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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Hapivirins and Diprovirins: Novel θ-Defensin Analogs With Potent Activity Against Influenza A Virus<sup><xref rid="FN4" ref-type="fn">a</xref></sup></title><author><name sortKey="Doss, Mona" sort="Doss, Mona" uniqKey="Doss M" first="Mona" last="Doss">Mona Doss</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Ruchala, Piotr" sort="Ruchala, Piotr" uniqKey="Ruchala P" first="Piotr" last="Ruchala">Piotr Ruchala</name><affiliation><nlm:aff id="A4">Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</nlm:aff></affiliation></author><author><name sortKey="Tecle, Tesfaldet" sort="Tecle, Tesfaldet" uniqKey="Tecle T" first="Tesfaldet" last="Tecle">Tesfaldet Tecle</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Gantz, Donald" sort="Gantz, Donald" uniqKey="Gantz D" first="Donald" last="Gantz">Donald Gantz</name><affiliation><nlm:aff id="A2">Department of Biophysics, Boston University School of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Verma, Anamika" sort="Verma, Anamika" uniqKey="Verma A" first="Anamika" last="Verma">Anamika Verma</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Hartshorn, Alex" sort="Hartshorn, Alex" uniqKey="Hartshorn A" first="Alex" last="Hartshorn">Alex Hartshorn</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Crouch, Erika C" sort="Crouch, Erika C" uniqKey="Crouch E" first="Erika C." last="Crouch">Erika C. Crouch</name><affiliation><nlm:aff id="A3">Washington University School of Medicine, Department of Pathology and Immunology, St. Louis, MO</nlm:aff></affiliation></author><author><name sortKey="Luong, Hai" sort="Luong, Hai" uniqKey="Luong H" first="Hai" last="Luong">Hai Luong</name><affiliation><nlm:aff id="A4">Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</nlm:aff></affiliation></author><author><name sortKey="Micewicz, Ewa D" sort="Micewicz, Ewa D" uniqKey="Micewicz E" first="Ewa D." last="Micewicz">Ewa D. Micewicz</name><affiliation><nlm:aff id="A4">Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</nlm:aff></affiliation></author><author><name sortKey="Lehrer, Robert I" sort="Lehrer, Robert I" uniqKey="Lehrer R" first="Robert I." last="Lehrer">Robert I. Lehrer</name><affiliation><nlm:aff id="A4">Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</nlm:aff></affiliation></author><author><name sortKey="Hartshorn, Kevan L" sort="Hartshorn, Kevan L" uniqKey="Hartshorn K" first="Kevan L." last="Hartshorn">Kevan L. Hartshorn</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22345650</idno><idno type="pmc">3294087</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3294087</idno><idno type="RBID">PMC:3294087</idno><idno type="doi">10.4049/jimmunol.1101335</idno><date when="2012">2012</date><idno type="wicri:Area/Pmc/Corpus">000C22</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000C22</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Hapivirins and Diprovirins: Novel θ-Defensin Analogs With Potent Activity Against Influenza A Virus<sup><xref rid="FN4" ref-type="fn">a</xref></sup></title><author><name sortKey="Doss, Mona" sort="Doss, Mona" uniqKey="Doss M" first="Mona" last="Doss">Mona Doss</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Ruchala, Piotr" sort="Ruchala, Piotr" uniqKey="Ruchala P" first="Piotr" last="Ruchala">Piotr Ruchala</name><affiliation><nlm:aff id="A4">Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</nlm:aff></affiliation></author><author><name sortKey="Tecle, Tesfaldet" sort="Tecle, Tesfaldet" uniqKey="Tecle T" first="Tesfaldet" last="Tecle">Tesfaldet Tecle</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Gantz, Donald" sort="Gantz, Donald" uniqKey="Gantz D" first="Donald" last="Gantz">Donald Gantz</name><affiliation><nlm:aff id="A2">Department of Biophysics, Boston University School of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Verma, Anamika" sort="Verma, Anamika" uniqKey="Verma A" first="Anamika" last="Verma">Anamika Verma</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Hartshorn, Alex" sort="Hartshorn, Alex" uniqKey="Hartshorn A" first="Alex" last="Hartshorn">Alex Hartshorn</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author><author><name sortKey="Crouch, Erika C" sort="Crouch, Erika C" uniqKey="Crouch E" first="Erika C." last="Crouch">Erika C. Crouch</name><affiliation><nlm:aff id="A3">Washington University School of Medicine, Department of Pathology and Immunology, St. Louis, MO</nlm:aff></affiliation></author><author><name sortKey="Luong, Hai" sort="Luong, Hai" uniqKey="Luong H" first="Hai" last="Luong">Hai Luong</name><affiliation><nlm:aff id="A4">Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</nlm:aff></affiliation></author><author><name sortKey="Micewicz, Ewa D" sort="Micewicz, Ewa D" uniqKey="Micewicz E" first="Ewa D." last="Micewicz">Ewa D. Micewicz</name><affiliation><nlm:aff id="A4">Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</nlm:aff></affiliation></author><author><name sortKey="Lehrer, Robert I" sort="Lehrer, Robert I" uniqKey="Lehrer R" first="Robert I." last="Lehrer">Robert I. Lehrer</name><affiliation><nlm:aff id="A4">Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</nlm:aff></affiliation></author><author><name sortKey="Hartshorn, Kevan L" sort="Hartshorn, Kevan L" uniqKey="Hartshorn K" first="Kevan L." last="Hartshorn">Kevan L. Hartshorn</name><affiliation><nlm:aff id="A1">Boston University School of Medicine, Department of Medicine, Boston, MA</nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Immunology (Baltimore, Md. : 1950)</title><idno type="ISSN">0022-1767</idno><idno type="eISSN">1550-6606</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">θ-defensins are cyclic octadecapeptides found in non-human primates whose broad antiviral-spectrum includes HIV-1, HSV-1, SARS, and influenza A virus (IAV). We previously reported that synthetic θ-defensins called retrocyclins can neutralize and aggregate various strains of IAV and increase IAV uptake by neutrophils. This report describes two families of peptides, hapivirins (HpVs) and diprovirins (DpVs), whose design was inspired by retrocyclins. The goal was to develop smaller partially cyclic peptides that retain the antiviral activity of retrocyclins, while being easier to synthesize. The novel peptides also allowed for systemic substitution of key residues to evaluate the role of charge or hydrophobicity on antiviral activity. Seventy-two HpV or DpV peptides are described in this report, including several whose anti-IAV activity equals or exceeds that of normal α– or θ-defensins. Some of these also had strong antibacterial and antifungal activity. These new peptides were active against H3N2 and H1N1 strains of IAV. Structural features imparting strong antiviral activity were identified through iterative cycles of synthesis and testing. Our findings show the importance of hydrophobic residues for antiviral activity and show that pegylation, which often increases a peptide’s serum half-life <italic>in vivo</italic>, can increase the antiviral activity of DpVs. The new peptides acted at an early phase of viral infection and when combined with pulmonary surfactant protein D, their antiviral effects were additive. The peptides strongly increased neutrophil and macrophage uptake of IAV, while inhibiting monocyte cytokine generation. Development of modified θ– defensin analogues provides an approach for creating novel antiviral agents for IAV infections.</p></div></front></TEI><pmc article-type="research-article" xml:lang="en"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">2985117R</journal-id><journal-id journal-id-type="pubmed-jr-id">4816</journal-id><journal-id journal-id-type="nlm-ta">J Immunol</journal-id><journal-title-group><journal-title>Journal of Immunology (Baltimore, Md. : 1950)</journal-title></journal-title-group><issn pub-type="ppub">0022-1767</issn><issn pub-type="epub">1550-6606</issn></journal-meta><article-meta><article-id pub-id-type="pmid">22345650</article-id><article-id pub-id-type="pmc">3294087</article-id><article-id pub-id-type="doi">10.4049/jimmunol.1101335</article-id><article-id pub-id-type="manuscript">NIHMS349077</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Hapivirins and Diprovirins: Novel θ-Defensin Analogs With Potent Activity Against Influenza A Virus<sup><xref rid="FN4" ref-type="fn">a</xref></sup></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Doss</surname><given-names>Mona</given-names></name><xref rid="A1" ref-type="aff">1</xref><xref rid="FN2" ref-type="author-notes">*</xref></contrib><contrib contrib-type="author"><name><surname>Ruchala</surname><given-names>Piotr</given-names></name><xref rid="A4" ref-type="aff">4</xref><xref rid="FN2" ref-type="author-notes">*</xref></contrib><contrib contrib-type="author"><name><surname>Tecle</surname><given-names>Tesfaldet</given-names></name><xref rid="A1" ref-type="aff">1</xref></contrib><contrib contrib-type="author"><name><surname>Gantz</surname><given-names>Donald</given-names></name><xref rid="A2" ref-type="aff">2</xref></contrib><contrib contrib-type="author"><name><surname>Verma</surname><given-names>Anamika</given-names></name><xref rid="A1" ref-type="aff">1</xref></contrib><contrib contrib-type="author"><name><surname>Hartshorn</surname><given-names>Alex</given-names></name><xref rid="A1" ref-type="aff">1</xref></contrib><contrib contrib-type="author"><name><surname>Crouch</surname><given-names>Erika C.</given-names></name><xref rid="A3" ref-type="aff">3</xref></contrib><contrib contrib-type="author"><name><surname>Luong</surname><given-names>Hai</given-names></name><xref rid="A4" ref-type="aff">4</xref></contrib><contrib contrib-type="author"><name><surname>Micewicz</surname><given-names>Ewa D.</given-names></name><xref rid="A4" ref-type="aff">4</xref></contrib><contrib contrib-type="author"><name><surname>Lehrer</surname><given-names>Robert I.</given-names></name><xref rid="A4" ref-type="aff">4</xref></contrib><contrib contrib-type="author"><name><surname>Hartshorn</surname><given-names>Kevan L.</given-names></name><xref rid="A1" ref-type="aff">1</xref></contrib></contrib-group><aff id="A1"><label>1</label>Boston University School of Medicine, Department of Medicine, Boston, MA</aff><aff id="A2"><label>2</label>Department of Biophysics, Boston University School of Medicine, Boston, MA</aff><aff id="A3"><label>3</label>Washington University School of Medicine, Department of Pathology and Immunology, St. Louis, MO</aff><aff id="A4"><label>4</label>Department of Medicine, David Geffen School of Medicine at UCLA, Los Angeles, CA</aff><author-notes><corresp id="FN1">Address Correspondence: Kevan L. Hartshorn, MD, Boston University School of Medicine, EBRC 414, 650 Albany Street, Boston, MA 02118, Telephone 617 - 638-5638, FAX 617 - 638-7530, <email>khartsho@bu.edu</email></corresp><fn id="FN2" fn-type="equal"><label>*</label><p>Mona Doss and Piotr Ruchala contributed equally to this manuscript</p></fn><fn id="FN3" fn-type="present-address"><label>§</label><p>Current address: Astellas Pharma Inc., 2225 Colorado Avenue, Santa Monica, CA 90404</p></fn></author-notes><pub-date pub-type="nihms-submitted"><day>13</day><month>1</month><year>2012</year></pub-date><pub-date pub-type="epub"><day>15</day><month>2</month><year>2012</year></pub-date><pub-date pub-type="ppub"><day>15</day><month>3</month><year>2012</year></pub-date><pub-date pub-type="pmc-release"><day>15</day><month>3</month><year>2013</year></pub-date><volume>188</volume><issue>6</issue><fpage>2759</fpage><lpage>2768</lpage><abstract><p id="P1">θ-defensins are cyclic octadecapeptides found in non-human primates whose broad antiviral-spectrum includes HIV-1, HSV-1, SARS, and influenza A virus (IAV). We previously reported that synthetic θ-defensins called retrocyclins can neutralize and aggregate various strains of IAV and increase IAV uptake by neutrophils. This report describes two families of peptides, hapivirins (HpVs) and diprovirins (DpVs), whose design was inspired by retrocyclins. The goal was to develop smaller partially cyclic peptides that retain the antiviral activity of retrocyclins, while being easier to synthesize. The novel peptides also allowed for systemic substitution of key residues to evaluate the role of charge or hydrophobicity on antiviral activity. Seventy-two HpV or DpV peptides are described in this report, including several whose anti-IAV activity equals or exceeds that of normal α– or θ-defensins. Some of these also had strong antibacterial and antifungal activity. These new peptides were active against H3N2 and H1N1 strains of IAV. Structural features imparting strong antiviral activity were identified through iterative cycles of synthesis and testing. Our findings show the importance of hydrophobic residues for antiviral activity and show that pegylation, which often increases a peptide’s serum half-life <italic>in vivo</italic>, can increase the antiviral activity of DpVs. The new peptides acted at an early phase of viral infection and when combined with pulmonary surfactant protein D, their antiviral effects were additive. The peptides strongly increased neutrophil and macrophage uptake of IAV, while inhibiting monocyte cytokine generation. Development of modified θ– defensin analogues provides an approach for creating novel antiviral agents for IAV infections.</p></abstract><kwd-group><kwd>antiviral peptides</kwd><kwd>defensins</kwd><kwd>innate immunity</kwd><kwd>peptidomimetics</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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