The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus
In addition to their well-known antibacterial activity some antimicrobial peptides and proteins (AMPs) display also antiviral effects. A 27 aa peptide from the N-terminal part of human bactericidal/permeability-increasing protein (BPI) previously shown to harbour antibacterial activity inhibits the...
Gespeichert in:
| Veröffentlicht in: | PloS one 2016-06, Vol.11 (6), p.e0156929-e0156929 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | e0156929 |
|---|---|
| container_issue | 6 |
| container_start_page | e0156929 |
| container_title | PloS one |
| container_volume | 11 |
| creator | Pinkenburg, Olaf Meyer, Torben Bannert, Norbert Norley, Steven Bolte, Kathrin Czudai-Matwich, Volker Herold, Susanne Gessner, André Schnare, Markus |
| description | In addition to their well-known antibacterial activity some antimicrobial peptides and proteins (AMPs) display also antiviral effects. A 27 aa peptide from the N-terminal part of human bactericidal/permeability-increasing protein (BPI) previously shown to harbour antibacterial activity inhibits the infectivity of multiple Influenza A virus strains (H1N1, H3N2 and H5N1) the causing agent of the Influenza pneumonia. In contrast, the homologous murine BPI-peptide did not show activity against Influenza A virus. In addition human BPI-peptide inhibits the activation of immune cells mediated by Influenza A virus. By changing the human BPI-peptide to the sequence of the mouse homologous peptide the antiviral activity was completely abolished. Furthermore, the human BPI-peptide also inhibited the pathogenicity of the Vesicular Stomatitis Virus but failed to interfere with HIV and measles virus. Electron microscopy indicate that the human BPI-peptide interferes with the virus envelope and at high concentrations was able to destroy the particles completely. |
| doi_str_mv | 10.1371/journal.pone.0156929 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_plos_</sourceid><recordid>TN_cdi_plos_journals_1794120622</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A454994243</galeid><doaj_id>oai_doaj_org_article_8f84aa30cde24196a8d4163d7c9b99cc</doaj_id><sourcerecordid>A454994243</sourcerecordid><originalsourceid>FETCH-LOGICAL-c618t-65a03afd86f0c6e088756147ed235f518b9b52081d17b66a361afd4f154401613</originalsourceid><addsrcrecordid>eNqFkl1rFDEYhQdRbK3-A9EBQerFbvM1meRG2Ba1AwX3onobMpnMbpZsUpNMoV75082402VXBK_y9bwnb05OUbyGYA5xDS82fghO2vmdd3oOYEU54k-KU8gxmlEE8NOD-UnxIsYNABVmlD4vTlCNagwBOS1-3a51eT1spSsXLpmtUcG3RtpyGXzSxpWXUiUdjDKdtBdLHbZatsaa9DBrnApaRuNWe_j8ctl8KBu3Nq1JsUxZu3G9Vsnc54rS9-PSDtr9lOWi_G7CEF8Wz3ppo341jWfFt8-fbq-uZzdfvzRXi5uZopClGa0kwLLvGO2BohowVlcUklp3CFd9BVnL2woBBjtYt5RKTGGmSQ8rQgCkEJ8Vb3e6d9ZHMZkXBaw5gQhQhDLR7IjOy424C2Yrw4Pw0og_Gz6shAzJKKsF6xmREgPVaUQgp5J1BFLc1Yq3nCuVtT5Otw3tVndKuxSkPRI9PnFmLVb-XhDGSUVZFjifBIL_MeiYxNZEpa2VTvsh980Ay58IKP8_WvNqZDnO6Lu_0H8bMVErmd9qXO9zi2oUFQtSEc4JIqPW-wNqraVN6-jtkIx38RgkOzBHK8ag-70NEIgxyo9NiDHKYopyLntzaOG-6DG7-DewH---</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1794120622</pqid></control><display><type>article</type><title>The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus</title><source>Public Library of Science (PLoS) Journals Open Access</source><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Pinkenburg, Olaf ; Meyer, Torben ; Bannert, Norbert ; Norley, Steven ; Bolte, Kathrin ; Czudai-Matwich, Volker ; Herold, Susanne ; Gessner, André ; Schnare, Markus</creator><creatorcontrib>Pinkenburg, Olaf ; Meyer, Torben ; Bannert, Norbert ; Norley, Steven ; Bolte, Kathrin ; Czudai-Matwich, Volker ; Herold, Susanne ; Gessner, André ; Schnare, Markus</creatorcontrib><description>In addition to their well-known antibacterial activity some antimicrobial peptides and proteins (AMPs) display also antiviral effects. A 27 aa peptide from the N-terminal part of human bactericidal/permeability-increasing protein (BPI) previously shown to harbour antibacterial activity inhibits the infectivity of multiple Influenza A virus strains (H1N1, H3N2 and H5N1) the causing agent of the Influenza pneumonia. In contrast, the homologous murine BPI-peptide did not show activity against Influenza A virus. In addition human BPI-peptide inhibits the activation of immune cells mediated by Influenza A virus. By changing the human BPI-peptide to the sequence of the mouse homologous peptide the antiviral activity was completely abolished. Furthermore, the human BPI-peptide also inhibited the pathogenicity of the Vesicular Stomatitis Virus but failed to interfere with HIV and measles virus. Electron microscopy indicate that the human BPI-peptide interferes with the virus envelope and at high concentrations was able to destroy the particles completely.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0156929</identifier><identifier>PMID: 27273104</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Animals ; Antibacterial activity ; Antimicrobial agents ; Antimicrobial Cationic Peptides - metabolism ; Antimicrobial Cationic Peptides - pharmacology ; Antimicrobial peptides ; Antiviral activity ; Antiviral Agents - metabolism ; Antiviral Agents - pharmacology ; Avian influenza ; Bacteria ; Biology and life sciences ; Blood Proteins - metabolism ; Blood Proteins - pharmacology ; BPI protein ; Care and treatment ; Cells, Cultured ; Cricetinae ; Cytoplasm ; Dogs ; Electron microscopy ; Genomes ; Gram-negative bacteria ; HIV ; Homology ; Human immunodeficiency virus ; Humans ; Immune system ; Immunology ; Infectivity ; Influenza ; Influenza A ; Influenza A virus ; Influenza A virus - drug effects ; Influenza A virus - pathogenicity ; Influenza A Virus, H1N1 Subtype - drug effects ; Influenza A Virus, H1N1 Subtype - pathogenicity ; Influenza A Virus, H3N2 Subtype - drug effects ; Influenza A Virus, H3N2 Subtype - pathogenicity ; Influenza A Virus, H5N1 Subtype - drug effects ; Influenza A Virus, H5N1 Subtype - pathogenicity ; Lentivirus ; Madin Darby Canine Kidney Cells ; Measles ; Measles virus ; Medicine and health sciences ; Monoclonal antibodies ; Neutrophils ; Neutrophils - metabolism ; Orthomyxoviridae ; Pathogenicity ; Pathogens ; Peptide Fragments - pharmacology ; Peptides ; Permeability ; Physiological aspects ; Proteins ; Research and Analysis Methods ; Retroviridae ; Stomatitis ; Vesicular stomatitis virus ; Virus Replication - drug effects ; Viruses</subject><ispartof>PloS one, 2016-06, Vol.11 (6), p.e0156929-e0156929</ispartof><rights>COPYRIGHT 2016 Public Library of Science</rights><rights>2016 Pinkenburg et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2016 Pinkenburg et al 2016 Pinkenburg et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c618t-65a03afd86f0c6e088756147ed235f518b9b52081d17b66a361afd4f154401613</citedby><cites>FETCH-LOGICAL-c618t-65a03afd86f0c6e088756147ed235f518b9b52081d17b66a361afd4f154401613</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/PMC4894568/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4894568/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79569,79570</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27273104$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pinkenburg, Olaf</creatorcontrib><creatorcontrib>Meyer, Torben</creatorcontrib><creatorcontrib>Bannert, Norbert</creatorcontrib><creatorcontrib>Norley, Steven</creatorcontrib><creatorcontrib>Bolte, Kathrin</creatorcontrib><creatorcontrib>Czudai-Matwich, Volker</creatorcontrib><creatorcontrib>Herold, Susanne</creatorcontrib><creatorcontrib>Gessner, André</creatorcontrib><creatorcontrib>Schnare, Markus</creatorcontrib><title>The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>In addition to their well-known antibacterial activity some antimicrobial peptides and proteins (AMPs) display also antiviral effects. A 27 aa peptide from the N-terminal part of human bactericidal/permeability-increasing protein (BPI) previously shown to harbour antibacterial activity inhibits the infectivity of multiple Influenza A virus strains (H1N1, H3N2 and H5N1) the causing agent of the Influenza pneumonia. In contrast, the homologous murine BPI-peptide did not show activity against Influenza A virus. In addition human BPI-peptide inhibits the activation of immune cells mediated by Influenza A virus. By changing the human BPI-peptide to the sequence of the mouse homologous peptide the antiviral activity was completely abolished. Furthermore, the human BPI-peptide also inhibited the pathogenicity of the Vesicular Stomatitis Virus but failed to interfere with HIV and measles virus. Electron microscopy indicate that the human BPI-peptide interferes with the virus envelope and at high concentrations was able to destroy the particles completely.</description><subject>Animals</subject><subject>Antibacterial activity</subject><subject>Antimicrobial agents</subject><subject>Antimicrobial Cationic Peptides - metabolism</subject><subject>Antimicrobial Cationic Peptides - pharmacology</subject><subject>Antimicrobial peptides</subject><subject>Antiviral activity</subject><subject>Antiviral Agents - metabolism</subject><subject>Antiviral Agents - pharmacology</subject><subject>Avian influenza</subject><subject>Bacteria</subject><subject>Biology and life sciences</subject><subject>Blood Proteins - metabolism</subject><subject>Blood Proteins - pharmacology</subject><subject>BPI protein</subject><subject>Care and treatment</subject><subject>Cells, Cultured</subject><subject>Cricetinae</subject><subject>Cytoplasm</subject><subject>Dogs</subject><subject>Electron microscopy</subject><subject>Genomes</subject><subject>Gram-negative bacteria</subject><subject>HIV</subject><subject>Homology</subject><subject>Human immunodeficiency virus</subject><subject>Humans</subject><subject>Immune system</subject><subject>Immunology</subject><subject>Infectivity</subject><subject>Influenza</subject><subject>Influenza A</subject><subject>Influenza A virus</subject><subject>Influenza A virus - drug effects</subject><subject>Influenza A virus - pathogenicity</subject><subject>Influenza A Virus, H1N1 Subtype - drug effects</subject><subject>Influenza A Virus, H1N1 Subtype - pathogenicity</subject><subject>Influenza A Virus, H3N2 Subtype - drug effects</subject><subject>Influenza A Virus, H3N2 Subtype - pathogenicity</subject><subject>Influenza A Virus, H5N1 Subtype - drug effects</subject><subject>Influenza A Virus, H5N1 Subtype - pathogenicity</subject><subject>Lentivirus</subject><subject>Madin Darby Canine Kidney Cells</subject><subject>Measles</subject><subject>Measles virus</subject><subject>Medicine and health sciences</subject><subject>Monoclonal antibodies</subject><subject>Neutrophils</subject><subject>Neutrophils - metabolism</subject><subject>Orthomyxoviridae</subject><subject>Pathogenicity</subject><subject>Pathogens</subject><subject>Peptide Fragments - pharmacology</subject><subject>Peptides</subject><subject>Permeability</subject><subject>Physiological aspects</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>Retroviridae</subject><subject>Stomatitis</subject><subject>Vesicular stomatitis virus</subject><subject>Virus Replication - drug effects</subject><subject>Viruses</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqFkl1rFDEYhQdRbK3-A9EBQerFbvM1meRG2Ba1AwX3onobMpnMbpZsUpNMoV75082402VXBK_y9bwnb05OUbyGYA5xDS82fghO2vmdd3oOYEU54k-KU8gxmlEE8NOD-UnxIsYNABVmlD4vTlCNagwBOS1-3a51eT1spSsXLpmtUcG3RtpyGXzSxpWXUiUdjDKdtBdLHbZatsaa9DBrnApaRuNWe_j8ctl8KBu3Nq1JsUxZu3G9Vsnc54rS9-PSDtr9lOWi_G7CEF8Wz3ppo341jWfFt8-fbq-uZzdfvzRXi5uZopClGa0kwLLvGO2BohowVlcUklp3CFd9BVnL2woBBjtYt5RKTGGmSQ8rQgCkEJ8Vb3e6d9ZHMZkXBaw5gQhQhDLR7IjOy424C2Yrw4Pw0og_Gz6shAzJKKsF6xmREgPVaUQgp5J1BFLc1Yq3nCuVtT5Otw3tVndKuxSkPRI9PnFmLVb-XhDGSUVZFjifBIL_MeiYxNZEpa2VTvsh980Ay58IKP8_WvNqZDnO6Lu_0H8bMVErmd9qXO9zi2oUFQtSEc4JIqPW-wNqraVN6-jtkIx38RgkOzBHK8ag-70NEIgxyo9NiDHKYopyLntzaOG-6DG7-DewH---</recordid><startdate>20160606</startdate><enddate>20160606</enddate><creator>Pinkenburg, Olaf</creator><creator>Meyer, Torben</creator><creator>Bannert, Norbert</creator><creator>Norley, Steven</creator><creator>Bolte, Kathrin</creator><creator>Czudai-Matwich, Volker</creator><creator>Herold, Susanne</creator><creator>Gessner, André</creator><creator>Schnare, Markus</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PIMPY</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20160606</creationdate><title>The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus</title><author>Pinkenburg, Olaf ; Meyer, Torben ; Bannert, Norbert ; Norley, Steven ; Bolte, Kathrin ; Czudai-Matwich, Volker ; Herold, Susanne ; Gessner, André ; Schnare, Markus</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c618t-65a03afd86f0c6e088756147ed235f518b9b52081d17b66a361afd4f154401613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Antibacterial activity</topic><topic>Antimicrobial agents</topic><topic>Antimicrobial Cationic Peptides - metabolism</topic><topic>Antimicrobial Cationic Peptides - pharmacology</topic><topic>Antimicrobial peptides</topic><topic>Antiviral activity</topic><topic>Antiviral Agents - metabolism</topic><topic>Antiviral Agents - pharmacology</topic><topic>Avian influenza</topic><topic>Bacteria</topic><topic>Biology and life sciences</topic><topic>Blood Proteins - metabolism</topic><topic>Blood Proteins - pharmacology</topic><topic>BPI protein</topic><topic>Care and treatment</topic><topic>Cells, Cultured</topic><topic>Cricetinae</topic><topic>Cytoplasm</topic><topic>Dogs</topic><topic>Electron microscopy</topic><topic>Genomes</topic><topic>Gram-negative bacteria</topic><topic>HIV</topic><topic>Homology</topic><topic>Human immunodeficiency virus</topic><topic>Humans</topic><topic>Immune system</topic><topic>Immunology</topic><topic>Infectivity</topic><topic>Influenza</topic><topic>Influenza A</topic><topic>Influenza A virus</topic><topic>Influenza A virus - drug effects</topic><topic>Influenza A virus - pathogenicity</topic><topic>Influenza A Virus, H1N1 Subtype - drug effects</topic><topic>Influenza A Virus, H1N1 Subtype - pathogenicity</topic><topic>Influenza A Virus, H3N2 Subtype - drug effects</topic><topic>Influenza A Virus, H3N2 Subtype - pathogenicity</topic><topic>Influenza A Virus, H5N1 Subtype - drug effects</topic><topic>Influenza A Virus, H5N1 Subtype - pathogenicity</topic><topic>Lentivirus</topic><topic>Madin Darby Canine Kidney Cells</topic><topic>Measles</topic><topic>Measles virus</topic><topic>Medicine and health sciences</topic><topic>Monoclonal antibodies</topic><topic>Neutrophils</topic><topic>Neutrophils - metabolism</topic><topic>Orthomyxoviridae</topic><topic>Pathogenicity</topic><topic>Pathogens</topic><topic>Peptide Fragments - pharmacology</topic><topic>Peptides</topic><topic>Permeability</topic><topic>Physiological aspects</topic><topic>Proteins</topic><topic>Research and Analysis Methods</topic><topic>Retroviridae</topic><topic>Stomatitis</topic><topic>Vesicular stomatitis virus</topic><topic>Virus Replication - drug effects</topic><topic>Viruses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pinkenburg, Olaf</creatorcontrib><creatorcontrib>Meyer, Torben</creatorcontrib><creatorcontrib>Bannert, Norbert</creatorcontrib><creatorcontrib>Norley, Steven</creatorcontrib><creatorcontrib>Bolte, Kathrin</creatorcontrib><creatorcontrib>Czudai-Matwich, Volker</creatorcontrib><creatorcontrib>Herold, Susanne</creatorcontrib><creatorcontrib>Gessner, André</creatorcontrib><creatorcontrib>Schnare, Markus</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pinkenburg, Olaf</au><au>Meyer, Torben</au><au>Bannert, Norbert</au><au>Norley, Steven</au><au>Bolte, Kathrin</au><au>Czudai-Matwich, Volker</au><au>Herold, Susanne</au><au>Gessner, André</au><au>Schnare, Markus</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2016-06-06</date><risdate>2016</risdate><volume>11</volume><issue>6</issue><spage>e0156929</spage><epage>e0156929</epage><pages>e0156929-e0156929</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>In addition to their well-known antibacterial activity some antimicrobial peptides and proteins (AMPs) display also antiviral effects. A 27 aa peptide from the N-terminal part of human bactericidal/permeability-increasing protein (BPI) previously shown to harbour antibacterial activity inhibits the infectivity of multiple Influenza A virus strains (H1N1, H3N2 and H5N1) the causing agent of the Influenza pneumonia. In contrast, the homologous murine BPI-peptide did not show activity against Influenza A virus. In addition human BPI-peptide inhibits the activation of immune cells mediated by Influenza A virus. By changing the human BPI-peptide to the sequence of the mouse homologous peptide the antiviral activity was completely abolished. Furthermore, the human BPI-peptide also inhibited the pathogenicity of the Vesicular Stomatitis Virus but failed to interfere with HIV and measles virus. Electron microscopy indicate that the human BPI-peptide interferes with the virus envelope and at high concentrations was able to destroy the particles completely.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>27273104</pmid><doi>10.1371/journal.pone.0156929</doi><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2016-06, Vol.11 (6), p.e0156929-e0156929 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_1794120622 |
| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals Antibacterial activity Antimicrobial agents Antimicrobial Cationic Peptides - metabolism Antimicrobial Cationic Peptides - pharmacology Antimicrobial peptides Antiviral activity Antiviral Agents - metabolism Antiviral Agents - pharmacology Avian influenza Bacteria Biology and life sciences Blood Proteins - metabolism Blood Proteins - pharmacology BPI protein Care and treatment Cells, Cultured Cricetinae Cytoplasm Dogs Electron microscopy Genomes Gram-negative bacteria HIV Homology Human immunodeficiency virus Humans Immune system Immunology Infectivity Influenza Influenza A Influenza A virus Influenza A virus - drug effects Influenza A virus - pathogenicity Influenza A Virus, H1N1 Subtype - drug effects Influenza A Virus, H1N1 Subtype - pathogenicity Influenza A Virus, H3N2 Subtype - drug effects Influenza A Virus, H3N2 Subtype - pathogenicity Influenza A Virus, H5N1 Subtype - drug effects Influenza A Virus, H5N1 Subtype - pathogenicity Lentivirus Madin Darby Canine Kidney Cells Measles Measles virus Medicine and health sciences Monoclonal antibodies Neutrophils Neutrophils - metabolism Orthomyxoviridae Pathogenicity Pathogens Peptide Fragments - pharmacology Peptides Permeability Physiological aspects Proteins Research and Analysis Methods Retroviridae Stomatitis Vesicular stomatitis virus Virus Replication - drug effects Viruses |
| title | The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of Influenza A Virus |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T19%3A44%3A40IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Human%20Antimicrobial%20Protein%20Bactericidal/Permeability-Increasing%20Protein%20(BPI)%20Inhibits%20the%20Infectivity%20of%20Influenza%20A%20Virus&rft.jtitle=PloS%20one&rft.au=Pinkenburg,%20Olaf&rft.date=2016-06-06&rft.volume=11&rft.issue=6&rft.spage=e0156929&rft.epage=e0156929&rft.pages=e0156929-e0156929&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0156929&rft_dat=%3Cgale_plos_%3EA454994243%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1794120622&rft_id=info:pmid/27273104&rft_galeid=A454994243&rft_doaj_id=oai_doaj_org_article_8f84aa30cde24196a8d4163d7c9b99cc&rfr_iscdi=true |