The cell envelope-associated protein, LytR, regulates the cysteine protease SpeB in Streptococcus pyogenes
Article first published online: 8 DEC 2011
© 2011 The Authors. APMIS © 2011 APMIS
Volume 120, Issue 5, pages 417–426, May 2012
How to Cite
MINAMI, M., ICHIKAWA, M., OHTA, M. and HASEGAWA, T. (2012), The cell envelope-associated protein, LytR, regulates the cysteine protease SpeB in Streptococcus pyogenes. APMIS, 120: 417–426. doi: 10.1111/j.1600-0463.2011.02847.x
- Issue published online: 19 APR 2012
- Article first published online: 8 DEC 2011
- Received 30 June 2011. Accepted 2 November 2011
- Streptococcus pyogenes;
Minami M, Ichikawa M, Ohta M, Hasegawa T. The cell envelope-associated protein, LytR, regulates the cysteine protease SpeB in Streptococcus pyogenes. APMIS 2012; 120: 417–26.
The LytR family of cell envelope-associated transcriptional attenuators in bacteria has been brought into focus of scientific interest on the expression of various virulence factors, as well as bacterial cell envelope maintenance. However, this protein of Streptococcus pyogenes has been only described as cell surface-associated protein, and its function is completely unknown. We created lytR mutant strains from two independent S. pyogenes strains to analyze the function of LytR. The protease assay in culture supernatant showed that lytR mutant had the higher cysteine protease activity than wild-type. Two-dimensional gel electrophoresis and western blotting analysis revealed that the amount of cysteine protease, SpeB in lytR mutant was more compared with that in wild-type. The level of speB mRNA in lytR mutant also increased compared with that of wild-type. The membrane integrity and potential in lytR mutant also were decreased compared with that of wild-type. Murine infection model showed that less survival was detected in mice inoculated with lytR mutant than that with wild-type, and the size of wound lesion of mice with lytR mutant was larger than that with wild-type. Our data suggest that the lytR regulates the expression of SpeB in S. pyogenes with relation to membrane integrity.