Focal targeting by human ß-defensin 2 disrupts localized virulence factor assembly sites in Enterococcus faecalis.
AuthorsKandaswamy K, Liew TH, Wang CY, Huston-Warren E, Meyer-Hoffert U, Hultenby K, Schröder JM, Caparon MG, Normark S, Henriques-Normark B, Hultgren SJ, Kline KA,
Journal
PubMed ID24191013
'Virulence factor secretion and assembly occurs at spatially restricted foci in some Gram-positive bacteria. Given the essentiality of the general secretion pathway in bacteria and the contribution of virulence factors to disease progression, the foci that coordinate these processes are attractive antimicrobial targets. In this study, we show in Enterococcus ... More
Serum amyloid A3 binds MD-2 to activate p38 and NF-?B pathways in a MyD88-dependent manner.
AuthorsDeguchi A, Tomita T, Omori T, Komatsu A, Ohto U, Takahashi S, Tanimura N, Akashi-Takamura S, Miyake K, Maru Y,
Journal
PubMed ID23858030
Serum amyloid A (SAA) 3 is a major component of the acute phase of inflammation. We previously reported that SAA3 served as an endogenous peptide ligand for TLR4 to facilitate lung metastasis. Because these experiments were performed with SAA3 recombinant proteins purified from Escherichia coli or mammalian cells, we could ... More
LytA, major autolysin of Streptococcus pneumoniae, requires access to nascent peptidoglycan.
The pneumococcal autolysin LytA is a virulence factor involved in autolysis as well as in fratricidal- and penicillin-induced lysis. In this study, we used biochemical and molecular biological approaches to elucidate which factors control the cytoplasmic translocation and lytic activation of LytA. We show that LytA is mainly localized intracellularly, ... More