In silico survey and characterization of babesia microti functional and non-functional proteases
- Autores
- Florin Christensen, Mónica; Wieser, Sarah Nathaly; Suarez, Carlos E.; Schnittger, Leonhard
- Año de publicación
- 2021
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- 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 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 B. microti 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 B. microti genome. We identified 64 active proteases and 25 nonactive protease homologs. These proteases can be classified into cysteine (n = 28), serine (n = 21), threonine (n = 14), asparagine (n = 7), and metallopeptidases (n = 19), which, in turn, are assigned to a total of 38 peptidase families. Comparative studies between the repertoire of B. bovis and B. microti proteases revealed differences among sensu stricto and sensu lato Babesia parasites that reflect their distinct evolutionary history. Overall, this data may help direct future research towards our understanding of the biology and pathogenicity of Babesia parasites and to explore proteases as targets for developing novel therapeutic interventions.
Fil: Florin Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina
Fil: Wieser, Sarah Nathaly. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina
Fil: Suarez, Carlos E.. United States Department of Agriculture. Agriculture Research Service; Estados Unidos. Washington State University; Estados Unidos
Fil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina - Materia
-
BABESIA MICROTI
HUMAN BABESIOSIS
PEPTIDASES
THERAPEUTIC DRUGS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/184900
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CONICET Digital (CONICET) |
spelling |
In silico survey and characterization of babesia microti functional and non-functional proteasesFlorin Christensen, MónicaWieser, Sarah NathalySuarez, Carlos E.Schnittger, LeonhardBABESIA MICROTIHUMAN BABESIOSISPEPTIDASESTHERAPEUTIC DRUGShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Human 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 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 B. microti 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 B. microti genome. We identified 64 active proteases and 25 nonactive protease homologs. These proteases can be classified into cysteine (n = 28), serine (n = 21), threonine (n = 14), asparagine (n = 7), and metallopeptidases (n = 19), which, in turn, are assigned to a total of 38 peptidase families. Comparative studies between the repertoire of B. bovis and B. microti proteases revealed differences among sensu stricto and sensu lato Babesia parasites that reflect their distinct evolutionary history. Overall, this data may help direct future research towards our understanding of the biology and pathogenicity of Babesia parasites and to explore proteases as targets for developing novel therapeutic interventions.Fil: Florin Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; ArgentinaFil: Wieser, Sarah Nathaly. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; ArgentinaFil: Suarez, Carlos E.. United States Department of Agriculture. Agriculture Research Service; Estados Unidos. Washington State University; Estados UnidosFil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; ArgentinaMultidisciplinary Digital Publishing Institute2021-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/184900Florin Christensen, Mónica; Wieser, Sarah Nathaly; Suarez, Carlos E.; Schnittger, Leonhard; In silico survey and characterization of babesia microti functional and non-functional proteases; Multidisciplinary Digital Publishing Institute; Pathogens; 10; 11; 11-2021; 1-262076-0817CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/10/11/1457info:eu-repo/semantics/altIdentifier/doi/10.3390/pathogens10111457info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:43:22Zoai:ri.conicet.gov.ar:11336/184900instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:43:23.199CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
In silico survey and characterization of babesia microti functional and non-functional proteases |
title |
In silico survey and characterization of babesia microti functional and non-functional proteases |
spellingShingle |
In silico survey and characterization of babesia microti functional and non-functional proteases Florin Christensen, Mónica BABESIA MICROTI HUMAN BABESIOSIS PEPTIDASES THERAPEUTIC DRUGS |
title_short |
In silico survey and characterization of babesia microti functional and non-functional proteases |
title_full |
In silico survey and characterization of babesia microti functional and non-functional proteases |
title_fullStr |
In silico survey and characterization of babesia microti functional and non-functional proteases |
title_full_unstemmed |
In silico survey and characterization of babesia microti functional and non-functional proteases |
title_sort |
In silico survey and characterization of babesia microti functional and non-functional proteases |
dc.creator.none.fl_str_mv |
Florin Christensen, Mónica Wieser, Sarah Nathaly Suarez, Carlos E. Schnittger, Leonhard |
author |
Florin Christensen, Mónica |
author_facet |
Florin Christensen, Mónica Wieser, Sarah Nathaly Suarez, Carlos E. Schnittger, Leonhard |
author_role |
author |
author2 |
Wieser, Sarah Nathaly Suarez, Carlos E. Schnittger, Leonhard |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
BABESIA MICROTI HUMAN BABESIOSIS PEPTIDASES THERAPEUTIC DRUGS |
topic |
BABESIA MICROTI HUMAN BABESIOSIS PEPTIDASES THERAPEUTIC DRUGS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
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 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 B. microti 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 B. microti genome. We identified 64 active proteases and 25 nonactive protease homologs. These proteases can be classified into cysteine (n = 28), serine (n = 21), threonine (n = 14), asparagine (n = 7), and metallopeptidases (n = 19), which, in turn, are assigned to a total of 38 peptidase families. Comparative studies between the repertoire of B. bovis and B. microti proteases revealed differences among sensu stricto and sensu lato Babesia parasites that reflect their distinct evolutionary history. Overall, this data may help direct future research towards our understanding of the biology and pathogenicity of Babesia parasites and to explore proteases as targets for developing novel therapeutic interventions. Fil: Florin Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina Fil: Wieser, Sarah Nathaly. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina Fil: Suarez, Carlos E.. United States Department of Agriculture. Agriculture Research Service; Estados Unidos. Washington State University; Estados Unidos Fil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Patobiología Veterinaria. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Patobiología Veterinaria; Argentina |
description |
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 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 B. microti 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 B. microti genome. We identified 64 active proteases and 25 nonactive protease homologs. These proteases can be classified into cysteine (n = 28), serine (n = 21), threonine (n = 14), asparagine (n = 7), and metallopeptidases (n = 19), which, in turn, are assigned to a total of 38 peptidase families. Comparative studies between the repertoire of B. bovis and B. microti proteases revealed differences among sensu stricto and sensu lato Babesia parasites that reflect their distinct evolutionary history. Overall, this data may help direct future research towards our understanding of the biology and pathogenicity of Babesia parasites and to explore proteases as targets for developing novel therapeutic interventions. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-11 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/184900 Florin Christensen, Mónica; Wieser, Sarah Nathaly; Suarez, Carlos E.; Schnittger, Leonhard; In silico survey and characterization of babesia microti functional and non-functional proteases; Multidisciplinary Digital Publishing Institute; Pathogens; 10; 11; 11-2021; 1-26 2076-0817 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/184900 |
identifier_str_mv |
Florin Christensen, Mónica; Wieser, Sarah Nathaly; Suarez, Carlos E.; Schnittger, Leonhard; In silico survey and characterization of babesia microti functional and non-functional proteases; Multidisciplinary Digital Publishing Institute; Pathogens; 10; 11; 11-2021; 1-26 2076-0817 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/10/11/1457 info:eu-repo/semantics/altIdentifier/doi/10.3390/pathogens10111457 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Multidisciplinary Digital Publishing Institute |
publisher.none.fl_str_mv |
Multidisciplinary Digital Publishing Institute |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1842268597915746304 |
score |
13.13397 |