Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus
Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributa...
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| Veröffentlicht in: | Pathogens and global health 2012-03, Vol.106 (1), p.12-19 |
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| creator | Ammendolia, Maria Grazia Agamennone, Mariangela Pietrantoni, Agostina Lannutti, Fabio Siciliano, Rosa Anna De Giulio, Beatrice Amici, Carla Superti, Fabiana |
| description | Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA
2
region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics. |
| doi_str_mv | 10.1179/2047773212Y.0000000004 |
| format | Article |
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2
region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics.</description><identifier>ISSN: 2047-7724</identifier><identifier>EISSN: 2047-7732</identifier><identifier>DOI: 10.1179/2047773212Y.0000000004</identifier><identifier>PMID: 22595270</identifier><language>eng</language><publisher>London: Taylor & Francis</publisher><subject>Amino Acid Sequence ; Animals ; Antiviral ; Antiviral Agents - metabolism ; Antiviral Agents - pharmacology ; Biological and medical sciences ; Bovine lactoferrin ; C-lobe ; Cells, Cultured ; Dogs ; Drug Evaluation, Preclinical - methods ; General aspects ; Hemagglutinins - metabolism ; Human viral diseases ; Infectious diseases ; Influenza ; Influenza virus ; Lactoferrin - genetics ; Lactoferrin - metabolism ; Lactoferrin - pharmacology ; Medical sciences ; Molecular Sequence Data ; Original ; Orthomyxoviridae - drug effects ; Orthomyxoviridae - metabolism ; Peptide Fragments - genetics ; Peptide Fragments - metabolism ; Peptide Fragments - pharmacology ; Peptides ; Protein Binding ; Sequence Alignment ; Viral diseases ; Viral diseases of the respiratory system and ent viral diseases</subject><ispartof>Pathogens and global health, 2012-03, Vol.106 (1), p.12-19</ispartof><rights>W. S. Maney & Ltd 2012 2012</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c535t-b2f1b7a428c7485af544bf4e053aba8b0b53363af46880319e7ba65343e121df3</citedby><cites>FETCH-LOGICAL-c535t-b2f1b7a428c7485af544bf4e053aba8b0b53363af46880319e7ba65343e121df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4001507/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4001507/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=26429852$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22595270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ammendolia, Maria Grazia</creatorcontrib><creatorcontrib>Agamennone, Mariangela</creatorcontrib><creatorcontrib>Pietrantoni, Agostina</creatorcontrib><creatorcontrib>Lannutti, Fabio</creatorcontrib><creatorcontrib>Siciliano, Rosa Anna</creatorcontrib><creatorcontrib>De Giulio, Beatrice</creatorcontrib><creatorcontrib>Amici, Carla</creatorcontrib><creatorcontrib>Superti, Fabiana</creatorcontrib><title>Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus</title><title>Pathogens and global health</title><addtitle>Pathog Glob Health</addtitle><description>Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA
2
region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antiviral</subject><subject>Antiviral Agents - metabolism</subject><subject>Antiviral Agents - pharmacology</subject><subject>Biological and medical sciences</subject><subject>Bovine lactoferrin</subject><subject>C-lobe</subject><subject>Cells, Cultured</subject><subject>Dogs</subject><subject>Drug Evaluation, Preclinical - methods</subject><subject>General aspects</subject><subject>Hemagglutinins - metabolism</subject><subject>Human viral diseases</subject><subject>Infectious diseases</subject><subject>Influenza</subject><subject>Influenza virus</subject><subject>Lactoferrin - genetics</subject><subject>Lactoferrin - metabolism</subject><subject>Lactoferrin - pharmacology</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Original</subject><subject>Orthomyxoviridae - drug effects</subject><subject>Orthomyxoviridae - metabolism</subject><subject>Peptide Fragments - genetics</subject><subject>Peptide Fragments - metabolism</subject><subject>Peptide Fragments - pharmacology</subject><subject>Peptides</subject><subject>Protein Binding</subject><subject>Sequence Alignment</subject><subject>Viral diseases</subject><subject>Viral diseases of the respiratory system and ent viral diseases</subject><issn>2047-7724</issn><issn>2047-7732</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUtv1TAQhS0EotWlf6HKBolNip9xskEqFQWkSmxg0ZU1TsbUyImDndyq_Pomuo-WFXhjj843R8c6hJwzesGYbt5zKrXWgjN-e0EPR74gp6tQrsrL45vLE3KW868VqRTTnL8mJ5yrRnFNT8ntx7j1AxYB2ik6TMkPZYfJb7ErRhwn32EuIBdD3GIobIrQlXnEdkpzX_jhzls_xZSL6JbJhRmHP1BsfZrzG_LKQch4tr835Mf1p-9XX8qbb5-_Xl3elK0Saiotd8xqkLxutawVOCWldRKpEmChttQqISoBTlZ1TQVrUFuolJACGWedExvyYec7zrbHrsVhShDMmHwP6cFE8OZvZfB35mfcGkkpU1QvBu_2Bin-njFPpve5xRBgwDhnw4SsZc2V-g90dWwqvYTfkGqHtinmnNAdEzFq1hbNsxbNU4vL4vnz_xzXDp0twNs9ALmF4BIMrc9PXCV5Uyu-cJc7bikmph7uYwqdmeAhxHRYEv8I8wj3Proh</recordid><startdate>20120301</startdate><enddate>20120301</enddate><creator>Ammendolia, Maria Grazia</creator><creator>Agamennone, Mariangela</creator><creator>Pietrantoni, Agostina</creator><creator>Lannutti, Fabio</creator><creator>Siciliano, Rosa Anna</creator><creator>De Giulio, Beatrice</creator><creator>Amici, Carla</creator><creator>Superti, Fabiana</creator><general>Taylor & Francis</general><general>Maney</general><general>Maney Publishing</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>7X8</scope><scope>7U9</scope><scope>H94</scope><scope>M7N</scope><scope>5PM</scope></search><sort><creationdate>20120301</creationdate><title>Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus</title><author>Ammendolia, Maria Grazia ; Agamennone, Mariangela ; Pietrantoni, Agostina ; Lannutti, Fabio ; Siciliano, Rosa Anna ; De Giulio, Beatrice ; Amici, Carla ; Superti, Fabiana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c535t-b2f1b7a428c7485af544bf4e053aba8b0b53363af46880319e7ba65343e121df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antiviral</topic><topic>Antiviral Agents - metabolism</topic><topic>Antiviral Agents - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Bovine lactoferrin</topic><topic>C-lobe</topic><topic>Cells, Cultured</topic><topic>Dogs</topic><topic>Drug Evaluation, Preclinical - methods</topic><topic>General aspects</topic><topic>Hemagglutinins - metabolism</topic><topic>Human viral diseases</topic><topic>Infectious diseases</topic><topic>Influenza</topic><topic>Influenza virus</topic><topic>Lactoferrin - genetics</topic><topic>Lactoferrin - metabolism</topic><topic>Lactoferrin - pharmacology</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Original</topic><topic>Orthomyxoviridae - drug effects</topic><topic>Orthomyxoviridae - metabolism</topic><topic>Peptide Fragments - genetics</topic><topic>Peptide Fragments - metabolism</topic><topic>Peptide Fragments - pharmacology</topic><topic>Peptides</topic><topic>Protein Binding</topic><topic>Sequence Alignment</topic><topic>Viral diseases</topic><topic>Viral diseases of the respiratory system and ent viral diseases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ammendolia, Maria Grazia</creatorcontrib><creatorcontrib>Agamennone, Mariangela</creatorcontrib><creatorcontrib>Pietrantoni, Agostina</creatorcontrib><creatorcontrib>Lannutti, Fabio</creatorcontrib><creatorcontrib>Siciliano, Rosa Anna</creatorcontrib><creatorcontrib>De Giulio, Beatrice</creatorcontrib><creatorcontrib>Amici, Carla</creatorcontrib><creatorcontrib>Superti, Fabiana</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>MEDLINE - Academic</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Pathogens and global health</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ammendolia, Maria Grazia</au><au>Agamennone, Mariangela</au><au>Pietrantoni, Agostina</au><au>Lannutti, Fabio</au><au>Siciliano, Rosa Anna</au><au>De Giulio, Beatrice</au><au>Amici, Carla</au><au>Superti, Fabiana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus</atitle><jtitle>Pathogens and global health</jtitle><addtitle>Pathog Glob Health</addtitle><date>2012-03-01</date><risdate>2012</risdate><volume>106</volume><issue>1</issue><spage>12</spage><epage>19</epage><pages>12-19</pages><issn>2047-7724</issn><eissn>2047-7732</eissn><abstract>Bovine lactoferrin (bLf) is a multifunctional glycoprotein that plays an important role in innate immunity against infections, including influenza. Here we have dissected bLf into its C- and N-lobes and show that inhibition of influenza virus hemagglutination and cell infection is entirely attributable to the C-lobe and that all major virus subtypes, including H1N1 and H3N2, are inhibited. By far-western blotting and sequencing studies, we demonstrate that bLf C-lobe strongly binds to the HA
2
region of viral hemagglutinin, precisely the highly conserved region containing the fusion peptide. By molecular docking studies, three C-lobe fragments were identified which inhibited virus hemagglutination and infection at fentomolar concentration range. Besides contributing to explain the broad anti-influenza activity of bLf, our findings lay the foundations for exploiting bLf fragments as source of potential anti-influenza therapeutics.</abstract><cop>London</cop><pub>Taylor & Francis</pub><pmid>22595270</pmid><doi>10.1179/2047773212Y.0000000004</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Antiviral Antiviral Agents - metabolism Antiviral Agents - pharmacology Biological and medical sciences Bovine lactoferrin C-lobe Cells, Cultured Dogs Drug Evaluation, Preclinical - methods General aspects Hemagglutinins - metabolism Human viral diseases Infectious diseases Influenza Influenza virus Lactoferrin - genetics Lactoferrin - metabolism Lactoferrin - pharmacology Medical sciences Molecular Sequence Data Original Orthomyxoviridae - drug effects Orthomyxoviridae - metabolism Peptide Fragments - genetics Peptide Fragments - metabolism Peptide Fragments - pharmacology Peptides Protein Binding Sequence Alignment Viral diseases Viral diseases of the respiratory system and ent viral diseases |
| title | Bovine lactoferrin-derived peptides as novel broad-spectrum inhibitors of influenza virus |
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