1 and core 2 structures. Secreted HIV-1 gp140 was modified to a lesser extent with mainly monosialylated core 1 O-glycans, suggesting that the ectodomain of the gp41 transmembrane component may limit the accessibility of Thr499 to glycosyltransferases. In striking contrast to these findings, gp120 on purified virions of HIV-1 Bal and SIV CP-MAC lacked any detectable O-glycosylation of the C-terminal threonine. Our results indicate the absence of O-linked carbohydrates on Thr499 as it exists on the surface of virions and suggest caution in the interpretation of analyses of post-translational modifications that utilize recombinant forms of envelope protein.http://europepmc.org/articles/PMC4410959?pdf=render |
| spellingShingle | Elizabeth Stansell Maria Panico Kevin Canis Poh-Choo Pang Laura Bouché Daniel Binet Michael-John O'Connor Elena Chertova Julian Bess Jeffrey D Lifson Stuart M Haslam Howard R Morris Ronald C Desrosiers Anne Dell Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate. PLoS ONE |
| title | Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate. |
| title_full | Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate. |
| title_fullStr | Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate. |
| title_full_unstemmed | Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate. |
| title_short | Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate. |
| title_sort | gp120 on hiv 1 virions lacks o linked carbohydrate |
| url | http://europepmc.org/articles/PMC4410959?pdf=render |
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