| Literature DB >> 18716756 |
Changjun Wang1, Ming Li, Youjun Feng, Feng Zheng, Yaqing Dong, Xiuzhen Pan, Gong Cheng, Ruiping Dong, Dan Hu, Xiaodan Feng, Junchao Ge, Di Liu, Jing Wang, Min Cao, Fuquan Hu, Jiaqi Tang.
Abstract
Sortase A (SrtA), originally identified as a transpeptidase in Staphylococcus aureus, plays key roles in full virulence of pathogenic bacteria. In silico genome-wide search suggested a srtA homologue from 05ZYH33, a Chinese human isolate of streptococcal toxic shock syndrome (STSS)-causing Streptococcus suis serotype 2 (S. suis 2, SS2). An isogenic srtA mutant (DeltasrtA) of 05ZYH33 strain was obtained by homologous recombination. Immunofluorescence analysis revealed that two known virulence-associated surface proteins featuring Leu-Pro-X-Thr-Gly motif, muramidase-released protein and surface antigen one, were absent in the DeltasrtA. Piglet infection experiments showed that deletion of srtA attenuated the full virulence of 05ZYH33 strain, and impaired its colonizing potential in specific organs. Furthermore, the DeltasrtA displayed significant reduction in adherence to human cells (Hep-2 and human umbilical vein endothelial cells). Collectively, we concluded that SrtA was involved in the virulence manifestation of STSS-causing SS2.Entities:
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Year: 2008 PMID： 18716756 DOI： 10.1007/s00203-008-0425-z
Source DB: PubMed Journal: Arch Microbiol ISSN： 0302-8933 Impact factor: 2.552