This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Grange, P. A.
Right arrow Articles by Francis, D. H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Grange, P. A.
Right arrow Articles by Francis, D. H.

 Previous Article  |  Next Article 

Infection and Immunity, January 1999, p. 165-172, Vol. 67, No. 1
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Identification of an Intestinal Neutral Glycosphingolipid as a Phenotype-Specific Receptor for the K88ad Fimbrial Adhesin of Escherichia colidagger

Philippe A. Grange,1 Alan K. Erickson,1,* Steven B. Levery,2 and David H. Francis1

Department of Veterinary Science, South Dakota State University, Brookings, South Dakota 57007,1 and Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 306022

Received 18 June 1998/Returned for modification 7 August 1998/Accepted 23 October 1998

In this study, we identified a receptor for the K88ad fimbrial adhesin of Escherichia coli in neutral glycosphingolipid preparations from intestinal epithelial cells of K88ad-adhesive pigs, which was absent in preparations from K88ad-nonadhesive pigs. Neither K88ab nor K88ac adhesin variants bound to this neutral glycosphingolipid. Because this receptor is an intestinal glycosphingolipid that binds K88ad adhesin, it has been designated IGLad. Carbohydrate compositional analysis of a partially purified preparation of IGLad identified galactose, glucose, and N-acetylglucosamine in a ratio of 1.5:1.0:0.5 as the major monosaccharides. Preliminary characterization experiments using lectins showed that IGLad contains the terminal glycanic structure Galbeta 1-4GlcNAc. Removal of terminal beta -linked galactose residues from IGLad decreased the recognition of IGLad by the K88ad adhesin, indicating that terminal beta -linked galactose is an essential component of the K88ad adhesin recognition site on IGLad. Studies with purified glycosphingolipid standards demonstrated that K88ad adhesin binds to neolactotetraosylceramide (nLc4Cer) (Galbeta 1-4GlcNAcbeta 1-3Galbeta 1-4Glcbeta 1-1Cer), lactotriosylceramide (GlcNAcbeta 1-3Galbeta 1-4Glcbeta 1-1Cer) and lactotetraosylceramide (Galbeta 1-3GlcNAcbeta 1-3Galbeta 1-4Glcbeta 1-1Cer). Based on these studies, IGLad appears to be nLc4Cer.

* Corresponding author. Mailing address: Department of Veterinary Science, P.O. Box 2175, South Dakota State University, Brookings, SD 57007-1396. Phone: (605) 688-5171. Fax: (605) 688-6003. E-mail: ericksoa{at}mg.sdstate.edu.

dagger South Dakota Agricultural Experiment Station paper no. 3083.

Infection and Immunity, January 1999, p. 165-172, Vol. 67, No. 1
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Coddens, A., Diswall, M., Angstrom, J., Breimer, M. E., Goddeeris, B., Cox, E., Teneberg, S. (2009). Recognition of Blood Group ABH Type 1 Determinants by the FedF Adhesin of F18-fimbriated Escherichia coli. J. Biol. Chem. 284: 9713-9726 [Abstract] [Full Text]  
  • Zhang, W., Fang, Y., Francis, D. H. (2009). Characterization of the Binding Specificity of K88ac and K88ad Fimbriae of Enterotoxigenic Escherichia coli by Constructing K88ac/K88ad Chimeric FaeG Major Subunits. Infect. Immun. 77: 699-706 [Abstract] [Full Text]  
  • Yan, X. M., Ren, J., Huang, X., Zhang, Z. Y., Ouyang, J., Zeng, W. H., Zou, Z. Z., Yang, S. J., Yang, B., Huang, L.-S. (2009). Comparison of production traits between pigs with and without the Escherichia coli F4 receptors in a White Duroc x Erhualian intercross F2 population. J ANIM SCI 87: 334-339 [Abstract] [Full Text]  
  • George, S., Oh, Y., Lindblom, S., Vilain, S., Rosa, A. J. M., Francis, D. H., Brozel, V. S., Kaushik, R. S. (2007). Lectin binding profile of the small intestine of five-week-old pigs in response to the use of chlortetracycline as a growth promotant and under gnotobiotic conditions. J ANIM SCI 85: 1640-1650 [Abstract] [Full Text]  
  • Grange, P. A., Mouricout, M. A., Levery, S. B., Francis, D. H., Erickson, A. K. (2002). Evaluation of Receptor Binding Specificity of Escherichia coli K88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors. Infect. Immun. 70: 2336-2343 [Abstract] [Full Text]  
  • Sun, R., Anderson, T. J., Erickson, A. K., Nelson, E. A., Francis, D. H. (2000). Inhibition of Adhesion of Escherichia coli K88ac Fimbria to Its Receptor, Intestinal Mucin-Type Glycoproteins, by a Monoclonal Antibody Directed against a Variable Domain of the Fimbria. Infect. Immun. 68: 3509-3515 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»