Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis

Autores
Nair, Manoj Kumar Mohan; De Masi, Leon; Yue, Ming; Galvan, Estela Maria; Chen, Huaiqing; Wang, Fang; Schifferli, Dieter M.
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Yersinia pestis is the causative agent of plague. This bacterium evolved from an ancestral enteroinvasive Yersinia pseudotuberculosis strain by gene loss and acquisition of new genes, allowing it to use fleas as transmission vectors. Infection frequently leads to a rapidly lethal outcome in humans, a variety of rodents, and cats. This study focuses on the Y. pestis KIM yapV gene and its product, recognized as an autotransporter protein by its typical sequence, outer membrane localization, and amino-terminal surface exposure. Comparison of Yersinia genomes revealed that DNA encoding YapV or each of three individual paralogous proteins (YapK, YapJ, and YapX) was present as a gene or pseudogene in a strain-specific manner and only in Y. pestis and Y. pseudotuberculosis. YapV acted as an adhesin for alveolar epithelial cells and specific extracellular matrix (ECM) proteins, as shown with recombinant Escherichia coli, Y. pestis, or purified passenger domains. Like YapV, YapK and YapJ demonstrated adhesive properties, suggesting that their previously related in vivo activity is due to their capacity to modulate binding properties of Y. pestis in its hosts, in conjunction with other adhesins. A differential host-specific type of binding to ECM proteins by YapV, YapK, and YapJ suggested that these proteins participate in broadening the host range of Y. pestis. A phylogenic tree including 36 Y. pestis strains highlighted an association between the gene profile for the four paralogous proteins and the geographic location of the corresponding isolated strains, suggesting an evolutionary adaption of Y. pestis to specific local animal hosts or reservoirs.
Fil: Nair, Manoj Kumar Mohan. University Of Pennsylvania; Estados Unidos
Fil: De Masi, Leon. University Of Pennsylvania; Estados Unidos
Fil: Yue, Ming. University Of Pennsylvania; Estados Unidos
Fil: Galvan, Estela Maria. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. State University Of Pennsylvania; Estados Unidos
Fil: Chen, Huaiqing. University Of Pennsylvania; Estados Unidos
Fil: Wang, Fang. University Of Pennsylvania; Estados Unidos
Fil: Schifferli, Dieter M.. University Of Pennsylvania; Estados Unidos
Materia
YERSINIA PESTIS
AUTOTRANSPORTER PROTEINS
ADHESION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/10500
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/10500
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestisNair, Manoj Kumar MohanDe Masi, LeonYue, MingGalvan, Estela MariaChen, HuaiqingWang, FangSchifferli, Dieter M.YERSINIA PESTISAUTOTRANSPORTER PROTEINSADHESIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Yersinia pestis is the causative agent of plague. This bacterium evolved from an ancestral enteroinvasive Yersinia pseudotuberculosis strain by gene loss and acquisition of new genes, allowing it to use fleas as transmission vectors. Infection frequently leads to a rapidly lethal outcome in humans, a variety of rodents, and cats. This study focuses on the Y. pestis KIM yapV gene and its product, recognized as an autotransporter protein by its typical sequence, outer membrane localization, and amino-terminal surface exposure. Comparison of Yersinia genomes revealed that DNA encoding YapV or each of three individual paralogous proteins (YapK, YapJ, and YapX) was present as a gene or pseudogene in a strain-specific manner and only in Y. pestis and Y. pseudotuberculosis. YapV acted as an adhesin for alveolar epithelial cells and specific extracellular matrix (ECM) proteins, as shown with recombinant Escherichia coli, Y. pestis, or purified passenger domains. Like YapV, YapK and YapJ demonstrated adhesive properties, suggesting that their previously related in vivo activity is due to their capacity to modulate binding properties of Y. pestis in its hosts, in conjunction with other adhesins. A differential host-specific type of binding to ECM proteins by YapV, YapK, and YapJ suggested that these proteins participate in broadening the host range of Y. pestis. A phylogenic tree including 36 Y. pestis strains highlighted an association between the gene profile for the four paralogous proteins and the geographic location of the corresponding isolated strains, suggesting an evolutionary adaption of Y. pestis to specific local animal hosts or reservoirs.Fil: Nair, Manoj Kumar Mohan. University Of Pennsylvania; Estados UnidosFil: De Masi, Leon. University Of Pennsylvania; Estados UnidosFil: Yue, Ming. University Of Pennsylvania; Estados UnidosFil: Galvan, Estela Maria. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. State University Of Pennsylvania; Estados UnidosFil: Chen, Huaiqing. University Of Pennsylvania; Estados UnidosFil: Wang, Fang. University Of Pennsylvania; Estados UnidosFil: Schifferli, Dieter M.. University Of Pennsylvania; Estados UnidosAmerican Society For Microbiology2015-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/10500Nair, Manoj Kumar Mohan; De Masi, Leon; Yue, Ming; Galvan, Estela Maria; Chen, Huaiqing; et al.; Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis; American Society For Microbiology; Infection And Immunity; 83; 5; 5-2015; 1809-18190019-9567enginfo:eu-repo/semantics/altIdentifier/url/http://iai.asm.org/content/83/5/1809info:eu-repo/semantics/altIdentifier/doi/10.1128/IAI.00094-15info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:56:37Zoai:ri.conicet.gov.ar:11336/10500instacron: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 09:56:37.958CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis
title Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis
spellingShingle Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis
Nair, Manoj Kumar Mohan
YERSINIA PESTIS
AUTOTRANSPORTER PROTEINS
ADHESION
title_short Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis
title_full Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis
title_fullStr Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis
title_full_unstemmed Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis
title_sort Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis
dc.creator.none.fl_str_mv Nair, Manoj Kumar Mohan
De Masi, Leon
Yue, Ming
Galvan, Estela Maria
Chen, Huaiqing
Wang, Fang
Schifferli, Dieter M.
author Nair, Manoj Kumar Mohan
author_facet Nair, Manoj Kumar Mohan
De Masi, Leon
Yue, Ming
Galvan, Estela Maria
Chen, Huaiqing
Wang, Fang
Schifferli, Dieter M.
author_role author
author2 De Masi, Leon
Yue, Ming
Galvan, Estela Maria
Chen, Huaiqing
Wang, Fang
Schifferli, Dieter M.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv YERSINIA PESTIS
AUTOTRANSPORTER PROTEINS
ADHESION
topic YERSINIA PESTIS
AUTOTRANSPORTER PROTEINS
ADHESION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Yersinia pestis is the causative agent of plague. This bacterium evolved from an ancestral enteroinvasive Yersinia pseudotuberculosis strain by gene loss and acquisition of new genes, allowing it to use fleas as transmission vectors. Infection frequently leads to a rapidly lethal outcome in humans, a variety of rodents, and cats. This study focuses on the Y. pestis KIM yapV gene and its product, recognized as an autotransporter protein by its typical sequence, outer membrane localization, and amino-terminal surface exposure. Comparison of Yersinia genomes revealed that DNA encoding YapV or each of three individual paralogous proteins (YapK, YapJ, and YapX) was present as a gene or pseudogene in a strain-specific manner and only in Y. pestis and Y. pseudotuberculosis. YapV acted as an adhesin for alveolar epithelial cells and specific extracellular matrix (ECM) proteins, as shown with recombinant Escherichia coli, Y. pestis, or purified passenger domains. Like YapV, YapK and YapJ demonstrated adhesive properties, suggesting that their previously related in vivo activity is due to their capacity to modulate binding properties of Y. pestis in its hosts, in conjunction with other adhesins. A differential host-specific type of binding to ECM proteins by YapV, YapK, and YapJ suggested that these proteins participate in broadening the host range of Y. pestis. A phylogenic tree including 36 Y. pestis strains highlighted an association between the gene profile for the four paralogous proteins and the geographic location of the corresponding isolated strains, suggesting an evolutionary adaption of Y. pestis to specific local animal hosts or reservoirs.
Fil: Nair, Manoj Kumar Mohan. University Of Pennsylvania; Estados Unidos
Fil: De Masi, Leon. University Of Pennsylvania; Estados Unidos
Fil: Yue, Ming. University Of Pennsylvania; Estados Unidos
Fil: Galvan, Estela Maria. Fundación Instituto Leloir; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. State University Of Pennsylvania; Estados Unidos
Fil: Chen, Huaiqing. University Of Pennsylvania; Estados Unidos
Fil: Wang, Fang. University Of Pennsylvania; Estados Unidos
Fil: Schifferli, Dieter M.. University Of Pennsylvania; Estados Unidos
description Yersinia pestis is the causative agent of plague. This bacterium evolved from an ancestral enteroinvasive Yersinia pseudotuberculosis strain by gene loss and acquisition of new genes, allowing it to use fleas as transmission vectors. Infection frequently leads to a rapidly lethal outcome in humans, a variety of rodents, and cats. This study focuses on the Y. pestis KIM yapV gene and its product, recognized as an autotransporter protein by its typical sequence, outer membrane localization, and amino-terminal surface exposure. Comparison of Yersinia genomes revealed that DNA encoding YapV or each of three individual paralogous proteins (YapK, YapJ, and YapX) was present as a gene or pseudogene in a strain-specific manner and only in Y. pestis and Y. pseudotuberculosis. YapV acted as an adhesin for alveolar epithelial cells and specific extracellular matrix (ECM) proteins, as shown with recombinant Escherichia coli, Y. pestis, or purified passenger domains. Like YapV, YapK and YapJ demonstrated adhesive properties, suggesting that their previously related in vivo activity is due to their capacity to modulate binding properties of Y. pestis in its hosts, in conjunction with other adhesins. A differential host-specific type of binding to ECM proteins by YapV, YapK, and YapJ suggested that these proteins participate in broadening the host range of Y. pestis. A phylogenic tree including 36 Y. pestis strains highlighted an association between the gene profile for the four paralogous proteins and the geographic location of the corresponding isolated strains, suggesting an evolutionary adaption of Y. pestis to specific local animal hosts or reservoirs.
publishDate 2015
dc.date.none.fl_str_mv 2015-05
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/11336/10500
Nair, Manoj Kumar Mohan; De Masi, Leon; Yue, Ming; Galvan, Estela Maria; Chen, Huaiqing; et al.; Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis; American Society For Microbiology; Infection And Immunity; 83; 5; 5-2015; 1809-1819
0019-9567
url http://hdl.handle.net/11336/10500
identifier_str_mv Nair, Manoj Kumar Mohan; De Masi, Leon; Yue, Ming; Galvan, Estela Maria; Chen, Huaiqing; et al.; Adhesive properties of YapV and paralogous autotransporter proteins of Yersinia pestis; American Society For Microbiology; Infection And Immunity; 83; 5; 5-2015; 1809-1819
0019-9567
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://iai.asm.org/content/83/5/1809
info:eu-repo/semantics/altIdentifier/doi/10.1128/IAI.00094-15
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society For Microbiology
publisher.none.fl_str_mv American Society For Microbiology
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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score 13.13397

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