The Carboxy-Terminal 18 Amino Acids of the Measles Virus Hemagglutinin Are Essential for Its Biological Function
The hemagglutinin (HA) glycoprotein encoded by measles virus (MV) is a type II integral membrane protein that is expressed at the infected cell surface. Genes encoding wild-type MV HA as well as two mutant HA proteins shortened at their carboxy-termini by either 18 (HAΔ18) or 223 (HAΔ223) amino acid...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1995-09, Vol.214 (3), p.1232-1238 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Blain, F. Liston, P. Briedis, D.J. |
| description | The hemagglutinin (HA) glycoprotein encoded by measles virus (MV) is a type II integral membrane protein that is expressed at the infected cell surface. Genes encoding wild-type MV HA as well as two mutant HA proteins shortened at their carboxy-termini by either 18 (HAΔ18) or 223 (HAΔ223) amino acids were constructed and studied in a transient expression system in COS cells. Under nonreducing conditions, assembly of HAΔ18 into homodimers was diminished while HAΔ223 remained in a monomeric form. Hemadsorption assays revealed that neither mutant was functional at the cell surface. These studies show that the carboxy-terminal ectodomain of the HA protein is essential to its proper folding and assembly into homodimers while its carboxy-terminal 18 amino acids are essential for the hemadsorption (receptor-binding) function of the protein. |
| doi_str_mv | 10.1006/bbrc.1995.2418 |
| format | Article |
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Genes encoding wild-type MV HA as well as two mutant HA proteins shortened at their carboxy-termini by either 18 (HAΔ18) or 223 (HAΔ223) amino acids were constructed and studied in a transient expression system in COS cells. Under nonreducing conditions, assembly of HAΔ18 into homodimers was diminished while HAΔ223 remained in a monomeric form. Hemadsorption assays revealed that neither mutant was functional at the cell surface. These studies show that the carboxy-terminal ectodomain of the HA protein is essential to its proper folding and assembly into homodimers while its carboxy-terminal 18 amino acids are essential for the hemadsorption (receptor-binding) function of the protein.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.1995.2418</identifier><identifier>PMID: 7575535</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Base Sequence ; Cell Line ; Cercopithecus aethiops ; Chymotrypsin ; Erythrocytes - immunology ; Hemagglutination ; Hemagglutinins, Viral - biosynthesis ; Hemagglutinins, Viral - chemistry ; Hemagglutinins, Viral - immunology ; Kidney ; Kinetics ; Macromolecular Substances ; Measles virus - immunology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptide Mapping ; Protein Folding ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - immunology ; Sequence Deletion ; Transfection ; Vero Cells</subject><ispartof>Biochemical and biophysical research communications, 1995-09, Vol.214 (3), p.1232-1238</ispartof><rights>1995 Academic Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-42cb16b57fe4a00f8101212e0eade549f7fefd3296ba11eba603f4fa8321a8223</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.1995.2418$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7575535$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Blain, F.</creatorcontrib><creatorcontrib>Liston, P.</creatorcontrib><creatorcontrib>Briedis, D.J.</creatorcontrib><title>The Carboxy-Terminal 18 Amino Acids of the Measles Virus Hemagglutinin Are Essential for Its Biological Function</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The hemagglutinin (HA) glycoprotein encoded by measles virus (MV) is a type II integral membrane protein that is expressed at the infected cell surface. Genes encoding wild-type MV HA as well as two mutant HA proteins shortened at their carboxy-termini by either 18 (HAΔ18) or 223 (HAΔ223) amino acids were constructed and studied in a transient expression system in COS cells. Under nonreducing conditions, assembly of HAΔ18 into homodimers was diminished while HAΔ223 remained in a monomeric form. Hemadsorption assays revealed that neither mutant was functional at the cell surface. These studies show that the carboxy-terminal ectodomain of the HA protein is essential to its proper folding and assembly into homodimers while its carboxy-terminal 18 amino acids are essential for the hemadsorption (receptor-binding) function of the protein.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Cell Line</subject><subject>Cercopithecus aethiops</subject><subject>Chymotrypsin</subject><subject>Erythrocytes - immunology</subject><subject>Hemagglutination</subject><subject>Hemagglutinins, Viral - biosynthesis</subject><subject>Hemagglutinins, Viral - chemistry</subject><subject>Hemagglutinins, Viral - immunology</subject><subject>Kidney</subject><subject>Kinetics</subject><subject>Macromolecular Substances</subject><subject>Measles virus - immunology</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Peptide Mapping</subject><subject>Protein Folding</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - immunology</subject><subject>Sequence Deletion</subject><subject>Transfection</subject><subject>Vero Cells</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1PwzAQhi0EKqWwsiH5DyT4nI8mY6haWqmIpSC2yHHOxSiJKztB9N_jqBUb053u_dDpIeQeWAiMpY9VZWUIeZ6EPIbsgkyB5SzgwOJLMmXeEfAcPq7JjXNfjAHEaT4hk3kyT5IomZLD7hPpQtjK_ByDHdpWd6KhkNHCb4YWUteOGkV7b3tB4Rp09F3bwdE1tmK_b4Zed7qjhUW6dA67Xvu8MpZuekeftGnMXkt_Wg2d7LXpbsmVEo3Du_OckbfVcrdYB9vX582i2AYyivI-iLmsIK2SucJYMKYyYMCBI0NRYxLnyguqjnieVgIAK5GySMVKZBEHkXEezUh46pXWOGdRlQerW2GPJbByJFeO5MqRXDmS84GHU-AwVC3Wf_YzKq9nJx39198abemkxk5irS3KvqyN_q_6FxGBfZc</recordid><startdate>19950925</startdate><enddate>19950925</enddate><creator>Blain, F.</creator><creator>Liston, P.</creator><creator>Briedis, D.J.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19950925</creationdate><title>The Carboxy-Terminal 18 Amino Acids of the Measles Virus Hemagglutinin Are Essential for Its Biological Function</title><author>Blain, F. ; Liston, P. ; Briedis, D.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-42cb16b57fe4a00f8101212e0eade549f7fefd3296ba11eba603f4fa8321a8223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Cell Line</topic><topic>Cercopithecus aethiops</topic><topic>Chymotrypsin</topic><topic>Erythrocytes - immunology</topic><topic>Hemagglutination</topic><topic>Hemagglutinins, Viral - biosynthesis</topic><topic>Hemagglutinins, Viral - chemistry</topic><topic>Hemagglutinins, Viral - immunology</topic><topic>Kidney</topic><topic>Kinetics</topic><topic>Macromolecular Substances</topic><topic>Measles virus - immunology</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Peptide Mapping</topic><topic>Protein Folding</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - immunology</topic><topic>Sequence Deletion</topic><topic>Transfection</topic><topic>Vero Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Blain, F.</creatorcontrib><creatorcontrib>Liston, P.</creatorcontrib><creatorcontrib>Briedis, D.J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Blain, F.</au><au>Liston, P.</au><au>Briedis, D.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Carboxy-Terminal 18 Amino Acids of the Measles Virus Hemagglutinin Are Essential for Its Biological Function</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1995-09-25</date><risdate>1995</risdate><volume>214</volume><issue>3</issue><spage>1232</spage><epage>1238</epage><pages>1232-1238</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The hemagglutinin (HA) glycoprotein encoded by measles virus (MV) is a type II integral membrane protein that is expressed at the infected cell surface. Genes encoding wild-type MV HA as well as two mutant HA proteins shortened at their carboxy-termini by either 18 (HAΔ18) or 223 (HAΔ223) amino acids were constructed and studied in a transient expression system in COS cells. Under nonreducing conditions, assembly of HAΔ18 into homodimers was diminished while HAΔ223 remained in a monomeric form. Hemadsorption assays revealed that neither mutant was functional at the cell surface. These studies show that the carboxy-terminal ectodomain of the HA protein is essential to its proper folding and assembly into homodimers while its carboxy-terminal 18 amino acids are essential for the hemadsorption (receptor-binding) function of the protein.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>7575535</pmid><doi>10.1006/bbrc.1995.2418</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1995-09, Vol.214 (3), p.1232-1238 |
| issn | 0006-291X 1090-2104 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Animals Base Sequence Cell Line Cercopithecus aethiops Chymotrypsin Erythrocytes - immunology Hemagglutination Hemagglutinins, Viral - biosynthesis Hemagglutinins, Viral - chemistry Hemagglutinins, Viral - immunology Kidney Kinetics Macromolecular Substances Measles virus - immunology Molecular Sequence Data Mutagenesis, Site-Directed Peptide Mapping Protein Folding Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - immunology Sequence Deletion Transfection Vero Cells |
| title | The Carboxy-Terminal 18 Amino Acids of the Measles Virus Hemagglutinin Are Essential for Its Biological Function |
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