Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate
| العنوان: | Gp120 on HIV-1 Virions Lacks O-Linked Carbohydrate |
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| المؤلفون: | Elena Chertova, Ronald C. Desrosiers, Laura Bouché, Maria Panico, Jeffrey D. Lifson, Michael O'Connor, Kevin Canis, Howard R. Morris, Stuart M. Haslam, Elizabeth Stansell, Julian W. Bess, Daniel Binet, Anne Dell, Poh-Choo Pang |
| المساهمون: | Biotechnology and Biological Sciences Research Council (BBSRC) |
| المصدر: | PLoS ONE, Vol 10, Iss 4, p e0124784 (2015) PLoS ONE |
| بيانات النشر: | Public Library of Science (PLoS), 2015. |
| سنة النشر: | 2015 |
| مصطلحات موضوعية: | Threonine, viruses, lcsh:Medicine, HIV Envelope Protein gp120, law.invention, ACTIVATION, Viral Envelope Proteins, RECOMBINANT, law, lcsh:Science, Multidisciplinary, Membrane Glycoproteins, TYPE-1 ENVELOPE GLYCOPROTEIN, GLYCOSYLATION SITES, virus diseases, Transmembrane protein, Recombinant Proteins, 3. Good health, Multidisciplinary Sciences, Biochemistry, Ectodomain, Influenza A virus, HUMAN-IMMUNODEFICIENCY-VIRUS, Recombinant DNA, Science & Technology - Other Topics, ENDOPROTEOLYTIC CLEAVAGE, Research Article, STRUCTURAL-CHARACTERIZATION, Glycan, PROTEINS, General Science & Technology, Carbohydrates, Biology, Gp41, MD Multidisciplinary, Humans, INFECTIVITY, PROTEOLYTIC CLEAVAGE, Secretory pathway, Science & Technology, lcsh:R, Virion, Secretory protein, HEK293 Cells, biology.protein, HIV-1, lcsh:Q, Protein Processing, Post-Translational, HeLa Cells |
| الوصف: | 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. |
| اللغة: | English |
| تدمد: | 1932-6203 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6721c0601ee01e0668515068f8a0447f http://europepmc.org/articles/PMC4410959?pdf=render |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....6721c0601ee01e0668515068f8a0447f |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19326203 |
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