Fibronectin tetrapeptide is target for syphilis spirochete cytadherence
The syphilis bacterium, Treponema pallidum, parasitizes host cells through recognition of fibronectin (Fn) on cell surfaces. The active site of the Fn molecule has been identified as a four-amino acid sequence, arg-gly-asp-ser (RGDS), located on each monomer of the cell-binding domain. The synthetic heptapeptide gly-arg-gly-asp-ser-pro-cys (GRGDSPC), with the active site sequence RGDS, specifically competed with SVI-labeled cell-binding domain acquisition by T. pallidum. Additionally, the same heptapeptide with the RGDS sequence diminished treponemal attachment to HEp-2 and HT1080 cell monolayers. Related heptapeptides altered in one key amino acid within the RGDS sequence failed to inhibit Fn cell-binding domain acquisition or parasitism of host cells by T. pallidum. The data support the view that T. pallidum cytadherence of host cells is through recognition of the RGDS sequence also important for eukaryotic cell-Fn binding.
- Research Organization:
- Univ. of Texas Health Science Center, San Antonio
- OSTI ID:
- 6296926
- Journal Information:
- J. Exp. Med.; (United States), Journal Name: J. Exp. Med.; (United States) Vol. 5; ISSN JEMEA
- Country of Publication:
- United States
- Language:
- English
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62 RADIOLOGY AND NUCLEAR MEDICINE
BACTERIA
BETA DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CELL CONSTITUENTS
CELL MEMBRANES
DAYS LIVING RADIOISOTOPES
DIAGNOSTIC USES
ELECTRON CAPTURE RADIOISOTOPES
ENZYMES
HYDROLASES
IMMUNOLOGY
INTERMEDIATE MASS NUCLEI
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IODINE ISOTOPES
ISOTOPES
KINETICS
LEUKOCYTES
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MEMBRANES
MICROORGANISMS
MONOCYTES
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PROTEINS
RADIOISOTOPES
SERINE PROTEINASES
SPIROCHAETES
TRYPSIN
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