1. The involvement of sortase A in high virulence of STSS-causing Streptococcus suis serotype 2
- Author
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Gong Cheng, Youjun Feng, Jing Wang, Xiaodan Feng, Jiaqi Tang, Ruiping Dong, Ming Li, Changjun Wang, Yaqing Dong, Fuquan Hu, Di Liu, Dan Hu, Junchao Ge, Xiuzhen Pan, Feng Zheng, and Min Cao
- Subjects
Serotype ,Streptococcus suis ,Swine ,Virulence ,Biology ,medicine.disease_cause ,Biochemistry ,Microbiology ,Bacterial Adhesion ,Cell Line ,Random Allocation ,Antigen ,Bacterial Proteins ,Streptococcal Infections ,Genetics ,medicine ,Animals ,Humans ,Molecular Biology ,Cells, Cultured ,Streptococcus suis serotype 2 ,Endothelial Cells ,Pathogenic bacteria ,General Medicine ,Aminoacyltransferases ,Shock, Septic ,Cysteine Endopeptidases ,Staphylococcus aureus ,Sortase A ,Homologous recombination - 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.
- Published
- 2008