STRUCTURE OF A MICROSPORIDIAN METHIONINE AMINOPEPTIDASE TYPE 2 COMPLEXED WITH FUMAGILLIN AND TNP470
Identifieur interne : 000321 ( Pmc/Checkpoint ); précédent : 000320; suivant : 000322STRUCTURE OF A MICROSPORIDIAN METHIONINE AMINOPEPTIDASE TYPE 2 COMPLEXED WITH FUMAGILLIN AND TNP470
Auteurs : John Jeff Alvarado [États-Unis] ; Anjana Nemkal [États-Unis] ; J. Michael Sauder [États-Unis] ; Marijane Russell [États-Unis] ; Donna E. Akiyoshi [États-Unis] ; Wuxian Shi [États-Unis] ; Steven C. Almo [États-Unis] ; Louis M. Weiss [États-Unis]Source :
- Molecular and biochemical parasitology [ 0166-6851 ] ; 2009.
Abstract
Microsporidia are protists that have been reported to cause infections in both vertebrates and invertebrates. They have emerged as human pathogens particularly in patients that are immunnosuppressed and cases of gastrointestinal infection, encephalitis, keratitis, sinusitis, myositis and disseminated infection are well described in the literature. While benzimidazoles are active against many species of Microsporidia, these drugs do not have significant activity against
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DOI: 10.1016/j.molbiopara.2009.07.008
PubMed: 19660503
PubMed Central: 2759695
Affiliations:
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<front><div type="abstract" xml:lang="en"><p id="P1">Microsporidia are protists that have been reported to cause infections in both vertebrates and invertebrates. They have emerged as human pathogens particularly in patients that are immunnosuppressed and cases of gastrointestinal infection, encephalitis, keratitis, sinusitis, myositis and disseminated infection are well described in the literature. While benzimidazoles are active against many species of Microsporidia, these drugs do not have significant activity against <italic>Enterocytozoon bieneusi.</italic>
Fumagillin and its analogues have been demonstrated to have activity <italic>in vitro</italic>
and in animal models of microsporidiosis and human infections due to <italic>E. bieneusi.</italic>
Fumagillin and its analogues inhibit methionine aminopeptidase type 2. <italic>Encephalitozoon cuniculi</italic>
MetAP2 (EcMetAP2) was cloned and expressed as an active enzyme using a baculovirus system. The crystal structure of EcMetAP2 was determined with and without the bound inhibitors fumagillin and TNP470. This structure classifies EcMetAP2 as a member of the MetAP2c family. The EcMetAP2 structure was used to generate a homology model of the <italic>E. bieneusi</italic>
MetAP2. Comparison of microsporidian MetAP2 structures with human MetAP2 provide insights into the design of inhibitors that might exhibit specificity for microsporidian MetAP2.</p>
</div>
</front>
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<journal-id journal-id-type="pubmed-jr-id">5984</journal-id>
<journal-id journal-id-type="nlm-ta">Mol Biochem Parasitol</journal-id>
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<contrib-group><contrib contrib-type="author"><name><surname>ALVARADO</surname>
<given-names>JOHN JEFF</given-names>
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<contrib contrib-type="author"><name><surname>NEMKAL</surname>
<given-names>ANJANA</given-names>
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<contrib contrib-type="author"><name><surname>SAUDER</surname>
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<contrib contrib-type="author"><name><surname>RUSSELL</surname>
<given-names>MARIJANE</given-names>
</name>
<xref ref-type="aff" rid="A3">c</xref>
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<contrib contrib-type="author"><name><surname>AKIYOSHI</surname>
<given-names>DONNA E.</given-names>
</name>
<xref ref-type="aff" rid="A4">d</xref>
</contrib>
<contrib contrib-type="author"><name><surname>SHI</surname>
<given-names>WUXIAN</given-names>
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<contrib contrib-type="author"><name><surname>ALMO</surname>
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<given-names>LOUIS M.</given-names>
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<xref ref-type="aff" rid="A6">f</xref>
<xref ref-type="corresp" rid="CR1">*</xref>
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<aff id="A1"><label>a</label>
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY, USA.</aff>
<aff id="A2"><label>b</label>
Department of Pathology, Albert Einstein College of Medicine, Bronx, NY, USA.</aff>
<aff id="A3"><label>c</label>
Eli Lilly; San Diego, CA, USA.</aff>
<aff id="A4"><label>d</label>
Division of Infectious Diseases, Tufts University School of Veterinary Medicine, Grafton, MA, USA.</aff>
<aff id="A5"><label>e</label>
Center for Synchrotron Biosciences, Case Western Reserve University, Cleveland, OH, USA.</aff>
<aff id="A6"><label>f</label>
Department of Medicine, Albert Einstein College of Medicine, Bronx, NY, USA.</aff>
<author-notes><corresp id="CR1"><label>*</label>
To whom correspondence should be addressed: <email>lmweiss@aecom.yu.edu</email>
; phone, (718)-430-2142; fax, (718)-430-8543.</corresp>
</author-notes>
<pub-date pub-type="nihms-submitted"><day>7</day>
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<year>2009</year>
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<year>2009</year>
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<pub-date pub-type="pmc-release"><day>1</day>
<month>12</month>
<year>2010</year>
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<volume>168</volume>
<issue>2</issue>
<fpage>158</fpage>
<lpage>167</lpage>
<permissions><copyright-statement>© 2009 Elsevier B.V. All rights reserved.</copyright-statement>
<copyright-year>2009</copyright-year>
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<abstract><p id="P1">Microsporidia are protists that have been reported to cause infections in both vertebrates and invertebrates. They have emerged as human pathogens particularly in patients that are immunnosuppressed and cases of gastrointestinal infection, encephalitis, keratitis, sinusitis, myositis and disseminated infection are well described in the literature. While benzimidazoles are active against many species of Microsporidia, these drugs do not have significant activity against <italic>Enterocytozoon bieneusi.</italic>
Fumagillin and its analogues have been demonstrated to have activity <italic>in vitro</italic>
and in animal models of microsporidiosis and human infections due to <italic>E. bieneusi.</italic>
Fumagillin and its analogues inhibit methionine aminopeptidase type 2. <italic>Encephalitozoon cuniculi</italic>
MetAP2 (EcMetAP2) was cloned and expressed as an active enzyme using a baculovirus system. The crystal structure of EcMetAP2 was determined with and without the bound inhibitors fumagillin and TNP470. This structure classifies EcMetAP2 as a member of the MetAP2c family. The EcMetAP2 structure was used to generate a homology model of the <italic>E. bieneusi</italic>
MetAP2. Comparison of microsporidian MetAP2 structures with human MetAP2 provide insights into the design of inhibitors that might exhibit specificity for microsporidian MetAP2.</p>
</abstract>
<kwd-group><kwd>Microsporidia</kwd>
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