Inhibition of sialidase activity as a therapeutic approach
Identifieur interne : 000F28 ( Ncbi/Merge ); précédent : 000F27; suivant : 000F29Inhibition of sialidase activity as a therapeutic approach
Auteurs : Victor Yu Glanz [Russie] ; Veronika A. Myasoedova ; Andrey V. Grechko [Russie] ; Alexander N. OrekhovSource :
- Drug Design, Development and Therapy [ 1177-8881 ] ; 2018.
Abstract
The demand for novel anti-influenza drugs persists, which is highlighted by the recent pandemics of influenza affecting thousands of people across the globe. One of the approaches to block the virus spreading is inhibiting viral sialidase (neuraminidase). This enzyme cleaves the sialic acid link between the newly formed virions and the host cell surface liberating the virions from the cell and maintaining the cycle of infection. Viral neuraminidases appear therefore as attractive therapeutic targets for preventing further spread of influenza infection. Compared to ion channel blockers that were the first approved anti-influenza drugs, neuraminidase inhibitors are well tolerated and target both influenza A and B viruses. Moreover, neuraminidase/sialidase inhibitors may be useful for managing some other human pathologies, such as cancer. In this review, we discuss the available knowledge on neuraminidase or sialidase inhibitors, their design, clinical application, and the current challenges.
Url:
DOI: 10.2147/DDDT.S176220
PubMed: 30349196
PubMed Central: 6186905
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Inhibition of sialidase activity as a therapeutic approach</title><author><name sortKey="Glanz, Victor Yu" sort="Glanz, Victor Yu" uniqKey="Glanz V" first="Victor Yu" last="Glanz">Victor Yu Glanz</name><affiliation wicri:level="1"><nlm:aff id="af1-dddt-12-3431">Department of Genetics, Cytology and Bioengineering, Faculty of Biology and Medicine, Voronezh State University, Voronezh, Russia</nlm:aff><country xml:lang="fr">Russie</country><wicri:regionArea>Department of Genetics, Cytology and Bioengineering, Faculty of Biology and Medicine, Voronezh State University, Voronezh</wicri:regionArea><wicri:noRegion>Voronezh</wicri:noRegion></affiliation></author><author><name sortKey="Myasoedova, Veronika A" sort="Myasoedova, Veronika A" uniqKey="Myasoedova V" first="Veronika A" last="Myasoedova">Veronika A. Myasoedova</name><affiliation><nlm:aff id="af2-dddt-12-3431">Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, Moscow, Russia,<email>a.h.opexob@gmail.com</email></nlm:aff></affiliation></author><author><name sortKey="Grechko, Andrey V" sort="Grechko, Andrey V" uniqKey="Grechko A" first="Andrey V" last="Grechko">Andrey V. Grechko</name><affiliation wicri:level="3"><nlm:aff id="af3-dddt-12-3431">Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology, Moscow, Russia</nlm:aff><country xml:lang="fr">Russie</country><wicri:regionArea>Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology, Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Orekhov, Alexander N" sort="Orekhov, Alexander N" uniqKey="Orekhov A" first="Alexander N" last="Orekhov">Alexander N. Orekhov</name><affiliation><nlm:aff id="af2-dddt-12-3431">Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, Moscow, Russia,<email>a.h.opexob@gmail.com</email></nlm:aff></affiliation><affiliation><nlm:aff id="af4-dddt-12-3431">Institute for Atherosclerosis Research, Skolkovo Innovative Center, Moscow, Russia,<email>a.h.opexob@gmail.com</email></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">30349196</idno><idno type="pmc">6186905</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6186905</idno><idno type="RBID">PMC:6186905</idno><idno type="doi">10.2147/DDDT.S176220</idno><date when="2018">2018</date><idno type="wicri:Area/Pmc/Corpus">000D21</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000D21</idno><idno type="wicri:Area/Pmc/Curation">000D21</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000D21</idno><idno type="wicri:Area/Pmc/Checkpoint">000130</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000130</idno><idno type="wicri:Area/Ncbi/Merge">000F28</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Inhibition of sialidase activity as a therapeutic approach</title><author><name sortKey="Glanz, Victor Yu" sort="Glanz, Victor Yu" uniqKey="Glanz V" first="Victor Yu" last="Glanz">Victor Yu Glanz</name><affiliation wicri:level="1"><nlm:aff id="af1-dddt-12-3431">Department of Genetics, Cytology and Bioengineering, Faculty of Biology and Medicine, Voronezh State University, Voronezh, Russia</nlm:aff><country xml:lang="fr">Russie</country><wicri:regionArea>Department of Genetics, Cytology and Bioengineering, Faculty of Biology and Medicine, Voronezh State University, Voronezh</wicri:regionArea><wicri:noRegion>Voronezh</wicri:noRegion></affiliation></author><author><name sortKey="Myasoedova, Veronika A" sort="Myasoedova, Veronika A" uniqKey="Myasoedova V" first="Veronika A" last="Myasoedova">Veronika A. Myasoedova</name><affiliation><nlm:aff id="af2-dddt-12-3431">Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, Moscow, Russia,<email>a.h.opexob@gmail.com</email></nlm:aff></affiliation></author><author><name sortKey="Grechko, Andrey V" sort="Grechko, Andrey V" uniqKey="Grechko A" first="Andrey V" last="Grechko">Andrey V. Grechko</name><affiliation wicri:level="3"><nlm:aff id="af3-dddt-12-3431">Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology, Moscow, Russia</nlm:aff><country xml:lang="fr">Russie</country><wicri:regionArea>Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology, Moscow</wicri:regionArea><placeName><settlement type="city">Moscou</settlement><region>District fédéral central</region></placeName></affiliation></author><author><name sortKey="Orekhov, Alexander N" sort="Orekhov, Alexander N" uniqKey="Orekhov A" first="Alexander N" last="Orekhov">Alexander N. Orekhov</name><affiliation><nlm:aff id="af2-dddt-12-3431">Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, Moscow, Russia,<email>a.h.opexob@gmail.com</email></nlm:aff></affiliation><affiliation><nlm:aff id="af4-dddt-12-3431">Institute for Atherosclerosis Research, Skolkovo Innovative Center, Moscow, Russia,<email>a.h.opexob@gmail.com</email></nlm:aff></affiliation></author></analytic><series><title level="j">Drug Design, Development and Therapy</title><idno type="eISSN">1177-8881</idno><imprint><date when="2018">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The demand for novel anti-influenza drugs persists, which is highlighted by the recent pandemics of influenza affecting thousands of people across the globe. One of the approaches to block the virus spreading is inhibiting viral sialidase (neuraminidase). This enzyme cleaves the sialic acid link between the newly formed virions and the host cell surface liberating the virions from the cell and maintaining the cycle of infection. Viral neuraminidases appear therefore as attractive therapeutic targets for preventing further spread of influenza infection. Compared to ion channel blockers that were the first approved anti-influenza drugs, neuraminidase inhibitors are well tolerated and target both influenza A and B viruses. Moreover, neuraminidase/sialidase inhibitors may be useful for managing some other human pathologies, such as cancer. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Drug Des Devel Ther</journal-id><journal-id journal-id-type="iso-abbrev">Drug Des Devel Ther</journal-id><journal-id journal-id-type="publisher-id">Drug Design, Development and Therapy</journal-id><journal-title-group><journal-title>Drug Design, Development and Therapy</journal-title></journal-title-group><issn pub-type="epub">1177-8881</issn><publisher><publisher-name>Dove Medical Press</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">30349196</article-id><article-id pub-id-type="pmc">6186905</article-id><article-id pub-id-type="doi">10.2147/DDDT.S176220</article-id><article-id pub-id-type="publisher-id">dddt-12-3431</article-id><article-categories><subj-group subj-group-type="heading"><subject>Review</subject></subj-group></article-categories><title-group><article-title>Inhibition of sialidase activity as a therapeutic approach</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Glanz</surname><given-names>Victor Yu</given-names></name><xref ref-type="aff" rid="af1-dddt-12-3431">1</xref></contrib><contrib contrib-type="author"><name><surname>Myasoedova</surname><given-names>Veronika A</given-names></name><xref ref-type="aff" rid="af2-dddt-12-3431">2</xref></contrib><contrib contrib-type="author"><name><surname>Grechko</surname><given-names>Andrey V</given-names></name><xref ref-type="aff" rid="af3-dddt-12-3431">3</xref></contrib><contrib contrib-type="author"><name><surname>Orekhov</surname><given-names>Alexander N</given-names></name><xref ref-type="aff" rid="af2-dddt-12-3431">2</xref><xref ref-type="aff" rid="af4-dddt-12-3431">4</xref><xref ref-type="corresp" rid="c1-dddt-12-3431"></xref></contrib></contrib-group><aff id="af1-dddt-12-3431"><label>1</label>Department of Genetics, Cytology and Bioengineering, Faculty of Biology and Medicine, Voronezh State University, Voronezh, Russia</aff><aff id="af2-dddt-12-3431"><label>2</label>Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, Moscow, Russia,<email>a.h.opexob@gmail.com</email></aff><aff id="af3-dddt-12-3431"><label>3</label>Federal Research and Clinical Center of Intensive Care Medicine and Rehabilitology, Moscow, Russia</aff><aff id="af4-dddt-12-3431"><label>4</label>Institute for Atherosclerosis Research, Skolkovo Innovative Center, Moscow, Russia,<email>a.h.opexob@gmail.com</email></aff><author-notes><corresp id="c1-dddt-12-3431">Correspondence: Alexander N Orekhov, Laboratory of Angiopathology, Institute of General Pathology and Pathophysiology, 125315 Moscow, Russia, Tel +7 903 169 0866, Email <email>a.h.opexob@gmail.com</email></corresp></author-notes><pub-date pub-type="collection"><year>2018</year></pub-date><pub-date pub-type="epub"><day>10</day><month>10</month><year>2018</year></pub-date><volume>12</volume><fpage>3431</fpage><lpage>3437</lpage><permissions><copyright-statement>© 2018 Glanz et al. This work is published and licensed by Dove Medical Press Limited</copyright-statement><copyright-year>2018</copyright-year><license><license-p>The full terms of this license are available at <ext-link ext-link-type="uri" xlink:href="https://www.dovepress.com/terms.php">https://www.dovepress.com/terms.php</ext-link> and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/3.0/">http://creativecommons.org/licenses/by-nc/3.0/</ext-link>). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed.</license-p></license></permissions><abstract><p>The demand for novel anti-influenza drugs persists, which is highlighted by the recent pandemics of influenza affecting thousands of people across the globe. One of the approaches to block the virus spreading is inhibiting viral sialidase (neuraminidase). This enzyme cleaves the sialic acid link between the newly formed virions and the host cell surface liberating the virions from the cell and maintaining the cycle of infection. Viral neuraminidases appear therefore as attractive therapeutic targets for preventing further spread of influenza infection. Compared to ion channel blockers that were the first approved anti-influenza drugs, neuraminidase inhibitors are well tolerated and target both influenza A and B viruses. Moreover, neuraminidase/sialidase inhibitors may be useful for managing some other human pathologies, such as cancer. In this review, we discuss the available knowledge on neuraminidase or sialidase inhibitors, their design, clinical application, and the current challenges.</p></abstract><kwd-group><title>Keywords</title><kwd>sialidase</kwd><kwd>neuraminidase</kwd><kwd>neuraminidase inhibitor</kwd><kwd>influenza</kwd><kwd>drug design</kwd></kwd-group></article-meta></front><floats-group><fig id="f1-dddt-12-3431" position="float"><label>Figure 1</label><caption><p>Simplified presentation of the influenza virus life cycle.</p><p><bold>Notes:</bold> Virions attach to host cells via interaction with surface receptors containing sialic acid residues in the glycoconjugate parts. Virions are then internalized by the cell through endocytosis. After uncoating of the virion, its genetic material is release into the cell and replicated by the RNA polymerase. New viral RNA (ribonucleoprotein) and viral proteins synthesized by the host cell assemble at the cell surface into new virions. After budding, virions need to be detached from the host cell by viral neuraminidase. This step is the target of anti-influenza neuraminidase inhibitors used in clinical practice.</p></caption><graphic xlink:href="dddt-12-3431Fig1"></graphic></fig><table-wrap id="t1-dddt-12-3431" position="float"><label>Table 1</label><caption><p>Some characteristics of viral neuraminidase inhibitors</p></caption><table frame="hsides" rules="all"><thead><tr><th valign="top" align="left" rowspan="1" colspan="1"></th><th valign="top" align="left" rowspan="1" colspan="1">Zanamivir (Relenza)</th><th valign="top" align="left" rowspan="1" colspan="1">Oseltamivir (Tamiflu)</th><th valign="top" align="left" rowspan="1" colspan="1">Laninamivir (R-125489)</th><th valign="top" align="left" rowspan="1" colspan="1">Peramivir (Rapiacta)</th><th valign="top" align="left" rowspan="1" colspan="1">TCN-032</th></tr></thead><tbody><tr><td valign="top" align="left" rowspan="1" colspan="1">Licensing</td><td valign="top" align="left" rowspan="1" colspan="1">UK, USA</td><td valign="top" align="left" rowspan="1" colspan="1">UK, USA</td><td valign="top" align="left" rowspan="1" colspan="1">Japan</td><td valign="top" align="left" rowspan="1" colspan="1">Japan, South Korea</td><td valign="top" align="left" rowspan="1" colspan="1">Prospective</td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Delivery</td><td valign="top" align="left" rowspan="1" colspan="1">Inhalation</td><td valign="top" align="left" rowspan="1" colspan="1">Oral administration</td><td valign="top" align="left" rowspan="1" colspan="1">Inhalation</td><td valign="top" align="left" rowspan="1" colspan="1">Intravenous administration</td><td valign="top" align="left" rowspan="1" colspan="1">Intravenous administration</td></tr><tr><td valign="top" align="left" rowspan="1" colspan="1">Other features</td><td valign="top" align="left" rowspan="1" colspan="1">Powder inhalation may be unsuitable in severe influenza</td><td valign="top" align="left" rowspan="1" colspan="1">Possible mutation-induced resistance</td><td valign="top" align="left" rowspan="1" colspan="1">Comparable clinical efficacy to oseltamivir and zanamivir against H1N1 pandemic and seasonal H3N2, as well as influenza B</td><td valign="top" align="left" rowspan="1" colspan="1">Emergency use authorization (US) for treatment of pandemic 2009 H1N1 INFV</td><td valign="top" align="left" rowspan="1" colspan="1">Does not affect M2 ion channel activity in the virion and interferes with budding Safe and relatively efficient in Phase I clinical trial</td></tr></tbody></table><table-wrap-foot><fn id="tfn1-dddt-12-3431"><p><bold>Abbreviation:</bold> INFV, influenza.</p></fn></table-wrap-foot></table-wrap></floats-group></pmc><affiliations><list><country><li>Russie</li></country><region><li>District fédéral central</li></region><settlement><li>Moscou</li></settlement></list><tree><noCountry><name sortKey="Myasoedova, Veronika A" sort="Myasoedova, Veronika A" uniqKey="Myasoedova V" first="Veronika A" last="Myasoedova">Veronika A. Myasoedova</name><name sortKey="Orekhov, Alexander N" sort="Orekhov, Alexander N" uniqKey="Orekhov A" first="Alexander N" last="Orekhov">Alexander N. Orekhov</name></noCountry><country name="Russie"><noRegion><name sortKey="Glanz, Victor Yu" sort="Glanz, Victor Yu" uniqKey="Glanz V" first="Victor Yu" last="Glanz">Victor Yu Glanz</name></noRegion><name sortKey="Grechko, Andrey V" sort="Grechko, Andrey V" uniqKey="Grechko A" first="Andrey V" last="Grechko">Andrey V. Grechko</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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