Fibronectin tetrapeptide is target for syphilis spirochete cytadherence

Journal Article · Fri Nov 01 00:00:00 EST 1985 · J. Exp. Med.; (United States)

DOI:https://doi.org/10.1084/jem.162.5.1715· OSTI ID:6296926

Thomas, D D; Baseman, J B; Alderete, J F

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), Vol. 5
• Country of Publication: United States
• Language: English

Related Subjects

62 RADIOLOGY AND NUCLEAR MEDICINE
IODINE 125
DIAGNOSTIC USES
SPIROCHAETES
IMMUNOLOGY
CELL MEMBRANES
KINETICS
MONOCYTES
PROTEINS
TRYPSIN
BACTERIA
BETA DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CELL CONSTITUENTS
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
ENZYMES
HYDROLASES
INTERMEDIATE MASS NUCLEI
IODINE ISOTOPES
ISOTOPES
LEUKOCYTES
MATERIALS
MEMBRANES
MICROORGANISMS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
RADIOISOTOPES
SERINE PROTEINASES
USES
550601* - Medicine- Unsealed Radionuclides in Diagnostics