FEBS J. 2014 Jul 2. doi: 10.1111/febs.12903. [Epub ahead of print]
GHIP in Streptococcus pneumoniae is involved in antibacterial resistance and elicits a strong innate immune response through TLR2 and JNK/p38MAPK.
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Abstract
Interaction between pneumococcal virulence factors and innate immune receptors triggers host responses via specific signaling pathways after infection. By generating deficient mutant, we showed here that, compared with wild-type parent strain, glycosyl hydrolase 25 relating to invasion protein mutant strain was impaired in rapid dissemination into vessel and caused less severe inflammation in mice lungs. Further study demonstrated that the lack of this protein in Streptococcus pneumoniae caused an increased susceptibility to the whole blood or neutrophils, while this impairment could be recovered by supplementing recombinant GHIP (rGHIP). Additionally, secreted glycosyl hydrolase 25 relating to invasion protein could be detected in culture medium, and purified protein was capable to induce the release of tumor necrosis factor alpha and interleukin 6 from peritoneal macrophage. Further investigations revealed that the induction of interleukin 6 by this virulence factor depended on the phosphorylation of c-Jun N- terminal kinase and p38 mitogen activated protein kinase and Toll-like receptor 2. Taken together, glycosyl hydrolase 25 relating to invasion protein, a novel pneumococcal virulence factor, appeared to play a critical role in bacterial survival and the induction of host innate immune response during pneumococcal infection. This article is protected by copyright. All rights reserved.
This article is protected by copyright. All rights reserved.
KEYWORDS:
Streptococcus pneumoniae ; antibacterial resistance; glycosyl hydrolase 25; leukocytes recruitment; toll-like receptor 2
PMID: 24989111 [PubMed - as supplied by publisher]
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