Role of sortase A in the pathogenesis of Staphylococcus aureus‐induced mastitis in mice. Issue 1 (22nd January 2014)
- Record Type:
- Journal Article
- Title:
- Role of sortase A in the pathogenesis of Staphylococcus aureus‐induced mastitis in mice. Issue 1 (22nd January 2014)
- Main Title:
- Role of sortase A in the pathogenesis of Staphylococcus aureus‐induced mastitis in mice
- Authors:
- Chen, Fuguang
Liu, Bingrun
Wang, Dacheng
Wang, Lin
Deng, Xuming
Bi, Chongwei
Xiong, Ying
Wu, Qianchao
Cui, Yiwen
Zhang, Yong
Li, Xinlan
Wang, Ying
Liu, Bo
Cao, Yongguo - Abstract:
- <abstract abstract-type="main" id="fml12354-abs-0001"> <title>Abstract</title> <p>Sortase A (SrtA), a transpeptidase, anchors surface proteins with an LPXTG‐motif sorting signal to the cell envelope. To determine the role of SrtA in the pathogenesis of <italic>Staphylococcus aureus</italic>, we constructed a mutant strain, ∆SrtA, by genetic techniques and identified its functions in a <italic>S. aureus</italic>‐induced mastitis mouse model. The histological and myeloperoxidase (MPO) level results showed that the ∆SrtA strain attenuated the inflammatory reaction in the mammary tissue of mice compared with wild‐type <italic>S. aureus</italic> challenge. Additionally, the ELISA results showed that the ∆SrtA strain impaired the induction of pro‐inflammatory cytokines such as tumor necrosis factor‐α (TNF‐α), interleukin‐1β (IL‐1β) and interleukin‐6 (IL‐6), and the Western blot results showed that the mutant strain blocked the activation of nuclear factor‐κB (NF‐κB) and mitogen‐activated protein kinases (MAPKs) by attenuating the degradation and phosphorylation of signaling pathway molecules such as IκBα, p65 and p38. These results suggest that SrtA is a key virulence factor in the pathogenesis of <italic>S. aureus</italic>‐induced mastitis in mice. It appears that the <italic>srtA</italic> mutant affected the attachment of <italic>S. aureus</italic> to host cells, thus attenuating the activation of the NF‐κB and MAPK signaling pathways, which regulated the expression of<abstract abstract-type="main" id="fml12354-abs-0001"> <title>Abstract</title> <p>Sortase A (SrtA), a transpeptidase, anchors surface proteins with an LPXTG‐motif sorting signal to the cell envelope. To determine the role of SrtA in the pathogenesis of <italic>Staphylococcus aureus</italic>, we constructed a mutant strain, ∆SrtA, by genetic techniques and identified its functions in a <italic>S. aureus</italic>‐induced mastitis mouse model. The histological and myeloperoxidase (MPO) level results showed that the ∆SrtA strain attenuated the inflammatory reaction in the mammary tissue of mice compared with wild‐type <italic>S. aureus</italic> challenge. Additionally, the ELISA results showed that the ∆SrtA strain impaired the induction of pro‐inflammatory cytokines such as tumor necrosis factor‐α (TNF‐α), interleukin‐1β (IL‐1β) and interleukin‐6 (IL‐6), and the Western blot results showed that the mutant strain blocked the activation of nuclear factor‐κB (NF‐κB) and mitogen‐activated protein kinases (MAPKs) by attenuating the degradation and phosphorylation of signaling pathway molecules such as IκBα, p65 and p38. These results suggest that SrtA is a key virulence factor in the pathogenesis of <italic>S. aureus</italic>‐induced mastitis in mice. It appears that the <italic>srtA</italic> mutant affected the attachment of <italic>S. aureus</italic> to host cells, thus attenuating the activation of the NF‐κB and MAPK signaling pathways, which regulated the expression of pro‐inflammatory cytokines and decreased the susceptibility to mastitis.</p> </abstract> … (more)
- Is Part Of:
- FEMS microbiology letters. Volume 351:Issue 1(2014:Feb.)
- Journal:
- FEMS microbiology letters
- Issue:
- Volume 351:Issue 1(2014:Feb.)
- Issue Display:
- Volume 351, Issue 1 (2014)
- Year:
- 2014
- Volume:
- 351
- Issue:
- 1
- Issue Sort Value:
- 2014-0351-0001-0000
- Page Start:
- 95
- Page End:
- 103
- Publication Date:
- 2014-01-22
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1574-6968/issues ↗
http://www.sciencedirect.com/science/journal/03781097 ↗
http://onlinelibrary.wiley.com/ ↗
http://femsle.oxfordjournals.org/content/ ↗
http://firstsearch.oclc.org ↗ - DOI:
- 10.1111/1574-6968.12354 ↗
- Languages:
- English
- ISSNs:
- 0378-1097
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3905.300000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3224.xml