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.
"Although the main function of these proteins remains unclear, they are known to influence the clinically relevant attributes of various gram-positive pathogens, such as cell division and septum formation (Chatfield et al., 2005; Hübscher et al., 2008; Johnsborg and Havarstein, 2009; Over et al., 2011). Recently, Minami et al. (2012) found that the lytR mutant strain of the gram-positive bacterium Streptococcus pyogenes had a higher activity of the cysteine protease SpeB and was more virulent than the wild-type strain. Consistent with the results of Dumas et al. (2008), the LytR protein of S. pyogenes (25% similar to the Lmo0443 protein of L. monocytogenes) seems to play an important role in the virulence of S. pyogenes. "
[Show abstract][Hide abstract] ABSTRACT: Abstract Bacterial exoproteomes vary in composition and quantity among species and within each species, depending on the environmental conditions to which the cells are exposed. This article critically reviews the literature available on exoproteins synthesized by the foodborne pathogenic bacterium Listeria monocytogenes grown at different temperatures. The main challenges posed for exoproteome analyses and the strategies that are being used to overcome these constraints are discussed. Over thirty exoproteins from L. monocytogenes are considered, and the multifunctionality of some of them is discussed. Thus, at the host temperature of 37°C, good examples are provided by Lmo0443, a potential marker for low virulence, and by the virulence factors internalin C (InlC) and listeriolysin O (LLO). Based on the reported LLO-induced mucin exocytosis, a model is proposed for the involvement of extracellular LLO in optimizing the conditions for InlC intervention in the invasion of intestinal epithelial cells. At lower growth temperatures, exoproteins such as flagellin (FlaA) and oligopeptide permease (OppA) may explain the persistence of particular strains in the food industry environment, eventually allowing the development of new tools to eradicate L. monocytogenes, a major concern for public health.
Omics A Journal of Integrative Biology 08/2014; DOI:10.1089/omi.2013.0151 · 2.36 Impact Factor
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