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
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