Effects of Glycosylation on the Properties and Functions of Influenza Virus Hemagglutinin
The influenza virus A hemagglutinin (HA) is a trimeric glycoprotein that contains 3–9 N-linked glycosylation sequons per subunit, depending on the strain. The location of these sites is determined by the nucleotide sequence of the HA gene, and, since the viral genome is replicated by an errorprone R...
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| Veröffentlicht in: | The Journal of infectious diseases 1997-08, Vol.176 (Supplement-1), p.S24-S28 |
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| container_title | The Journal of infectious diseases |
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| creator | Schulze, Irene T. |
| description | The influenza virus A hemagglutinin (HA) is a trimeric glycoprotein that contains 3–9 N-linked glycosylation sequons per subunit, depending on the strain. The location of these sites is determined by the nucleotide sequence of the HA gene, and, since the viral genome is replicated by an errorprone RNA polymerase, mutations, which add or remove glycosylation sites, occur at a high frequency. Mutations that are not lethal to the virus add to the structural diversity of the virus population. Factors that determine the glycosylation of the HA are reviewed herein, as are the effects of host-specific glycosylation on receptor binding, fusion activity, and antigenic properties of the virus. Effects of host-specific glycosylation and selection on virulence and on vaccine efficacy and surveillance are discussed. In addition, inadequacies in our understanding of HA glycosylation and its effects on host range are emphasized. |
| doi_str_mv | 10.1086/514170 |
| format | Article |
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The location of these sites is determined by the nucleotide sequence of the HA gene, and, since the viral genome is replicated by an errorprone RNA polymerase, mutations, which add or remove glycosylation sites, occur at a high frequency. Mutations that are not lethal to the virus add to the structural diversity of the virus population. Factors that determine the glycosylation of the HA are reviewed herein, as are the effects of host-specific glycosylation on receptor binding, fusion activity, and antigenic properties of the virus. Effects of host-specific glycosylation and selection on virulence and on vaccine efficacy and surveillance are discussed. In addition, inadequacies in our understanding of HA glycosylation and its effects on host range are emphasized.</description><identifier>ISSN: 0022-1899</identifier><identifier>EISSN: 1537-6613</identifier><identifier>DOI: 10.1086/514170</identifier><identifier>PMID: 9240690</identifier><identifier>CODEN: JIDIAQ</identifier><language>eng</language><publisher>Chicago, IL: The University of Chicago Press</publisher><subject>Animals ; Biological and medical sciences ; Cell growth ; Fundamental and applied biological sciences. Psychology ; Glycosylation ; Hemagglutinin Glycoproteins, Influenza Virus - chemistry ; Hemagglutinin Glycoproteins, Influenza Virus - metabolism ; Human growth ; Humans ; Influenza A virus ; Microbiology ; Oligosaccharides ; Orthomyxoviridae ; Orthomyxoviridae - pathogenicity ; Receptors ; Structure-Activity Relationship ; Vaccination ; Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies ; Virology ; Virulence ; Viruses</subject><ispartof>The Journal of infectious diseases, 1997-08, Vol.176 (Supplement-1), p.S24-S28</ispartof><rights>1997 INIST-CNRS</rights><rights>Copyright University of Chicago, acting through its Press Aug 1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4340-53fb0a73d19a067941b8c258b1074f1661dbc0676d979c3468e0807868c8bc923</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/30106832$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/30106832$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>309,310,314,776,780,785,786,799,23909,23910,25118,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2793263$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9240690$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Schulze, Irene T.</creatorcontrib><title>Effects of Glycosylation on the Properties and Functions of Influenza Virus Hemagglutinin</title><title>The Journal of infectious diseases</title><addtitle>J Infect Dis</addtitle><description>The influenza virus A hemagglutinin (HA) is a trimeric glycoprotein that contains 3–9 N-linked glycosylation sequons per subunit, depending on the strain. The location of these sites is determined by the nucleotide sequence of the HA gene, and, since the viral genome is replicated by an errorprone RNA polymerase, mutations, which add or remove glycosylation sites, occur at a high frequency. Mutations that are not lethal to the virus add to the structural diversity of the virus population. Factors that determine the glycosylation of the HA are reviewed herein, as are the effects of host-specific glycosylation on receptor binding, fusion activity, and antigenic properties of the virus. Effects of host-specific glycosylation and selection on virulence and on vaccine efficacy and surveillance are discussed. In addition, inadequacies in our understanding of HA glycosylation and its effects on host range are emphasized.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell growth</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycosylation</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - metabolism</subject><subject>Human growth</subject><subject>Humans</subject><subject>Influenza A virus</subject><subject>Microbiology</subject><subject>Oligosaccharides</subject><subject>Orthomyxoviridae</subject><subject>Orthomyxoviridae - pathogenicity</subject><subject>Receptors</subject><subject>Structure-Activity Relationship</subject><subject>Vaccination</subject><subject>Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies</subject><subject>Virology</subject><subject>Virulence</subject><subject>Viruses</subject><issn>0022-1899</issn><issn>1537-6613</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV1rFDEUhoModV31HwiDiHejJ9_JpZR2t1hQsH71JmQySZ11NtkmM-D213fWXbbgjRDIxfOcF855EXqJ4R0GJd5zzLCER2iGOZW1EJg-RjMAQmqstH6KnpWyAgBGhTxBJ5owEBpm6OdZCN4NpUqhWvRbl8q2t0OXYjW94ZevPue08XnofKlsbKvzMbod_jtwEUM_-nhnq29dHku19Gt7c9OPQxe7-Bw9CbYv_sXhn6Ov52dXp8v68tPi4vTDZe0YZVBzGhqwkrZYWxBSM9woR7hqMEgW8LRI27gJiFZL7SgTyoMCqYRyqnGa0Dl6u8_d5HQ7-jKYdVec73sbfRqLkRozTZX4r4gF4UxNF5qj1_-IqzTmOC1hCKEaYy75Q5rLqZTsg9nkbm3z1mAwu0bMvpFJfHVIG5u1b4_aoYKJvzlwW5ztQ7bRdeWoEakpEfQhZlWGlI-YAgah6O4M9Z53ZfB_jtzm30ZIKrlZ_rg26pqLq49fvpsFvQejZ6hO</recordid><startdate>199708</startdate><enddate>199708</enddate><creator>Schulze, Irene T.</creator><general>The University of Chicago Press</general><general>University of Chicago Press</general><general>Oxford University Press</general><scope>BSCLL</scope><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>K9.</scope><scope>NAPCQ</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>199708</creationdate><title>Effects of Glycosylation on the Properties and Functions of Influenza Virus Hemagglutinin</title><author>Schulze, Irene T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4340-53fb0a73d19a067941b8c258b1074f1661dbc0676d979c3468e0807868c8bc923</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell growth</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycosylation</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - metabolism</topic><topic>Human growth</topic><topic>Humans</topic><topic>Influenza A virus</topic><topic>Microbiology</topic><topic>Oligosaccharides</topic><topic>Orthomyxoviridae</topic><topic>Orthomyxoviridae - pathogenicity</topic><topic>Receptors</topic><topic>Structure-Activity Relationship</topic><topic>Vaccination</topic><topic>Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies</topic><topic>Virology</topic><topic>Virulence</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schulze, Irene T.</creatorcontrib><collection>Istex</collection><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>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Premium</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of infectious diseases</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schulze, Irene T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of Glycosylation on the Properties and Functions of Influenza Virus Hemagglutinin</atitle><jtitle>The Journal of infectious diseases</jtitle><addtitle>J Infect Dis</addtitle><date>1997-08</date><risdate>1997</risdate><volume>176</volume><issue>Supplement-1</issue><spage>S24</spage><epage>S28</epage><pages>S24-S28</pages><issn>0022-1899</issn><eissn>1537-6613</eissn><coden>JIDIAQ</coden><abstract>The influenza virus A hemagglutinin (HA) is a trimeric glycoprotein that contains 3–9 N-linked glycosylation sequons per subunit, depending on the strain. The location of these sites is determined by the nucleotide sequence of the HA gene, and, since the viral genome is replicated by an errorprone RNA polymerase, mutations, which add or remove glycosylation sites, occur at a high frequency. Mutations that are not lethal to the virus add to the structural diversity of the virus population. Factors that determine the glycosylation of the HA are reviewed herein, as are the effects of host-specific glycosylation on receptor binding, fusion activity, and antigenic properties of the virus. Effects of host-specific glycosylation and selection on virulence and on vaccine efficacy and surveillance are discussed. In addition, inadequacies in our understanding of HA glycosylation and its effects on host range are emphasized.</abstract><cop>Chicago, IL</cop><pub>The University of Chicago Press</pub><pmid>9240690</pmid><doi>10.1086/514170</doi><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0022-1899 |
| ispartof | The Journal of infectious diseases, 1997-08, Vol.176 (Supplement-1), p.S24-S28 |
| issn | 0022-1899 1537-6613 |
| language | eng |
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| source | Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current); MEDLINE |
| subjects | Animals Biological and medical sciences Cell growth Fundamental and applied biological sciences. Psychology Glycosylation Hemagglutinin Glycoproteins, Influenza Virus - chemistry Hemagglutinin Glycoproteins, Influenza Virus - metabolism Human growth Humans Influenza A virus Microbiology Oligosaccharides Orthomyxoviridae Orthomyxoviridae - pathogenicity Receptors Structure-Activity Relationship Vaccination Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies Virology Virulence Viruses |
| title | Effects of Glycosylation on the Properties and Functions of Influenza Virus Hemagglutinin |
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