Open AccessBiological role of an arginine residue present in a histidine‐rich peptide which inhibits hemagglutination of Porphyromonas gingivalis
Author(s) -
Murakami Yukitaka,
Tamagawa Hiroo,
Shizukuishi Satoshi,
Tsunemitsu Akira,
Aimoto Saburo
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05514.x
Subject(s) - porphyromonas gingivalis , arginine , histidine , peptide , microbiology and biotechnology , chemistry , residue (chemistry) , hemagglutination , biochemistry , biology , bacteria , amino acid , immunology , antibody , genetics
Inhibitory effects of synthetic fragments in histatin 8, having the sequence Lys‐Phe‐His‐Glu‐Lys‐His‐His‐Ser‐His‐Arg‐Gly‐Tyr, on hemagglutination by Porphyromonas gingivalis 381 were examined. The hemagglutinating activity was reduced much more by the peptide Lys‐His‐His‐Ser‐His‐Arg‐Gly‐Tyr than by the peptides Lys‐His‐His=Ser‐His and/or Lys‐Phe‐His‐Glu‐Lys. These results suggest that the arginine residue may have an important role in the inhibition of hemagglutination by P. gingivalis .