Open AccessThe erythrocyte receptor for Fusobacterium necrophorum hemolysin: phosphatidylcholine as a possible candidate
Author(s) -
Amoako Kingsley Kwaku,
Goto Yoshitaka,
Misawa Naoaki,
Xu De Long,
Shinjo Toshiharu
Publication year - 1998
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.1574-6968.1998.tb13256.x
Subject(s) - hemolysin , fusobacterium necrophorum , biochemistry , biology , phosphatidylcholine , phospholipase , phospholipase c , trypsin , red blood cell , phospholipase a2 , microbiology and biotechnology , receptor , chemistry , membrane , enzyme , phospholipid , virulence , gene
An attempt was made to determine the receptor for the hemolysin of Fusobacterium necrophorum using horse erythrocyte or its membranes as target. The spectrum of erythrocyte sensitivity has indicated that horse, dog and mouse erythrocytes are highly sensitive whereas cattle, sheep, goat and chicken red blood cells are insensitive to this hemolysin. A high correlation between sensitivity and phosphatidylcholine content of the erythrocyte membranes was noted. Binding of hemolysin to horse erythrocyte membranes was reduced significantly by prior treatment of membranes with phospholipase A 2 but not with phospholipase C. Pretreatment of erythrocyte membranes with pronase, proteinase K, trypsin or neuraminidase did not alter binding of hemolysin to the membranes, suggesting that protein or sialyl residues are not involved as receptors. Gas liquid chromatography analysis showed that the fatty acid profile from hydrolysis of bovine liver phosphatidylcholine by hemolysin and phospholipase A 2 were similar. In conclusion, this report presents evidence that phosphatidylcholine may be acting as a possible receptor for the hemolysin of F. necrophorum .