Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola
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چکیده
منابع مشابه
Modulation of human neutrophil functions in vitro by Treponema denticola major outer sheath protein.
In this study of human polymorphonuclear leukocytes (PMNs), pretreatment with Treponema denticola major outer sheath protein (Msp) inhibited formyl-methionyl-leucyl-phenylalanine (fMLP)-induced chemotaxis, phagocytosis of immunoglobulin G-coated microspheres, fMLP-stimulated calcium transients, and actin assembly. Msp neither altered oxidative responses to phorbol myristate or fMLP nor induced ...
متن کاملActivation of MAPK in fibroblasts by Treponema denticola major outer sheath protein.
The major outer sheath protein (Msp) of Treponema denticola induces Ca(2+) entry and actin reorganization in cultured fibroblasts, but the pathways by which Msp mediates these responses are not yet defined. We considered that Msp may activate protein kinases as a stress response that precedes actin remodelling. Phospho-kinase screens showed that Msp induced phosphorylation of multiple kinases i...
متن کاملBinding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405.
There is growing evidence that a number of oral Treponema species, in particular Treponema denticola, are associated with the progression of human periodontal disease. The major sheath (or surface) protein (Msp) of T. denticola is implicated in adhesion of bacteria to host cells and tissue proteins and is likely to be an important virulence factor. However, the binding regions of the Msp are no...
متن کاملTreponema denticola Major Outer Sheath Protein Impairs the Cellular Phosphoinositide Balance That Regulates Neutrophil Chemotaxis
The major outer sheath protein (Msp) of Treponema denticola inhibits neutrophil polarization and directed chemotaxis together with actin dynamics in vitro in response to the chemoattractant N-formyl-methionine-leucine-phenylanine (fMLP). Msp disorients chemotaxis through inhibition of a Rac1-dependent signaling pathway, but the upstream mechanisms are unknown. We challenged murine bone marrow n...
متن کاملDentilisin activity affects the organization of the outer sheath of Treponema denticola.
Prolyl-phenylalanine-specific serine protease (dentilisin) is a major extracellular protease produced by Treponema denticola. The gene, prtP, coding for the protease was recently cloned and sequenced (K. Ishihara, T. Miura, H. K. Kuramitsu, and K. Okuda, Infect. Immun. 64:5178-5186, 1996). In order to determine the role of this protease in the physiology and virulence of T. denticola, a dentili...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1996
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.178.9.2489-2497.1996