Glycoprotein glycans that inhibit adhesion of Escherichia coli mediated by K99 fimbriae: treatment of experimental colibacillosis.

نویسندگان

  • M Mouricout
  • J M Petit
  • J R Carias
  • R Julien
چکیده

Calf diarrhea due to infection by enterotoxigenic Escherichia coli was treated by administration of glycoprotein glycans derived from bovine plasma. The glycan moieties of the nonimmunoglobulin fraction of plasma mimicked the oligosaccharide moiety of intestinal receptors recognized by K99 pili. These glycoprotein glycans inhibited adhesion of E. coli K99+ ST+ to erythrocyte glycoconjugates in vitro, and they protected colostrum-deprived newborn calves against lethal doses of enterotoxigenic E. coli (10(10) bacteria). Adhesion of bacteria to the intestines (duodenum, jejunum, and ileum) was significantly reduced (by 2 orders of magnitude) in treated calves.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Efficacy of dietary supplementation of bacteriophages in treatment of concurrent infections with enterotoxigenic <em>Escherichia coli</em> K88 and K99 in postweaning pigs

Postweaning diarrhea or colibacillosis is a costly disease causing substantial mortality, as well as growth retardation, in swine production.1-3 Colibacillosis is typically associated with avid intestinal adhesion and fecal shedding of enterotoxigenic Escherichia coli (ETEC). The ETEC causing diarrhea in postweaning pigs carries the F4 (K88) or F18 fimbrial antigen in most cases.4-6 The F5 (K99...

متن کامل

Swine enteric colibacillosis: diagnosis, therapy and antimicrobial resistance

Intestinal infection with enterotoxigenic Escherichia coli (ETEC) is an important disease in swine resulting in significant economic losses. Knowledge about the epidemiology, the diagnostic approach and methods of control are of fundamental importance to tackle the disease. The ETEC causing neonatal colibacillosis mostly carry the fimbriae F4 (k88), F5 (k99), F6 (987P) or F41, while the ETEC of...

متن کامل

ISOLATION BY PHAGE DISPLAY OF SINGLE-CHAIN Fv ANTIBODIES AGAINST Escerichia coli K99 FIMBRIAE

Single-chain antibodies (scFv) are small, recombinant proteins in which variable domains from immunoglobulin heavy and light chains are physically linked with a flexible peptide. They are monovalent and lack the heavy chain constant domins for activation of complement and binding to cellular receptors. However scFvs can possess biological activity by binding to and inhibiting the action of thei...

متن کامل

Isolation and structural characterization of the equine erythrocyte receptor for enterotoxigenic Escherichia coli K99 fimbrial adhesin.

The erythrocyte receptor for Escherichia coli K99 fimbrial adhesin was isolated from equine erythrocytes and characterized as Neu5Gc-alpha(2----3)-Galp-beta(1----4)-GLcp-beta(1----1)-Ceramide. This glycolipid acted as the receptor for K99 by four different experimental approaches: inhibition of equine erythrocyte hemagglutination by preincubation of K99-positive bacteria or purified K99 fimbria...

متن کامل

Glycosylation changes as important factors for the susceptibility to urinary tract infection.

FimH is the type 1 fimbrial tip adhesin and invasin of Escherichia coli. Its ligands are the glycans on specific proteins enriched in membrane microdomains. FimH binding shows high-affinity recognition of paucimannosidic glycans, which are shortened high-mannose glycans such as oligomannose-3 and -5. FimH can recognize equally the (single) high-mannose glycan on uroplakin Ia, on the urinary def...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Infection and immunity

دوره 58 1  شماره 

صفحات  -

تاریخ انتشار 1990