Palmitoylation of the HIV-1 Envelope Glycoprotein Is Critical for Viral Infectivity
Recent studies suggest that HIV-1 budding occurs selectively from detergent-insoluble membrane domains, referred to as lipid rafts. Palmitoylation is thought to be one of the factors responsible for targeting membrane proteins to lipid rafts. The cytoplasmic domain of the HIV-1 envelope glycoprotein...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2000-12, Vol.97 (25), p.13523-13525 |
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| creator | Rousso, I Mixon, M B Chen, B K Kim, P S |
| description | Recent studies suggest that HIV-1 budding occurs selectively from detergent-insoluble membrane domains, referred to as lipid rafts. Palmitoylation is thought to be one of the factors responsible for targeting membrane proteins to lipid rafts. The cytoplasmic domain of the HIV-1 envelope glycoprotein (gp160) contains two palmitoylated cysteine residues. In this work, we studied the solubility of gp160 after detergent extraction. We show that wild-type gp160 is mostly insoluble after ice-cold Triton X-100 extraction, but that it becomes almost completely soluble at 37⚬C. In contrast, we find that a mutant gp160, in which the two palmitoylated cysteine residues are replaced by serine, is Triton X-100 soluble even under ice-cold extraction. These findings are consistent with the properties of proteins that localize to lipid rafts and strongly suggest that gp160 is associated with lipid rafts. Further, removal of both palmitoylation sites results in the formation of virus with low levels of gp160 incorporation as well as a decrease in viral infectivity by 60-fold. Our results strongly support the suggestion that HIV-1 buds from lipid rafts and point to a role for rafts as a viral assembly hub. |
| doi_str_mv | 10.1073/pnas.240459697 |
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Palmitoylation is thought to be one of the factors responsible for targeting membrane proteins to lipid rafts. The cytoplasmic domain of the HIV-1 envelope glycoprotein (gp160) contains two palmitoylated cysteine residues. In this work, we studied the solubility of gp160 after detergent extraction. We show that wild-type gp160 is mostly insoluble after ice-cold Triton X-100 extraction, but that it becomes almost completely soluble at 37⚬C. In contrast, we find that a mutant gp160, in which the two palmitoylated cysteine residues are replaced by serine, is Triton X-100 soluble even under ice-cold extraction. These findings are consistent with the properties of proteins that localize to lipid rafts and strongly suggest that gp160 is associated with lipid rafts. Further, removal of both palmitoylation sites results in the formation of virus with low levels of gp160 incorporation as well as a decrease in viral infectivity by 60-fold. 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Palmitoylation is thought to be one of the factors responsible for targeting membrane proteins to lipid rafts. The cytoplasmic domain of the HIV-1 envelope glycoprotein (gp160) contains two palmitoylated cysteine residues. In this work, we studied the solubility of gp160 after detergent extraction. We show that wild-type gp160 is mostly insoluble after ice-cold Triton X-100 extraction, but that it becomes almost completely soluble at 37⚬C. In contrast, we find that a mutant gp160, in which the two palmitoylated cysteine residues are replaced by serine, is Triton X-100 soluble even under ice-cold extraction. These findings are consistent with the properties of proteins that localize to lipid rafts and strongly suggest that gp160 is associated with lipid rafts. Further, removal of both palmitoylation sites results in the formation of virus with low levels of gp160 incorporation as well as a decrease in viral infectivity by 60-fold. 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Mixon, M B ; Chen, B K ; Kim, P S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c586t-b3c981a0a0e4e8561123dd3f7afc58b44d9f17409ec8ea2111a6afd9630f3ad13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Biochemistry</topic><topic>Biological Sciences</topic><topic>Budding</topic><topic>Cell Line</topic><topic>Cell membranes</topic><topic>glycoprotein gp160</topic><topic>Glycoproteins</topic><topic>HIV</topic><topic>HIV 1</topic><topic>HIV Envelope Protein gp160 - metabolism</topic><topic>HIV-1 - metabolism</topic><topic>HIV-1 - pathogenicity</topic><topic>Human immunodeficiency virus</topic><topic>Human immunodeficiency virus 1</topic><topic>Humans</topic><topic>Incorporation</topic><topic>Lipids</topic><topic>Palmitic Acid - metabolism</topic><topic>Proteins</topic><topic>Rafts</topic><topic>Solubility</topic><topic>Triton X-100</topic><topic>Virions</topic><topic>Virulence</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rousso, I</creatorcontrib><creatorcontrib>Mixon, M B</creatorcontrib><creatorcontrib>Chen, B K</creatorcontrib><creatorcontrib>Kim, P S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rousso, I</au><au>Mixon, M B</au><au>Chen, B K</au><au>Kim, P S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Palmitoylation of the HIV-1 Envelope Glycoprotein Is Critical for Viral Infectivity</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2000-12-05</date><risdate>2000</risdate><volume>97</volume><issue>25</issue><spage>13523</spage><epage>13525</epage><pages>13523-13525</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Recent studies suggest that HIV-1 budding occurs selectively from detergent-insoluble membrane domains, referred to as lipid rafts. 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| subjects | Biochemistry Biological Sciences Budding Cell Line Cell membranes glycoprotein gp160 Glycoproteins HIV HIV 1 HIV Envelope Protein gp160 - metabolism HIV-1 - metabolism HIV-1 - pathogenicity Human immunodeficiency virus Human immunodeficiency virus 1 Humans Incorporation Lipids Palmitic Acid - metabolism Proteins Rafts Solubility Triton X-100 Virions Virulence Viruses |
| title | Palmitoylation of the HIV-1 Envelope Glycoprotein Is Critical for Viral Infectivity |
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