Induction of De Novo Subcortical Actin Filament Assembly by Treponema denticola Major Outer Sheath Protein

AUTOR(ES)

Amin, Mohsen

FONTE

American Society for Microbiology

RESUMO

Treponema denticola and its major outer sheath protein (Msp) induce actin reorganization in fibroblasts. We adapted a barbed-end labeling/imaging assay to monitor Msp-induced subcortical actin filament assembly in neutrophils and fibroblasts. Msp, at an actin-reorganizing concentration, inhibited migration of these dissimilar cell types, whose cytoskeletal functions in locomotion and phagocytosis are crucial for immunity and healing of peripheral infections.

Documentos Relacionados

• Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola.
• Proteases of Treponema denticola outer sheath and extracellular vesicles.
• Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola.
• Chemical and biological activities of a 64-kilodalton outer sheath protein from Treponema denticola strains.
• Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola