Inhibition
of S-fimbria-mediated adhesion to human ileostomy glycoproteins by
a protein isolated from bovine colostrum
AC Ouwehand, PL
Conway and SJ Salminen
Department of General and Marine Microbiology, Goteborg University,
Sweden.
The aim of this study was to isolate and purify the component in bovine
colostrum which is responsible for the inhibition of S-fimbria-mediated
adhesion of Escherichia coli. Whey from defatted colostrum was fractionated
by ultrafiltration, and the < 100K, < 30K, and < 10K fractions
and the colostral whey were tested for inhibition of in vitro adhesion
of radiolabelled S-fimbria-bearing E. coli to human ileostomy glycoproteins,
which provide a model for human intestinal mucus. The inhibiting compound
was purified from a dialyzed < 30K fraction with an anion exchange
column which was eluted with a NaCl gradient (0 to 1.0 M). The compound
was found to be a heat-resistant but pepsin-sensitive protein with
an Mr of approximately 18,000 and an isoelectric point of approximately
5.75. The protein appears to block receptor sites for S- fimbriae
on ileostomy glycoproteins, with steric hindrance being the most likely
mechanism. Analysis of the amino acid sequence of the amino terminus
of the 18K protein showed similarity with the sequence of beta- lactoglobulin.
Arch. Dis. Child.
1994 70: c356-c357.
Bovine colostrum immunoglobulin concentrate for cryptosporidiosis
in AIDS
P Heaton
Archives of Disease in Childhood, Vol 69, 451-453, Copyright 1993
by Archives of Disease in Childhood.
Articles
22
