Back to Search
Start Over
CrfP, a fratricide protein, contributes to natural transformation in Streptococcus suis
- Source :
- Veterinary Research, Vol 52, Iss 1, Pp 1-14 (2021)
- Publication Year :
- 2021
- Publisher :
- BMC, 2021.
-
Abstract
- 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.
- Subjects :
- S. suis
CrfP
Murein hydrolase
Competence
Virulence
Veterinary medicine
SF600-1100
Subjects
Details
- Language :
- English
- ISSN :
- 12979716
- Volume :
- 52
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Veterinary Research
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.f651e2415ed4376b7eb203c667351fe
- Document Type :
- article
- Full Text :
- https://doi.org/10.1186/s13567-021-00917-x