S-Space College of Medicine/School of Medicine (의과대학/대학원) Microbiology (미생물학전공) Journal Papers (저널논문_미생물학전공)
Fibronectin facilitates the invasion of Orientia tsutsugamushi into host cells through interaction with a 56-kDa type-specific antigen
- Lee, Jung-Hee; Cho, Nam-Hyuk; Kim, Se-Yoon; Bang, Sun-Young; Chu, Hyuk; Choi, Myung-Sik; Kim, Ik-Sang
- Issue Date
- University of Chicago Press
- J Infect Dis. 2008 Jul 15;198(2):250-7.
- Animals; Antigens, Bacterial/*physiology; Bacterial Adhesion/*physiology; Binding Sites; Cell Division; Fibronectins/*physiology; Glutathione Transferase/metabolism; Humans; L Cells (Cell Line); Mice; Orientia tsutsugamushi/*pathogenicity; Recombinant Proteins/metabolism; Serum Albumin, Bovine/physiology
- BACKGROUND: Orientia tsutsugamushi, the causative agent of scrub typhus, is an obligate intracellular bacterium. The pathogen's mechanism of cellular invasion is poorly characterized. METHODS: Through ligand immunoblots, glutathione S-transferase (GST) pull-down assays, and in vitro inhibition assays of intracellular invasion, a bacterial ligand was identified and was shown to interact with fibronectin (Fn) to enhance the intracellular invasion of O. tsutsugamushi. RESULTS: O. tsutsugamushi can bind to immobilized Fn in vitro, and exogenous Fn stimulates bacterial invasion of mammalian host cells. Bacterial invasion in the presence of Fn was abrogated by the addition of Arg-Gly-Asp peptides or by an anti-alpha5beta1 integrin antibody. Through a ligand immunoblot and GST pull-down assay, a 56-kDa type-specific antigen (TSA56) was identified as the bacterial ligand responsible for the interaction with Fn. Antigenic domain III and the adjacent C-terminal region (aa 243-349) of TSA56 interacted with Fn. Furthermore, we found that the enhanced invasion of the pathogen was abrogated by the addition of purified recombinant peptides derived from TSA56. CONCLUSION: Fn facilitates the invasion of O. tsutsugamushi through its interaction with TSA56.
- 0022-1899 (Print)