The virulence of Streptococcus pneumoniae partially depends on dprA
Autor(a) principal: | |
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Data de Publicação: | 2017 |
Outros Autores: | , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Journal of Microbiology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822017000200225 |
Resumo: | Abstract Streptococcus pneumoniae is one of the most frequent opportunistic pathogens worldwide. DNA processing protein A (DprA) is an important factor involved in bacterial uptake and DNA integration into bacterial genome, but its role in S. pneumoniae virulence remains unclear. The aim of this study was to characterize the effects of the pneumococcal dprA gene on the pathogenesis of S. pneumoniae. To construct a dprA-deficient pneumococcal strain, the dprA gene of the S. pneumoniae strain D39 was inactivated. The virulence of this dprA-deficient strain, designated ΔD39, was compared with that of the wild-type strain by evaluating their respective capabilities to adhere to human pulmonary epithelial cells (PEC-A549) and by analyzing their choline-binding protein expression levels. In addition, the expression profiles of genes associated with virulence and host survival assays were also conducted with the mutant and the wild-type strain. Our results indicate that the capability of ΔD39 to adhere to the PEC-A549 airway cells was significantly lower (p < 0.01) compared with D39. Additionally, the 100-KD choline-binding protein was not detected in ΔD39. The addition of competence-stimulating peptide (CSP) lead to a significantly reduction of psaA mRNA expression in the dprA-deficient mutant and an increased level of psaA transcripts in the wild-type strain (p < 0.01). The median survival time of mice intraperitoneally infected with ΔD39 was significantly higher (p < 0.01) than that of mice infected with D39. The results of this study suggest that DprA has a significant effect on virulence characteristics of S. pneumoniae by influencing the expression of choline-binding protein and PsaA. |
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Brazilian Journal of Microbiology |
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The virulence of Streptococcus pneumoniae partially depends on dprAStreptococcus pneumoniaeDprATransformationVirulenceAbstract Streptococcus pneumoniae is one of the most frequent opportunistic pathogens worldwide. DNA processing protein A (DprA) is an important factor involved in bacterial uptake and DNA integration into bacterial genome, but its role in S. pneumoniae virulence remains unclear. The aim of this study was to characterize the effects of the pneumococcal dprA gene on the pathogenesis of S. pneumoniae. To construct a dprA-deficient pneumococcal strain, the dprA gene of the S. pneumoniae strain D39 was inactivated. The virulence of this dprA-deficient strain, designated ΔD39, was compared with that of the wild-type strain by evaluating their respective capabilities to adhere to human pulmonary epithelial cells (PEC-A549) and by analyzing their choline-binding protein expression levels. In addition, the expression profiles of genes associated with virulence and host survival assays were also conducted with the mutant and the wild-type strain. Our results indicate that the capability of ΔD39 to adhere to the PEC-A549 airway cells was significantly lower (p < 0.01) compared with D39. Additionally, the 100-KD choline-binding protein was not detected in ΔD39. The addition of competence-stimulating peptide (CSP) lead to a significantly reduction of psaA mRNA expression in the dprA-deficient mutant and an increased level of psaA transcripts in the wild-type strain (p < 0.01). The median survival time of mice intraperitoneally infected with ΔD39 was significantly higher (p < 0.01) than that of mice infected with D39. The results of this study suggest that DprA has a significant effect on virulence characteristics of S. pneumoniae by influencing the expression of choline-binding protein and PsaA.Sociedade Brasileira de Microbiologia2017-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822017000200225Brazilian Journal of Microbiology v.48 n.2 2017reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1016/j.bjm.2016.10.019info:eu-repo/semantics/openAccessYu,YiChang,DeXu,HuiwenZhang,XuelinPan,LeiXu,ChouHuang,BingZhou,HongLi,JiaGuo,JunLiu,Changtingeng2017-05-11T00:00:00Zoai:scielo:S1517-83822017000200225Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2017-05-11T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false |
dc.title.none.fl_str_mv |
The virulence of Streptococcus pneumoniae partially depends on dprA |
title |
The virulence of Streptococcus pneumoniae partially depends on dprA |
spellingShingle |
The virulence of Streptococcus pneumoniae partially depends on dprA Yu,Yi Streptococcus pneumoniae DprA Transformation Virulence |
title_short |
The virulence of Streptococcus pneumoniae partially depends on dprA |
title_full |
The virulence of Streptococcus pneumoniae partially depends on dprA |
title_fullStr |
The virulence of Streptococcus pneumoniae partially depends on dprA |
title_full_unstemmed |
The virulence of Streptococcus pneumoniae partially depends on dprA |
title_sort |
The virulence of Streptococcus pneumoniae partially depends on dprA |
author |
Yu,Yi |
author_facet |
Yu,Yi Chang,De Xu,Huiwen Zhang,Xuelin Pan,Lei Xu,Chou Huang,Bing Zhou,Hong Li,Jia Guo,Jun Liu,Changting |
author_role |
author |
author2 |
Chang,De Xu,Huiwen Zhang,Xuelin Pan,Lei Xu,Chou Huang,Bing Zhou,Hong Li,Jia Guo,Jun Liu,Changting |
author2_role |
author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Yu,Yi Chang,De Xu,Huiwen Zhang,Xuelin Pan,Lei Xu,Chou Huang,Bing Zhou,Hong Li,Jia Guo,Jun Liu,Changting |
dc.subject.por.fl_str_mv |
Streptococcus pneumoniae DprA Transformation Virulence |
topic |
Streptococcus pneumoniae DprA Transformation Virulence |
description |
Abstract Streptococcus pneumoniae is one of the most frequent opportunistic pathogens worldwide. DNA processing protein A (DprA) is an important factor involved in bacterial uptake and DNA integration into bacterial genome, but its role in S. pneumoniae virulence remains unclear. The aim of this study was to characterize the effects of the pneumococcal dprA gene on the pathogenesis of S. pneumoniae. To construct a dprA-deficient pneumococcal strain, the dprA gene of the S. pneumoniae strain D39 was inactivated. The virulence of this dprA-deficient strain, designated ΔD39, was compared with that of the wild-type strain by evaluating their respective capabilities to adhere to human pulmonary epithelial cells (PEC-A549) and by analyzing their choline-binding protein expression levels. In addition, the expression profiles of genes associated with virulence and host survival assays were also conducted with the mutant and the wild-type strain. Our results indicate that the capability of ΔD39 to adhere to the PEC-A549 airway cells was significantly lower (p < 0.01) compared with D39. Additionally, the 100-KD choline-binding protein was not detected in ΔD39. The addition of competence-stimulating peptide (CSP) lead to a significantly reduction of psaA mRNA expression in the dprA-deficient mutant and an increased level of psaA transcripts in the wild-type strain (p < 0.01). The median survival time of mice intraperitoneally infected with ΔD39 was significantly higher (p < 0.01) than that of mice infected with D39. The results of this study suggest that DprA has a significant effect on virulence characteristics of S. pneumoniae by influencing the expression of choline-binding protein and PsaA. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-06-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822017000200225 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822017000200225 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1016/j.bjm.2016.10.019 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
publisher.none.fl_str_mv |
Sociedade Brasileira de Microbiologia |
dc.source.none.fl_str_mv |
Brazilian Journal of Microbiology v.48 n.2 2017 reponame:Brazilian Journal of Microbiology instname:Sociedade Brasileira de Microbiologia (SBM) instacron:SBM |
instname_str |
Sociedade Brasileira de Microbiologia (SBM) |
instacron_str |
SBM |
institution |
SBM |
reponame_str |
Brazilian Journal of Microbiology |
collection |
Brazilian Journal of Microbiology |
repository.name.fl_str_mv |
Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM) |
repository.mail.fl_str_mv |
bjm@sbmicrobiologia.org.br||mbmartin@usp.br |
_version_ |
1752122208872824832 |