In Silico Survey and Characterization of Babesia microti Functional and Non-Functional Proteases

Human babesiosis caused by the intraerythrocytic apicomplexan Babesia microti is an expanding tick-borne zoonotic disease that may cause severe symptoms and death in elderly or immunocompromised individuals. In light of an increasing resistance of B. microti to...

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Autores principales:	Monica Florin-Christensen, Sarah N. Wieser, Carlos E. Suarez, Leonhard Schnittger
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	human babesiosis <i>Babesia microti</i> therapeutic drugs peptidases Medicine R
Acceso en línea:	https://doaj.org/article/d2014fd2d1c34026b82479bfbe514ed9
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spelling	oai:doaj.org-article:d2014fd2d1c34026b82479bfbe514ed92021-11-25T18:38:23ZIn Silico Survey and Characterization of <i>Babesia microti</i> Functional and Non-Functional Proteases10.3390/pathogens101114572076-0817https://doaj.org/article/d2014fd2d1c34026b82479bfbe514ed92021-11-01T00:00:00Zhttps://www.mdpi.com/2076-0817/10/11/1457https://doaj.org/toc/2076-0817Human babesiosis caused by the intraerythrocytic apicomplexan <i>Babesia microti</i> is an expanding tick-borne zoonotic disease that may cause severe symptoms and death in elderly or immunocompromised individuals. In light of an increasing resistance of <i>B. microti</i> to drugs, there is a lack of therapeutic alternatives. Species-specific proteases are essential for parasite survival and possible chemotherapeutic targets. However, the repertoire of proteases in <i>B. microti</i> remains poorly investigated. Herein, we employed several combined bioinformatics tools and strategies to organize and identify genes encoding for the full repertoire of proteases in the <i>B. microti</i> genome. We identified 64 active proteases and 25 nonactive protease homologs. These proteases can be classified into cysteine (<i>n</i> = 28), serine (<i>n</i> = 21), threonine (<i>n</i> = 14), asparagine (<i>n</i> = 7), and metallopeptidases (<i>n</i> = 19), which, in turn, are assigned to a total of 38 peptidase families. Comparative studies between the repertoire of <i>B. bovis</i> and <i>B. microti</i> proteases revealed differences among sensu stricto and sensu lato <i>Babesia</i> parasites that reflect their distinct evolutionary history. Overall, this data may help direct future research towards our understanding of the biology and pathogenicity of <i>Babesia</i> parasites and to explore proteases as targets for developing novel therapeutic interventions.Monica Florin-ChristensenSarah N. WieserCarlos E. SuarezLeonhard SchnittgerMDPI AGarticlehuman babesiosis<i>Babesia microti</i>therapeutic drugspeptidasesMedicineRENPathogens, Vol 10, Iss 1457, p 1457 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	human babesiosis <i>Babesia microti</i> therapeutic drugs peptidases Medicine R
spellingShingle	human babesiosis <i>Babesia microti</i> therapeutic drugs peptidases Medicine R Monica Florin-Christensen Sarah N. Wieser Carlos E. Suarez Leonhard Schnittger In Silico Survey and Characterization of <i>Babesia microti</i> Functional and Non-Functional Proteases
description	Human babesiosis caused by the intraerythrocytic apicomplexan <i>Babesia microti</i> is an expanding tick-borne zoonotic disease that may cause severe symptoms and death in elderly or immunocompromised individuals. In light of an increasing resistance of <i>B. microti</i> to drugs, there is a lack of therapeutic alternatives. Species-specific proteases are essential for parasite survival and possible chemotherapeutic targets. However, the repertoire of proteases in <i>B. microti</i> remains poorly investigated. Herein, we employed several combined bioinformatics tools and strategies to organize and identify genes encoding for the full repertoire of proteases in the <i>B. microti</i> genome. We identified 64 active proteases and 25 nonactive protease homologs. These proteases can be classified into cysteine (<i>n</i> = 28), serine (<i>n</i> = 21), threonine (<i>n</i> = 14), asparagine (<i>n</i> = 7), and metallopeptidases (<i>n</i> = 19), which, in turn, are assigned to a total of 38 peptidase families. Comparative studies between the repertoire of <i>B. bovis</i> and <i>B. microti</i> proteases revealed differences among sensu stricto and sensu lato <i>Babesia</i> parasites that reflect their distinct evolutionary history. Overall, this data may help direct future research towards our understanding of the biology and pathogenicity of <i>Babesia</i> parasites and to explore proteases as targets for developing novel therapeutic interventions.
format	article
author	Monica Florin-Christensen Sarah N. Wieser Carlos E. Suarez Leonhard Schnittger
author_facet	Monica Florin-Christensen Sarah N. Wieser Carlos E. Suarez Leonhard Schnittger
author_sort	Monica Florin-Christensen
title	In Silico Survey and Characterization of <i>Babesia microti</i> Functional and Non-Functional Proteases
title_short	In Silico Survey and Characterization of <i>Babesia microti</i> Functional and Non-Functional Proteases
title_full	In Silico Survey and Characterization of <i>Babesia microti</i> Functional and Non-Functional Proteases
title_fullStr	In Silico Survey and Characterization of <i>Babesia microti</i> Functional and Non-Functional Proteases
title_full_unstemmed	In Silico Survey and Characterization of <i>Babesia microti</i> Functional and Non-Functional Proteases
title_sort	in silico survey and characterization of <i>babesia microti</i> functional and non-functional proteases
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/d2014fd2d1c34026b82479bfbe514ed9
work_keys_str_mv	AT monicaflorinchristensen insilicosurveyandcharacterizationofibabesiamicrotiifunctionalandnonfunctionalproteases AT sarahnwieser insilicosurveyandcharacterizationofibabesiamicrotiifunctionalandnonfunctionalproteases AT carlosesuarez insilicosurveyandcharacterizationofibabesiamicrotiifunctionalandnonfunctionalproteases AT leonhardschnittger insilicosurveyandcharacterizationofibabesiamicrotiifunctionalandnonfunctionalproteases
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In Silico Survey and Characterization of <i>Babesia microti</i> Functional and Non-Functional Proteases

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