CobaltMaghrebV1, Main, Exploration, bibRecord, 000650

STRUCTURE OF A MICROSPORIDIAN METHIONINE AMINOPEPTIDASE TYPE 2 COMPLEXED WITH FUMAGILLIN AND TNP470

Identifieur interne : 000650 ( Main/Exploration ); précédent : 000649; suivant : 000651

STRUCTURE 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.

RBID : PMC:2759695

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 Enterocytozoon bieneusi. Fumagillin and its analogues have been demonstrated to have activity in vitro and in animal models of microsporidiosis and human infections due to E. bieneusi. Fumagillin and its analogues inhibit methionine aminopeptidase type 2. Encephalitozoon cuniculi 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 E. bieneusi MetAP2. Comparison of microsporidian MetAP2 structures with human MetAP2 provide insights into the design of inhibitors that might exhibit specificity for microsporidian MetAP2.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2759695

DOI: 10.1016/j.molbiopara.2009.07.008
PubMed: 19660503
PubMed Central: 2759695

Affiliations:

États-Unis

Le document en format XML

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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>
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Serveur d'exploration sur le cobalt au Maghreb

STRUCTURE OF A MICROSPORIDIAN METHIONINE AMINOPEPTIDASE TYPE 2 COMPLEXED WITH FUMAGILLIN AND TNP470

STRUCTURE OF A MICROSPORIDIAN METHIONINE AMINOPEPTIDASE TYPE 2 COMPLEXED WITH FUMAGILLIN AND TNP470

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Abstract

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