Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis

Detalhes bibliográficos
Autor(a) principal: Silva, Patrick da [UNESP]
Data de Publicação: 2018
Outros Autores: Manieri, Fernanda Z. [UNESP], Herrera, Carmen M., Trent, M. Stephen, Moreira, Cristiano G. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1128/IAI.00319-18
http://hdl.handle.net/11449/164447
Resumo: Salmonella enterica serovars are associated with diarrhea and gastroenteritis and are a helpful model for understanding host-pathogen mechanisms. Salmonella enterica serovar Typhimurium regulates the distribution of O antigen (OAg) and presents a trimodal distribution based on Wzy polymerase and the Wzz(ST) (longchain-length OAg [L-OAg]) and Wzz(fepE) (very-long-chain-length OAg [VL-OAg]) copolymerases; however, several mechanisms regulating this process remain unclear. Here, we report that LPS modifications modulate the infectious process and that OAg chain length determination plays an essential role during infection. An increase in VL-OAg is dependent on Wzy polymerase, which is promoted by a growth condition resembling the environment of Salmonella-containing vacuoles (SCVs). The virulence- and stress-related periplasmic protein (VisP) participates in OAg synthesis, as a Delta visP mutant presents a semirough OAg phenotype. The Delta visP mutant has greatly decreased motility and J774 macrophage survival in a colitis model of infection. Interestingly, the phenotype is restored after mutation of the wzz(ST) or Wzz(fepE) gene in a Delta visP background. Loss of both the visP and wzz(ST) genes promotes an imbalance in flagellin secretion. L-OAg may function as a shield against host immune systems in the beginning of an infectious process, and VL-OAg protects bacteria during SCV maturation and facilitates intramacrophage replication. Taken together, these data highlight the roles of OAg length in generating phenotypes during S. Typhimurium pathogenesis and show the periplasmic protein VisP as a novel protein in the OAg biosynthesis pathway.
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spelling Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium PathogenesisSalmonellaLPSO antigenVisPlipopolysaccharideSalmonella enterica serovars are associated with diarrhea and gastroenteritis and are a helpful model for understanding host-pathogen mechanisms. Salmonella enterica serovar Typhimurium regulates the distribution of O antigen (OAg) and presents a trimodal distribution based on Wzy polymerase and the Wzz(ST) (longchain-length OAg [L-OAg]) and Wzz(fepE) (very-long-chain-length OAg [VL-OAg]) copolymerases; however, several mechanisms regulating this process remain unclear. Here, we report that LPS modifications modulate the infectious process and that OAg chain length determination plays an essential role during infection. An increase in VL-OAg is dependent on Wzy polymerase, which is promoted by a growth condition resembling the environment of Salmonella-containing vacuoles (SCVs). The virulence- and stress-related periplasmic protein (VisP) participates in OAg synthesis, as a Delta visP mutant presents a semirough OAg phenotype. The Delta visP mutant has greatly decreased motility and J774 macrophage survival in a colitis model of infection. Interestingly, the phenotype is restored after mutation of the wzz(ST) or Wzz(fepE) gene in a Delta visP background. Loss of both the visP and wzz(ST) genes promotes an imbalance in flagellin secretion. L-OAg may function as a shield against host immune systems in the beginning of an infectious process, and VL-OAg protects bacteria during SCV maturation and facilitates intramacrophage replication. Taken together, these data highlight the roles of OAg length in generating phenotypes during S. Typhimurium pathogenesis and show the periplasmic protein VisP as a novel protein in the OAg biosynthesis pathway.Sao Paulo State Univ, Sch Pharmaceut Sci, Dept Biol Sci, Araraquara, SP, BrazilUniv Georgia, Coll Vet Med, Ctr Vaccines & Immunol, Dept Infect Dis, Athens, GA USASao Paulo State Univ, Sch Pharmaceut Sci, Dept Biol Sci, Araraquara, SP, BrazilAmer Soc MicrobiologyUniversidade Estadual Paulista (Unesp)Univ GeorgiaSilva, Patrick da [UNESP]Manieri, Fernanda Z. [UNESP]Herrera, Carmen M.Trent, M. StephenMoreira, Cristiano G. [UNESP]2018-11-26T17:54:35Z2018-11-26T17:54:35Z2018-08-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article21application/pdfhttp://dx.doi.org/10.1128/IAI.00319-18Infection And Immunity. Washington: Amer Soc Microbiology, v. 86, n. 8, 21 p., 2018.0019-9567http://hdl.handle.net/11449/16444710.1128/IAI.00319-18WOS:000439474900023WOS000439474900023.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengInfection And Immunity1,954info:eu-repo/semantics/openAccess2024-06-24T13:07:51Zoai:repositorio.unesp.br:11449/164447Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T19:04:41.674282Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis
title Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis
spellingShingle Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis
Silva, Patrick da [UNESP]
Salmonella
LPS
O antigen
VisP
lipopolysaccharide
title_short Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis
title_full Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis
title_fullStr Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis
title_full_unstemmed Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis
title_sort Novel Role of VisP and the Wzz System during O-Antigen Assembly in Salmonella enterica Serovar Typhimurium Pathogenesis
author Silva, Patrick da [UNESP]
author_facet Silva, Patrick da [UNESP]
Manieri, Fernanda Z. [UNESP]
Herrera, Carmen M.
Trent, M. Stephen
Moreira, Cristiano G. [UNESP]
author_role author
author2 Manieri, Fernanda Z. [UNESP]
Herrera, Carmen M.
Trent, M. Stephen
Moreira, Cristiano G. [UNESP]
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
Univ Georgia
dc.contributor.author.fl_str_mv Silva, Patrick da [UNESP]
Manieri, Fernanda Z. [UNESP]
Herrera, Carmen M.
Trent, M. Stephen
Moreira, Cristiano G. [UNESP]
dc.subject.por.fl_str_mv Salmonella
LPS
O antigen
VisP
lipopolysaccharide
topic Salmonella
LPS
O antigen
VisP
lipopolysaccharide
description Salmonella enterica serovars are associated with diarrhea and gastroenteritis and are a helpful model for understanding host-pathogen mechanisms. Salmonella enterica serovar Typhimurium regulates the distribution of O antigen (OAg) and presents a trimodal distribution based on Wzy polymerase and the Wzz(ST) (longchain-length OAg [L-OAg]) and Wzz(fepE) (very-long-chain-length OAg [VL-OAg]) copolymerases; however, several mechanisms regulating this process remain unclear. Here, we report that LPS modifications modulate the infectious process and that OAg chain length determination plays an essential role during infection. An increase in VL-OAg is dependent on Wzy polymerase, which is promoted by a growth condition resembling the environment of Salmonella-containing vacuoles (SCVs). The virulence- and stress-related periplasmic protein (VisP) participates in OAg synthesis, as a Delta visP mutant presents a semirough OAg phenotype. The Delta visP mutant has greatly decreased motility and J774 macrophage survival in a colitis model of infection. Interestingly, the phenotype is restored after mutation of the wzz(ST) or Wzz(fepE) gene in a Delta visP background. Loss of both the visP and wzz(ST) genes promotes an imbalance in flagellin secretion. L-OAg may function as a shield against host immune systems in the beginning of an infectious process, and VL-OAg protects bacteria during SCV maturation and facilitates intramacrophage replication. Taken together, these data highlight the roles of OAg length in generating phenotypes during S. Typhimurium pathogenesis and show the periplasmic protein VisP as a novel protein in the OAg biosynthesis pathway.
publishDate 2018
dc.date.none.fl_str_mv 2018-11-26T17:54:35Z
2018-11-26T17:54:35Z
2018-08-01
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1128/IAI.00319-18
Infection And Immunity. Washington: Amer Soc Microbiology, v. 86, n. 8, 21 p., 2018.
0019-9567
http://hdl.handle.net/11449/164447
10.1128/IAI.00319-18
WOS:000439474900023
WOS000439474900023.pdf
url http://dx.doi.org/10.1128/IAI.00319-18
http://hdl.handle.net/11449/164447
identifier_str_mv Infection And Immunity. Washington: Amer Soc Microbiology, v. 86, n. 8, 21 p., 2018.
0019-9567
10.1128/IAI.00319-18
WOS:000439474900023
WOS000439474900023.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Infection And Immunity
1,954
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 21
application/pdf
dc.publisher.none.fl_str_mv Amer Soc Microbiology
publisher.none.fl_str_mv Amer Soc Microbiology
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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