
Calf small intestine receptors for K99 fimbriated enterotoxeginic Escherichia coli
Author(s) -
Teneberg Susann,
Willemsen Peter Th.J.,
Graaf Frits K.,
Karlsson KarlAnders
Publication year - 1993
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.1574-6968.1993.tb06151.x
Subject(s) - glycolipid , fimbria , escherichia coli , pilus , enterobacteriaceae , receptor , biochemistry , bacteria , small intestine , chemistry , biology , microbiology and biotechnology , genetics , gene
Non‐acid and acid glycolipids were isolated from the small intestine of a newborn calf and tested for the ability to bind Escherichia coli carrying K99 fimbriae. The bacteria did not bind to any of the non‐acid glycolipids, whereas in the acid glycolipid fraction several gangliosides were detected which bind to K99 fimbriae. Gangliosides capable of binding K99 fimbriated E. coli were characterized as NeuGc‐GM3, NeuGc‐GM2, NeuGc‐GD1a NeuAc‐SPG and NeuAc‐SPG. No binding was detected to NeuAc‐GM3 and NeuGc‐GM1.