Role of Oligosaccharides in the Processing and Maturation of Envelope Glycoproteins of Human Immunodeficiency Virus Type 1
The processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) were studied in infected cells treated with inhibitors of oligosaccharide processing. In MOLT-3 cells chronically infected with HIV-1 (strain HTLV-IIIB), tunicamycin severely inhibited the glycosyl...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1989-05, Vol.86 (9), p.3384-3388 |
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| creator | Pal, Ranajit Hoke, George M. Sarngadharan, M. G. |
| description | The processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) were studied in infected cells treated with inhibitors of oligosaccharide processing. In MOLT-3 cells chronically infected with HIV-1 (strain HTLV-IIIB), tunicamycin severely inhibited the glycosylation of envelope proteins. Deoxynojirimycin, an inhibitor of glucosidase I in the rough endoplasmic reticulum, inhibited the proteolytic processing of gp 160, whereas no such effect was noted with either deoxymannojirimycin or swainsonine, inhibitors of mannosidase I and II, respectively, in the Golgi complex. The processed gp120 and gp41 synthesized in the presence of deoxymannojirimycin were found to contain mannose-rich oligosaccharide cores as evidenced by their susceptibility to endoglycosidase H digestion. The formation of syncytia normally observed when CEM cells are cocultured with HIV-1-infected cells was markedly inhibited in the presence of deoxynojirimycin, but such inhibition was not observed in cells treated with deoxymannojirimycin or swainsonine. The infectivity of virions released from MOLT-3/HTLV-IIIBcells treated with deoxynojirimycin or deoxymannojirimycin was significantly lower than the infectivity of virions released from untreated cells. On the other hand, treatment with swainsonine did not affect the infectivity of the progeny virus. These results suggest that the proteolytic processing of gp160 takes place in infected cells when the glycoprotein has mannose-rich oligosaccharide structures. Trimming of glucose residues and the primary trimming of mannose residues are necessary for the release of infectious virus. |
| doi_str_mv | 10.1073/pnas.86.9.3384 |
| format | Article |
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G.</creator><creatorcontrib>Pal, Ranajit ; Hoke, George M. ; Sarngadharan, M. G.</creatorcontrib><description>The processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) were studied in infected cells treated with inhibitors of oligosaccharide processing. In MOLT-3 cells chronically infected with HIV-1 (strain HTLV-IIIB), tunicamycin severely inhibited the glycosylation of envelope proteins. Deoxynojirimycin, an inhibitor of glucosidase I in the rough endoplasmic reticulum, inhibited the proteolytic processing of gp 160, whereas no such effect was noted with either deoxymannojirimycin or swainsonine, inhibitors of mannosidase I and II, respectively, in the Golgi complex. The processed gp120 and gp41 synthesized in the presence of deoxymannojirimycin were found to contain mannose-rich oligosaccharide cores as evidenced by their susceptibility to endoglycosidase H digestion. The formation of syncytia normally observed when CEM cells are cocultured with HIV-1-infected cells was markedly inhibited in the presence of deoxynojirimycin, but such inhibition was not observed in cells treated with deoxymannojirimycin or swainsonine. The infectivity of virions released from MOLT-3/HTLV-IIIBcells treated with deoxynojirimycin or deoxymannojirimycin was significantly lower than the infectivity of virions released from untreated cells. On the other hand, treatment with swainsonine did not affect the infectivity of the progeny virus. These results suggest that the proteolytic processing of gp160 takes place in infected cells when the glycoprotein has mannose-rich oligosaccharide structures. Trimming of glucose residues and the primary trimming of mannose residues are necessary for the release of infectious virus.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.86.9.3384</identifier><identifier>PMID: 2541446</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>1-Deoxynojirimycin ; AIDS/HIV ; Alkaloids - pharmacology ; alpha-Glucosidases ; Biological and medical sciences ; Carbohydrates ; Cell Line ; Cultured cells ; Endoplasmic Reticulum - drug effects ; Endoplasmic Reticulum - metabolism ; Fundamental and applied biological sciences. Psychology ; Giant cells ; Glucosamine - analogs & derivatives ; Glucosamine - pharmacology ; Glycoproteins ; Glycoproteins - metabolism ; Glycoside Hydrolase Inhibitors ; Glycosylation ; Golgi apparatus ; Golgi Apparatus - drug effects ; Golgi Apparatus - metabolism ; HIV 1 ; HIV Antigens - metabolism ; HIV Envelope Protein gp120 ; HIV Envelope Protein gp160 ; HIV Envelope Protein gp41 ; HIV-1 - metabolism ; HIV-1 - pathogenicity ; human immunodeficiency virus 1 ; Mannose - metabolism ; Mannosidases - antagonists & inhibitors ; Medical sciences ; Microbiology ; Oligosaccharides ; Oligosaccharides - metabolism ; Protein precursors ; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains ; Retroviridae Proteins - metabolism ; Swainsonine ; Tunicamycin - pharmacology ; Viral Envelope Proteins - metabolism ; Virology ; Viruses</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1989-05, Vol.86 (9), p.3384-3388</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c583t-3001b82522396df67255af9c1994a518b7ff6c43cecc7da5cca37f69861333573</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/86/9.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/33873$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/33873$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19285132$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2541446$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pal, Ranajit</creatorcontrib><creatorcontrib>Hoke, George M.</creatorcontrib><creatorcontrib>Sarngadharan, M. G.</creatorcontrib><title>Role of Oligosaccharides in the Processing and Maturation of Envelope Glycoproteins of Human Immunodeficiency Virus Type 1</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) were studied in infected cells treated with inhibitors of oligosaccharide processing. In MOLT-3 cells chronically infected with HIV-1 (strain HTLV-IIIB), tunicamycin severely inhibited the glycosylation of envelope proteins. Deoxynojirimycin, an inhibitor of glucosidase I in the rough endoplasmic reticulum, inhibited the proteolytic processing of gp 160, whereas no such effect was noted with either deoxymannojirimycin or swainsonine, inhibitors of mannosidase I and II, respectively, in the Golgi complex. The processed gp120 and gp41 synthesized in the presence of deoxymannojirimycin were found to contain mannose-rich oligosaccharide cores as evidenced by their susceptibility to endoglycosidase H digestion. The formation of syncytia normally observed when CEM cells are cocultured with HIV-1-infected cells was markedly inhibited in the presence of deoxynojirimycin, but such inhibition was not observed in cells treated with deoxymannojirimycin or swainsonine. The infectivity of virions released from MOLT-3/HTLV-IIIBcells treated with deoxynojirimycin or deoxymannojirimycin was significantly lower than the infectivity of virions released from untreated cells. On the other hand, treatment with swainsonine did not affect the infectivity of the progeny virus. These results suggest that the proteolytic processing of gp160 takes place in infected cells when the glycoprotein has mannose-rich oligosaccharide structures. Trimming of glucose residues and the primary trimming of mannose residues are necessary for the release of infectious virus.</description><subject>1-Deoxynojirimycin</subject><subject>AIDS/HIV</subject><subject>Alkaloids - pharmacology</subject><subject>alpha-Glucosidases</subject><subject>Biological and medical sciences</subject><subject>Carbohydrates</subject><subject>Cell Line</subject><subject>Cultured cells</subject><subject>Endoplasmic Reticulum - drug effects</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Giant cells</subject><subject>Glucosamine - analogs & derivatives</subject><subject>Glucosamine - pharmacology</subject><subject>Glycoproteins</subject><subject>Glycoproteins - metabolism</subject><subject>Glycoside Hydrolase Inhibitors</subject><subject>Glycosylation</subject><subject>Golgi apparatus</subject><subject>Golgi Apparatus - drug effects</subject><subject>Golgi Apparatus - metabolism</subject><subject>HIV 1</subject><subject>HIV Antigens - metabolism</subject><subject>HIV Envelope Protein gp120</subject><subject>HIV Envelope Protein gp160</subject><subject>HIV Envelope Protein gp41</subject><subject>HIV-1 - metabolism</subject><subject>HIV-1 - pathogenicity</subject><subject>human immunodeficiency virus 1</subject><subject>Mannose - metabolism</subject><subject>Mannosidases - antagonists & inhibitors</subject><subject>Medical sciences</subject><subject>Microbiology</subject><subject>Oligosaccharides</subject><subject>Oligosaccharides - metabolism</subject><subject>Protein precursors</subject><subject>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</subject><subject>Retroviridae Proteins - metabolism</subject><subject>Swainsonine</subject><subject>Tunicamycin - pharmacology</subject><subject>Viral Envelope Proteins - metabolism</subject><subject>Virology</subject><subject>Viruses</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkbFv1DAYxS0EKteDlQEJyQvdEuw4TuyBoapKW6moCBVWy-fYd64cO9hOxfHXN9Edx7HA5OH93vP79AB4g1GJUUs-DF6mkjUlLwlh9TOwwIjjoqk5eg4WCFVtweqqfglOU3pACHHK0Ak4qWiN67pZgF9fg9MwGHjn7DokqdRGRtvpBK2HeaPhlxiUTsn6NZS-g59lHqPMNvjZdOkftQuDhlduq8IQQ9bWp1m5Hnvp4U3fjz502lhltVdb-N3GMcH77WTBr8ALI13Sr_fvEnz7dHl_cV3c3l3dXJzfFooykguCEF6xilYV4U1nmraiVBquMOe1pJitWmMaVROllWo7SZWSpDUNZw0mhNCWLMHHXe4wrnrdKe1zlE4M0fYybkWQVvyteLsR6_AoKtZiMvvP9v4Yfow6ZdHbpLRz0uswJtGyqQmt2X9BPN2A2dRqCcodqGJIKWpzKIORmFcV86qCNYKLedXJ8O74hAO-n3HS3-91mZR0JkqvbPqTyitGMamOcub83_LxP2f_0oUZncv6Z57AtzvwIeUQD-QEtYQ8AVzHzaE</recordid><startdate>19890501</startdate><enddate>19890501</enddate><creator>Pal, Ranajit</creator><creator>Hoke, George M.</creator><creator>Sarngadharan, M. G.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19890501</creationdate><title>Role of Oligosaccharides in the Processing and Maturation of Envelope Glycoproteins of Human Immunodeficiency Virus Type 1</title><author>Pal, Ranajit ; Hoke, George M. ; Sarngadharan, M. G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c583t-3001b82522396df67255af9c1994a518b7ff6c43cecc7da5cca37f69861333573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>1-Deoxynojirimycin</topic><topic>AIDS/HIV</topic><topic>Alkaloids - pharmacology</topic><topic>alpha-Glucosidases</topic><topic>Biological and medical sciences</topic><topic>Carbohydrates</topic><topic>Cell Line</topic><topic>Cultured cells</topic><topic>Endoplasmic Reticulum - drug effects</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Giant cells</topic><topic>Glucosamine - analogs & derivatives</topic><topic>Glucosamine - pharmacology</topic><topic>Glycoproteins</topic><topic>Glycoproteins - metabolism</topic><topic>Glycoside Hydrolase Inhibitors</topic><topic>Glycosylation</topic><topic>Golgi apparatus</topic><topic>Golgi Apparatus - drug effects</topic><topic>Golgi Apparatus - metabolism</topic><topic>HIV 1</topic><topic>HIV Antigens - metabolism</topic><topic>HIV Envelope Protein gp120</topic><topic>HIV Envelope Protein gp160</topic><topic>HIV Envelope Protein gp41</topic><topic>HIV-1 - metabolism</topic><topic>HIV-1 - pathogenicity</topic><topic>human immunodeficiency virus 1</topic><topic>Mannose - metabolism</topic><topic>Mannosidases - antagonists & inhibitors</topic><topic>Medical sciences</topic><topic>Microbiology</topic><topic>Oligosaccharides</topic><topic>Oligosaccharides - metabolism</topic><topic>Protein precursors</topic><topic>Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains</topic><topic>Retroviridae Proteins - metabolism</topic><topic>Swainsonine</topic><topic>Tunicamycin - pharmacology</topic><topic>Viral Envelope Proteins - metabolism</topic><topic>Virology</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pal, Ranajit</creatorcontrib><creatorcontrib>Hoke, George M.</creatorcontrib><creatorcontrib>Sarngadharan, M. G.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research 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>Pal, Ranajit</au><au>Hoke, George M.</au><au>Sarngadharan, M. G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Role of Oligosaccharides in the Processing and Maturation of Envelope Glycoproteins of Human Immunodeficiency Virus Type 1</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1989-05-01</date><risdate>1989</risdate><volume>86</volume><issue>9</issue><spage>3384</spage><epage>3388</epage><pages>3384-3388</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>The processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) were studied in infected cells treated with inhibitors of oligosaccharide processing. In MOLT-3 cells chronically infected with HIV-1 (strain HTLV-IIIB), tunicamycin severely inhibited the glycosylation of envelope proteins. Deoxynojirimycin, an inhibitor of glucosidase I in the rough endoplasmic reticulum, inhibited the proteolytic processing of gp 160, whereas no such effect was noted with either deoxymannojirimycin or swainsonine, inhibitors of mannosidase I and II, respectively, in the Golgi complex. The processed gp120 and gp41 synthesized in the presence of deoxymannojirimycin were found to contain mannose-rich oligosaccharide cores as evidenced by their susceptibility to endoglycosidase H digestion. The formation of syncytia normally observed when CEM cells are cocultured with HIV-1-infected cells was markedly inhibited in the presence of deoxynojirimycin, but such inhibition was not observed in cells treated with deoxymannojirimycin or swainsonine. The infectivity of virions released from MOLT-3/HTLV-IIIBcells treated with deoxynojirimycin or deoxymannojirimycin was significantly lower than the infectivity of virions released from untreated cells. On the other hand, treatment with swainsonine did not affect the infectivity of the progeny virus. These results suggest that the proteolytic processing of gp160 takes place in infected cells when the glycoprotein has mannose-rich oligosaccharide structures. Trimming of glucose residues and the primary trimming of mannose residues are necessary for the release of infectious virus.</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>2541446</pmid><doi>10.1073/pnas.86.9.3384</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1989-05, Vol.86 (9), p.3384-3388 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_86_9_3384 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | 1-Deoxynojirimycin AIDS/HIV Alkaloids - pharmacology alpha-Glucosidases Biological and medical sciences Carbohydrates Cell Line Cultured cells Endoplasmic Reticulum - drug effects Endoplasmic Reticulum - metabolism Fundamental and applied biological sciences. Psychology Giant cells Glucosamine - analogs & derivatives Glucosamine - pharmacology Glycoproteins Glycoproteins - metabolism Glycoside Hydrolase Inhibitors Glycosylation Golgi apparatus Golgi Apparatus - drug effects Golgi Apparatus - metabolism HIV 1 HIV Antigens - metabolism HIV Envelope Protein gp120 HIV Envelope Protein gp160 HIV Envelope Protein gp41 HIV-1 - metabolism HIV-1 - pathogenicity human immunodeficiency virus 1 Mannose - metabolism Mannosidases - antagonists & inhibitors Medical sciences Microbiology Oligosaccharides Oligosaccharides - metabolism Protein precursors Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Retroviridae Proteins - metabolism Swainsonine Tunicamycin - pharmacology Viral Envelope Proteins - metabolism Virology Viruses |
| title | Role of Oligosaccharides in the Processing and Maturation of Envelope Glycoproteins of Human Immunodeficiency Virus Type 1 |
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