| Title: | "CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis" |
| Author(s): | Zhu Y; Ma J; Zhang Y; Zhong X; Bai Q; Dong W; Pan Z; Liu G; Zhang C; Yao H; |
| Address: | "Institute of Animal Husbandry and Veterinary Sciences, Zhejiang Academy of Agricultural Sciences, Hangzhou, 310021, China. College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, 210095, China. Key Lab of Animal Bacteriology, Ministry of Agriculture, Nanjing, 210095, China. OIE Reference Lab for Swine Streptococcosis, Nanjing, 210095, China. College of Animal Science and Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450000, China. College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, 210095, China. yaohch@njau.edu.cn. Key Lab of Animal Bacteriology, Ministry of Agriculture, Nanjing, 210095, China. yaohch@njau.edu.cn. OIE Reference Lab for Swine Streptococcosis, Nanjing, 210095, China. yaohch@njau.edu.cn" |
| DOI: | 10.1186/s13567-021-00917-x |
| ISSN/ISBN: | 1297-9716 (Electronic) 0928-4249 (Print) 0928-4249 (Linking) |
| Abstract: | "Streptococcus suis (S. suis) is an important zoonotic pathogen that causes septicaemia, meningitis and streptococcal toxic shock-like syndrome in its host, and recent studies have shown that S. suis could be competent for natural genetic transformation. Transformation is an important mechanism for the horizontal transfer of DNA, but some elements that affect the transformation process need to be further explored. Upon entering the competent state, Streptococcus species stimulate the transcription of competence-related genes that are responsible for exogenous DNA binding, uptake and processing. In this study, we performed conserved promoter motif and qRT-PCR analyses and identified CrfP as a novel murein hydrolase that is widespread in S. suis and stimulated with a peptide pheromone in the competent state through a process controlled by ComX. A bioinformatics analysis revealed that CrfP consists of a CHAP hydrolase domain and two bacterial Src homology 3-binding (SH3b) domains. Further characterization showed that CrfP could be exported to extracellular bacterial cells and lytic S. suis strains of different serotypes, and this finding was verified by TEM and a turbidity assay. To investigate the potential effect of CrfP in vivo, a gene-deletion mutant (DeltacrfP) was constructed. Instead of stopping the natural transformation process, the inactivation of CrfP clearly reduced the effective transformation rate. Overall, these findings provide evidence showing that CrfP is important for S. suis serovar 2 competence" |
| Keywords: | "Animals Bacterial Proteins/*genetics/metabolism Gene Deletion Hydrolases/*genetics/metabolism Serogroup Streptococcal Infections/microbiology/*veterinary Streptococcus suis/enzymology/*genetics Sus scrofa Swine Swine Diseases/*microbiology Transformation, ;" |
| Notes: | "MedlineZhu, Yinchu Ma, Jiale Zhang, Yue Zhong, Xiaojun Bai, Qiankun Dong, Wenyang Pan, Zihao Liu, Guangjin Zhang, Cun Yao, Huochun eng (31972650)/Natural Science Foundation of China/ S0201700386/Shanghai Agriculture Applied Technology Development Program/ (KJQN201932)/the Key Project of Independent Innovation of the Fundamental Research Fund for the Central Universities of Nanjing Agricultural University/ England 2021/03/26 Vet Res. 2021 Mar 24; 52(1):50. doi: 10.1186/s13567-021-00917-x" |
