Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide
Hemagglutinin (HA), the trimeric spike of influenza virus, catalyzes fusion of viral and cellular membranes. We have synthesized the anchoring peptide including the linker, transmembrane region and cytoplasmic tail (HA-TMR-CT) in a cell-free system. Furthermore, to mimic the palmitoylation of three...
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| Veröffentlicht in: | Protein engineering, design and selection design and selection, 2013-09, Vol.26 (9), p.547-552 |
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| container_title | Protein engineering, design and selection |
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| creator | Mineev, Konstantin S. Lyukmanova, Ekaterina N. Krabben, Ludwig Serebryakova, Marina V. Shulepko, Mikhail A. Arseniev, Alexander S. Kordyukova, Larisa V. Veit, Michael |
| description | Hemagglutinin (HA), the trimeric spike of influenza virus, catalyzes fusion of viral and cellular membranes. We have synthesized the anchoring peptide including the linker, transmembrane region and cytoplasmic tail (HA-TMR-CT) in a cell-free system. Furthermore, to mimic the palmitoylation of three conserved cysteines within the CT, we chemically alkylated HA-TMR-CT using hexadecyl-methanethiosulfonate. While the nuclear magnetic resonance spectroscopy showed pure and refolded peptides, the formation of multiple oligomers of higher order impeded further structural analysis. Circular dichroism spectroscopy of both alkylated and non-alkylated HA-TMR-CT revealed an α-helical secondary structure. No major impact of the fatty acids on the secondary structure was detected. |
| doi_str_mv | 10.1093/protein/gzt034 |
| format | Article |
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We have synthesized the anchoring peptide including the linker, transmembrane region and cytoplasmic tail (HA-TMR-CT) in a cell-free system. Furthermore, to mimic the palmitoylation of three conserved cysteines within the CT, we chemically alkylated HA-TMR-CT using hexadecyl-methanethiosulfonate. While the nuclear magnetic resonance spectroscopy showed pure and refolded peptides, the formation of multiple oligomers of higher order impeded further structural analysis. Circular dichroism spectroscopy of both alkylated and non-alkylated HA-TMR-CT revealed an α-helical secondary structure. No major impact of the fatty acids on the secondary structure was detected.</description><identifier>ISSN: 1741-0126</identifier><identifier>EISSN: 1741-0134</identifier><identifier>DOI: 10.1093/protein/gzt034</identifier><identifier>PMID: 23873663</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Alkylation ; Amino Acid Sequence ; Escherichia coli - metabolism ; Hemagglutinin Glycoproteins, Influenza Virus - biosynthesis ; Hemagglutinin Glycoproteins, Influenza Virus - chemistry ; Influenza A Virus, H7N1 Subtype - chemistry ; Influenza A Virus, H7N1 Subtype - genetics ; Lipoylation ; Mesylates - chemistry ; Molecular Mimicry ; Molecular Sequence Data ; Peptides - chemistry ; Peptides - metabolism ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><ispartof>Protein engineering, design and selection, 2013-09, Vol.26 (9), p.547-552</ispartof><rights>The Author 2013. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com 2013</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c369t-eee245ba496fdbfdbd2ec33248032cc71c646de9410f8b67704156712787d4e13</citedby><cites>FETCH-LOGICAL-c369t-eee245ba496fdbfdbd2ec33248032cc71c646de9410f8b67704156712787d4e13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1584,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23873663$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mineev, Konstantin S.</creatorcontrib><creatorcontrib>Lyukmanova, Ekaterina N.</creatorcontrib><creatorcontrib>Krabben, Ludwig</creatorcontrib><creatorcontrib>Serebryakova, Marina V.</creatorcontrib><creatorcontrib>Shulepko, Mikhail A.</creatorcontrib><creatorcontrib>Arseniev, Alexander S.</creatorcontrib><creatorcontrib>Kordyukova, Larisa V.</creatorcontrib><creatorcontrib>Veit, Michael</creatorcontrib><title>Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide</title><title>Protein engineering, design and selection</title><addtitle>Protein Eng Des Sel</addtitle><description>Hemagglutinin (HA), the trimeric spike of influenza virus, catalyzes fusion of viral and cellular membranes. We have synthesized the anchoring peptide including the linker, transmembrane region and cytoplasmic tail (HA-TMR-CT) in a cell-free system. Furthermore, to mimic the palmitoylation of three conserved cysteines within the CT, we chemically alkylated HA-TMR-CT using hexadecyl-methanethiosulfonate. While the nuclear magnetic resonance spectroscopy showed pure and refolded peptides, the formation of multiple oligomers of higher order impeded further structural analysis. Circular dichroism spectroscopy of both alkylated and non-alkylated HA-TMR-CT revealed an α-helical secondary structure. No major impact of the fatty acids on the secondary structure was detected.</description><subject>Alkylation</subject><subject>Amino Acid Sequence</subject><subject>Escherichia coli - metabolism</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - biosynthesis</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</subject><subject>Influenza A Virus, H7N1 Subtype - chemistry</subject><subject>Influenza A Virus, H7N1 Subtype - genetics</subject><subject>Lipoylation</subject><subject>Mesylates - chemistry</subject><subject>Molecular Mimicry</subject><subject>Molecular Sequence Data</subject><subject>Peptides - chemistry</subject><subject>Peptides - metabolism</subject><subject>Protein Folding</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><issn>1741-0126</issn><issn>1741-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtLw0AQxhdRbK1ePUqOeki7r26So4gvKHiwnsNmM0lXkk3cR8H-9a609ioMzDB88_HND6FrgucEF2wx2sGDNot25zHjJ2hKMk5STBg_Pc5UTNCFc58YU5ERco4mlOUZE4JN0frd26B8sLJLtNmC87qVXg8mGZq4aLoAZieTrbbBJRvoZdt2wWujTdJDX1lpIJVGbQarTZuMMHpdwyU6a2Tn4OrQZ-jj6XH98JKu3p5fH-5XqWKi8CkAUL6sJC9EU1exagqKMcpzzKhSGVGCixoKTnCTVyLLMCfL-AHN8qzmQNgM3e59I4WvELOXvXYKui6mGoIrCac5FXkR_WZovpcqOzhnoSlHq3tpv0uCy1-S5YFkuScZD24O3qHqoT7K_9BFwd1eMITxP7MfK66B_w</recordid><startdate>201309</startdate><enddate>201309</enddate><creator>Mineev, Konstantin S.</creator><creator>Lyukmanova, Ekaterina N.</creator><creator>Krabben, Ludwig</creator><creator>Serebryakova, Marina V.</creator><creator>Shulepko, Mikhail A.</creator><creator>Arseniev, Alexander S.</creator><creator>Kordyukova, Larisa V.</creator><creator>Veit, Michael</creator><general>Oxford University Press</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><scope>7X8</scope></search><sort><creationdate>201309</creationdate><title>Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide</title><author>Mineev, Konstantin S. ; Lyukmanova, Ekaterina N. ; Krabben, Ludwig ; Serebryakova, Marina V. ; Shulepko, Mikhail A. ; Arseniev, Alexander S. ; Kordyukova, Larisa V. ; Veit, Michael</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c369t-eee245ba496fdbfdbd2ec33248032cc71c646de9410f8b67704156712787d4e13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Alkylation</topic><topic>Amino Acid Sequence</topic><topic>Escherichia coli - metabolism</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - biosynthesis</topic><topic>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</topic><topic>Influenza A Virus, H7N1 Subtype - chemistry</topic><topic>Influenza A Virus, H7N1 Subtype - genetics</topic><topic>Lipoylation</topic><topic>Mesylates - chemistry</topic><topic>Molecular Mimicry</topic><topic>Molecular Sequence Data</topic><topic>Peptides - chemistry</topic><topic>Peptides - metabolism</topic><topic>Protein Folding</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mineev, Konstantin S.</creatorcontrib><creatorcontrib>Lyukmanova, Ekaterina N.</creatorcontrib><creatorcontrib>Krabben, Ludwig</creatorcontrib><creatorcontrib>Serebryakova, Marina V.</creatorcontrib><creatorcontrib>Shulepko, Mikhail A.</creatorcontrib><creatorcontrib>Arseniev, Alexander S.</creatorcontrib><creatorcontrib>Kordyukova, Larisa V.</creatorcontrib><creatorcontrib>Veit, Michael</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Protein engineering, design and selection</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mineev, Konstantin S.</au><au>Lyukmanova, Ekaterina N.</au><au>Krabben, Ludwig</au><au>Serebryakova, Marina V.</au><au>Shulepko, Mikhail A.</au><au>Arseniev, Alexander S.</au><au>Kordyukova, Larisa V.</au><au>Veit, Michael</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide</atitle><jtitle>Protein engineering, design and selection</jtitle><addtitle>Protein Eng Des Sel</addtitle><date>2013-09</date><risdate>2013</risdate><volume>26</volume><issue>9</issue><spage>547</spage><epage>552</epage><pages>547-552</pages><issn>1741-0126</issn><eissn>1741-0134</eissn><abstract>Hemagglutinin (HA), the trimeric spike of influenza virus, catalyzes fusion of viral and cellular membranes. We have synthesized the anchoring peptide including the linker, transmembrane region and cytoplasmic tail (HA-TMR-CT) in a cell-free system. Furthermore, to mimic the palmitoylation of three conserved cysteines within the CT, we chemically alkylated HA-TMR-CT using hexadecyl-methanethiosulfonate. While the nuclear magnetic resonance spectroscopy showed pure and refolded peptides, the formation of multiple oligomers of higher order impeded further structural analysis. Circular dichroism spectroscopy of both alkylated and non-alkylated HA-TMR-CT revealed an α-helical secondary structure. No major impact of the fatty acids on the secondary structure was detected.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>23873663</pmid><doi>10.1093/protein/gzt034</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Alkylation Amino Acid Sequence Escherichia coli - metabolism Hemagglutinin Glycoproteins, Influenza Virus - biosynthesis Hemagglutinin Glycoproteins, Influenza Virus - chemistry Influenza A Virus, H7N1 Subtype - chemistry Influenza A Virus, H7N1 Subtype - genetics Lipoylation Mesylates - chemistry Molecular Mimicry Molecular Sequence Data Peptides - chemistry Peptides - metabolism Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| title | Structural investigation of influenza virus hemagglutinin membrane-anchoring peptide |
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