CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis

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 mechan...

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Main Authors: Yinchu Zhu, Jiale Ma, Yue Zhang, Xiaojun Zhong, Qiankun Bai, Wenyang Dong, Zihao Pan, Guangjin Liu, Cun Zhang, Huochun Yao
Format: Article
Language:English
Published: BMC 2021-03-01
Series:Veterinary Research
Subjects:
Online Access:https://doi.org/10.1186/s13567-021-00917-x
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author Yinchu Zhu
Jiale Ma
Yue Zhang
Xiaojun Zhong
Qiankun Bai
Wenyang Dong
Zihao Pan
Guangjin Liu
Cun Zhang
Huochun Yao
author_facet Yinchu Zhu
Jiale Ma
Yue Zhang
Xiaojun Zhong
Qiankun Bai
Wenyang Dong
Zihao Pan
Guangjin Liu
Cun Zhang
Huochun Yao
author_sort Yinchu Zhu
collection DOAJ
description 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 (ΔcrfP) 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.
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spelling doaj.art-cf651e2415ed4376b7eb203c667351fe2022-12-21T22:24:26ZengBMCVeterinary Research1297-97162021-03-0152111410.1186/s13567-021-00917-xCrfP, a fratricide protein, contributes to natural transformation in Streptococcus suisYinchu Zhu0Jiale Ma1Yue Zhang2Xiaojun Zhong3Qiankun Bai4Wenyang Dong5Zihao Pan6Guangjin Liu7Cun Zhang8Huochun Yao9Institute of Animal Husbandry and Veterinary Sciences, Zhejiang Academy of Agricultural SciencesCollege of Veterinary Medicine, Nanjing Agricultural UniversityCollege of Veterinary Medicine, Nanjing Agricultural UniversityCollege of Veterinary Medicine, Nanjing Agricultural UniversityCollege of Veterinary Medicine, Nanjing Agricultural UniversityCollege of Veterinary Medicine, Nanjing Agricultural UniversityCollege of Veterinary Medicine, Nanjing Agricultural UniversityCollege of Veterinary Medicine, Nanjing Agricultural UniversityInstitute of Animal Husbandry and Veterinary Sciences, Zhejiang Academy of Agricultural SciencesCollege of Veterinary Medicine, Nanjing Agricultural UniversityAbstract 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 (ΔcrfP) 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.https://doi.org/10.1186/s13567-021-00917-xS. suisCrfPMurein hydrolaseCompetenceVirulence
spellingShingle Yinchu Zhu
Jiale Ma
Yue Zhang
Xiaojun Zhong
Qiankun Bai
Wenyang Dong
Zihao Pan
Guangjin Liu
Cun Zhang
Huochun Yao
CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis
Veterinary Research
S. suis
CrfP
Murein hydrolase
Competence
Virulence
title CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis
title_full CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis
title_fullStr CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis
title_full_unstemmed CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis
title_short CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis
title_sort crfp a fratricide protein contributes to natural transformation in streptococcus suis
topic S. suis
CrfP
Murein hydrolase
Competence
Virulence
url https://doi.org/10.1186/s13567-021-00917-x
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