A peptide-based approach to evaluate the adaptability of influenza A virus to humans based on its hemagglutinin proteolytic cleavage site
Identifieur interne : 000349 ( Main/Exploration ); précédent : 000348; suivant : 000350A peptide-based approach to evaluate the adaptability of influenza A virus to humans based on its hemagglutinin proteolytic cleavage site
Auteurs : Marco R. Straus [États-Unis] ; Gary R. Whittaker [États-Unis]Source :
- PLoS ONE [ 1932-6203 ] ; 2017.
Abstract
Cleavage activation of the hemagglutinin (HA) protein by host proteases is a crucial step in the infection process of influenza A viruses (IAV). However, IAV exists in eighteen different HA subtypes in nature and their cleavage sites vary considerably. There is uncertainty regarding which specific proteases activate a given HA in the human respiratory tract. Understanding the relationship between different HA subtypes and human-specific proteases will be valuable in assessing the pandemic potential of circulating viruses. Here we utilized fluorogenic peptides mimicking the HA cleavage motif of representative IAV strains causing disease in humans or of zoonotic/pandemic potential and tested them with a range of proteases known to be present in the human respiratory tract. Our results show that peptides from the H1, H2 and H3 subtypes are cleaved efficiently by a wide range of proteases including trypsin, matriptase, human airway tryptase (HAT), kallikrein-related peptidases 5 (KLK5) and 12 (KLK12) and plasmin. Regarding IAVs currently of concern for human adaptation, cleavage site peptides from H10 viruses showed very limited cleavage by respiratory tract proteases. Peptide mimics from H6 viruses showed broader cleavage by respiratory tract proteases, while H5, H7 and H9 subtypes showed variable cleavage; particularly matriptase appeared to be a key protease capable of activating IAVs. We also tested HA substrate specificity of Factor Xa, a protease required for HA cleavage in chicken embryos and relevant for influenza virus production in eggs. Overall our data provide novel tool allowing the assessment of human adaptation of IAV HA subtypes.
Url:
DOI: 10.1371/journal.pone.0174827
PubMed: 28358853
PubMed Central: 5373629
Affiliations:
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Straus</name><affiliation wicri:level="4"><nlm:aff id="aff001"><addr-line>Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York</wicri:regionArea><placeName><region type="state">État de New York</region><settlement type="city">Ithaca (New York)</settlement></placeName><orgName type="university">Université Cornell</orgName></affiliation><affiliation wicri:level="2"><nlm:aff id="aff002"><addr-line>New York Center of Excellence for Influenza Research and Surveillance, University of Rochester Medical Center, Rochester, New York, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>New York Center of Excellence for Influenza Research and Surveillance, University of Rochester Medical Center, Rochester, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author><author><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R." last="Whittaker">Gary R. Whittaker</name><affiliation wicri:level="4"><nlm:aff id="aff001"><addr-line>Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, New York</wicri:regionArea><placeName><region type="state">État de New York</region><settlement type="city">Ithaca (New York)</settlement></placeName><orgName type="university">Université Cornell</orgName></affiliation><affiliation wicri:level="2"><nlm:aff id="aff002"><addr-line>New York Center of Excellence for Influenza Research and Surveillance, University of Rochester Medical Center, Rochester, New York, United States of America</addr-line></nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>New York Center of Excellence for Influenza Research and Surveillance, University of Rochester Medical Center, Rochester, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Cleavage activation of the hemagglutinin (HA) protein by host proteases is a crucial step in the infection process of influenza A viruses (IAV). However, IAV exists in eighteen different HA subtypes in nature and their cleavage sites vary considerably. There is uncertainty regarding which specific proteases activate a given HA in the human respiratory tract. Understanding the relationship between different HA subtypes and human-specific proteases will be valuable in assessing the pandemic potential of circulating viruses. Here we utilized fluorogenic peptides mimicking the HA cleavage motif of representative IAV strains causing disease in humans or of zoonotic/pandemic potential and tested them with a range of proteases known to be present in the human respiratory tract. Our results show that peptides from the H1, H2 and H3 subtypes are cleaved efficiently by a wide range of proteases including trypsin, matriptase, human airway tryptase (HAT), kallikrein-related peptidases 5 (KLK5) and 12 (KLK12) and plasmin. Regarding IAVs currently of concern for human adaptation, cleavage site peptides from H10 viruses showed very limited cleavage by respiratory tract proteases. Peptide mimics from H6 viruses showed broader cleavage by respiratory tract proteases, while H5, H7 and H9 subtypes showed variable cleavage; particularly matriptase appeared to be a key protease capable of activating IAVs. We also tested HA substrate specificity of Factor Xa, a protease required for HA cleavage in chicken embryos and relevant for influenza virus production in eggs. 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Hatta</name></author><author><name sortKey="Watanabe, S" uniqKey="Watanabe S">S Watanabe</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Feldmann, A" uniqKey="Feldmann A">A Feldmann</name></author><author><name sortKey="Sch Fer, Mk" uniqKey="Sch Fer M">MK Schäfer</name></author><author><name sortKey="Garten, W" uniqKey="Garten W">W Garten</name></author><author><name sortKey="Klenk, H D" uniqKey="Klenk H">H-D Klenk</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region><settlement><li>Ithaca (New York)</li></settlement><orgName><li>Université Cornell</li></orgName></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="Straus, Marco R" sort="Straus, Marco R" uniqKey="Straus M" first="Marco R." last="Straus">Marco R. Straus</name></region><name sortKey="Straus, Marco R" sort="Straus, Marco R" uniqKey="Straus M" first="Marco R." last="Straus">Marco R. Straus</name><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R." last="Whittaker">Gary R. Whittaker</name><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R." last="Whittaker">Gary R. Whittaker</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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