Abstract
A cyanogen bromide fragment derived from the K88ab adhesin inhibited the hemagglutinating activity of K88 fibrillae. Smaller fragments which inhibited the adherence of K88 fibrillae to erythrocytes or to intestinal epithelial cells were obtained by digestion of K88ab fibrillae with alpha-chymotrypsin. Active peptides were isolated from the digestion mixture and identified as Ser-Leu-Phe and Ala-Ile-Phe. Both tripeptides correspond to the peptide stretches Ser-148-Leu-Phe-150 and Ala-156-Ile-Phe-158, respectively, which are part of conserved regions in the primary structure of the K88 variants ab, ac, and ad. The isolated tripeptides inhibited the hemagglutinating activity of purified K88 fibrillae in the 1 to 5 microM range, while adherence of the fibrillae to intestinal epithelial cell brush borders was inhibited in the 10 to 50 microM range. Furthermore, the tripeptides were capable of eluting attached bacteria from agglutinated erythrocytes. The inhibitory activity of the isolated peptides was confirmed by testing various synthetic peptides for their ability to inhibit the interaction of the different K88 variants with various species of erythrocytes. The significance of these findings for the localization of the receptor-binding domain is discussed.
Full text
PDF






Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Ebberink R. H., van Loenhout H., Geraerts W. P., Joosse J. Purification and amino acid sequence of the ovulation neurohormone of Lymnaea stagnalis. Proc Natl Acad Sci U S A. 1985 Nov;82(22):7767–7771. doi: 10.1073/pnas.82.22.7767. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Falmagne P., Capiau C., Lambotte P., Zanen J., Cabiaux V., Ruysschaert J. M. The complete amino acid sequence of diphtheria toxin fragment B. Correlation with its lipid-binding properties. Biochim Biophys Acta. 1985 Jan 21;827(1):45–50. doi: 10.1016/0167-4838(85)90099-8. [DOI] [PubMed] [Google Scholar]
- Gaastra W., de Graaf F. K. Host-specific fimbrial adhesins of noninvasive enterotoxigenic Escherichia coli strains. Microbiol Rev. 1982 Jun;46(2):129–161. doi: 10.1128/mr.46.2.129-161.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Guinée P. A., Jansen W. H. Behavior of Escherichia coli K antigens K88ab, K88ac, and K88ad in immunoelectrophoresis, double diffusion, and hemagglutination. Infect Immun. 1979 Mar;23(3):700–705. doi: 10.1128/iai.23.3.700-705.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hacker J., Schmidt G., Hughes C., Knapp S., Marget M., Goebel W. Cloning and characterization of genes involved in production of mannose-resistant, neuraminidase-susceptible (X) fimbriae from a uropathogenic O6:K15:H31 Escherichia coli strain. Infect Immun. 1985 Feb;47(2):434–440. doi: 10.1128/iai.47.2.434-440.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hashimoto F., Horigome T., Kanbayashi M., Yoshida K., Sugano H. An improved method for separation of low-molecular-weight polypeptides by electrophoresis in sodium dodecyl sulfate-polyacrylamide gel. Anal Biochem. 1983 Feb 15;129(1):192–199. doi: 10.1016/0003-2697(83)90068-4. [DOI] [PubMed] [Google Scholar]
- Jacobs A. A., van Mechelen J. R., de Graaf F. K. Effect of chemical modifications on the K99 and K88ab fibrillar adhesins of Escherichia coli. Biochim Biophys Acta. 1985 Nov 29;832(2):148–155. doi: 10.1016/0167-4838(85)90326-7. [DOI] [PubMed] [Google Scholar]
- Lindberg F. P., Lund B., Normark S. Genes of pyelonephritogenic E. coli required for digalactoside-specific agglutination of human cells. EMBO J. 1984 May;3(5):1167–1173. doi: 10.1002/j.1460-2075.1984.tb01946.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Middeldorp J. M., Witholt B. K88-mediated binding of Escherichia coli outer membrane fragments to porcine intestinal epithelial cell brush borders. Infect Immun. 1981 Jan;31(1):42–51. doi: 10.1128/iai.31.1.42-51.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Mooi F. R., de Graaf F. K. Molecular biology of fimbriae of enterotoxigenic Escherichia coli. Curr Top Microbiol Immunol. 1985;118:119–138. doi: 10.1007/978-3-642-70586-1_7. [DOI] [PubMed] [Google Scholar]
- Mooi F. R., van Buuren M., Koopman G., Roosendaal B., de Graaf F. K. K88ab gene of Escherichia coli encodes a fimbria-like protein distinct from the K88ab fimbrial adhesin. J Bacteriol. 1984 Aug;159(2):482–487. doi: 10.1128/jb.159.2.482-487.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Norgren M., Normark S., Lark D., O'Hanley P., Schoolnik G., Falkow S., Svanborg-Edén C., Båga M., Uhlin B. E. Mutations in E coli cistrons affecting adhesion to human cells do not abolish Pap pili fiber formation. EMBO J. 1984 May;3(5):1159–1165. doi: 10.1002/j.1460-2075.1984.tb01945.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Proia R. L., Wray S. K., Hart D. A., Eidels L. Characterization and affinity labeling of the cationic phosphate-binding (nucleotide-binding) peptide located in the receptor-binding region of the B-fragment of diphtheria toxin. J Biol Chem. 1980 Dec 25;255(24):12025–12033. [PubMed] [Google Scholar]
- Schoolnik G. K., Fernandez R., Tai J. Y., Rothbard J., Gotschlich E. C. Gonococcal pili. Primary structure and receptor binding domain. J Exp Med. 1984 May 1;159(5):1351–1370. doi: 10.1084/jem.159.5.1351. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sparling P. F., Cannon J. G., So M. Phase and antigenic variation of pili and outer membrane protein II of Neisseria gonorrhoeae. J Infect Dis. 1986 Feb;153(2):196–201. doi: 10.1093/infdis/153.2.196. [DOI] [PubMed] [Google Scholar]