[Is the Arg-Gly-Asp sequence the site for foot-and-mouth disease virus binding with cell receptor?].
The Arg-Gly-Asp sequence is being found in an increasing wide range of proteins with "adhesive" function. Studying a series of synthetic peptide fragments of VP1 protein of FMDV, we showed that peptides containing the Arg-Gly-Asp sequence, but not control peptides, inhibited FMDV binding to pig kidney cells in vitro, thus indicating participation of that sequence in FMDV binding to host cells.
Surovoĭ
A Iu
AIu
Ivanov
V T
VT
Chepurkin
A V
AV
Ivaniushchenkov
V N
VN
Driagalin
N N
NN
D000595:Amino Acid Sequence; D000818:Animals; D005537:Aphthovirus / Q000276:immunology / Q000378:metabolism*; D001120:Arginine; D001224:Aspartic Acid; D002478:Cells, Cultured; D004338:Drug Combinations; D005998:Glycine; D008969:Molecular Sequence Data; D011991:Receptors, Virus / Q000378:metabolism*; D013552:Swine; D014764:Viral Proteins / Q000276:immunology
D004338:Drug Combinations; D011991:Receptors, Virus; D014764:Viral Proteins; D001224:Aspartic Acid; D001120:Arginine; D005998:Glycine
Iavliaetsia li posledovatel'nost' Arg-Gly-Asp uchastkom sviazyvaniia virusa iashchura s kletochnym retseptorom?