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

 Previous Article  |  Next Article 

Infect. Immun., 11 1997, 4572-4579, Vol 65, No. 11
Copyright © 1997, American Society for Microbiology

Escherichia coli strains with nonimmune immunoglobulin-binding activity

CH Sandt, YD Wang, RA Wilson and CW Hill
Department of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey 17033, USA. csandt@bcmic.hmc.psu.edu

We have identified several strains of Escherichia coli which contain immunoglobulin-binding activity on the cell surface. Affinity-purified antibodies ordinarily used as secondary antibodies in immunodetection protocols were bound by 6 of 72 strains of the ECOR reference collection of E. coli. The Fc fragments of both human and sheep immunoglobulin G (IgG) were also bound, demonstrating the nonimmune nature of the phenomenon. Binding of conjugated IgG Fc directly to unfixed cells was observed by fluorescence microscopy. Western blots showed that the immunoglobulin-binding material occurs in the form of multiple bands, with the apparent molecular masses of the most prominent bands exceeding 100 kDa. No two of the strains have the same pattern of bands. The binding activity in extracts was sensitive to proteinase K. The binding activity of intact cells was reduced preferentially by trypsin digestion, demonstrating exposure at the cell surface. Expression of binding activity in Luria-Bertani broth cultures was favored by a temperature of 37 degrees C and entry into stationary phase of growth.

This article has been cited by other articles:

• Lu, Y., Iyoda, S., Satou, H., Satou, H., Itoh, K., Saitoh, T., Watanabe, H. (2006). A New Immunoglobulin-Binding Protein, EibG, Is Responsible for the Chain-Like Adhesion Phenotype of Locus of Enterocyte Effacement-Negative, Shiga Toxin-Producing Escherichia coli.. Infect. Immun. 74: 5747-5755 [Abstract] [Full Text]  
• Nordstrom, T., Forsgren, A., Riesbeck, K. (2002). The Immunoglobulin D-binding Part of the Outer Membrane Protein MID from Moraxella catarrhalis Comprises 238 Amino Acids and a Tetrameric Structure. J. Biol. Chem. 277: 34692-34699 [Abstract] [Full Text]  
• Sandt, C. H., Hopper, J. E., Hill, C. W. (2002). Activation of Prophage eib Genes for Immunoglobulin-Binding Proteins by Genes from the IbrAB Genetic Island of Escherichia coli ECOR-9. J. Bacteriol. 184: 3640-3648 [Abstract] [Full Text]  
• Sandt, C. H., Hill, C. W. (2001). Nonimmune Binding of Human Immunoglobulin A (IgA) and IgG Fc by Distinct Sequence Segments of the EibF Cell Surface Protein of Escherichia coli. Infect. Immun. 69: 7293-7303 [Abstract] [Full Text]  
• Bong, C. T. H., Throm, R. E., Fortney, K. R., Katz, B. P., Hood, A. F., Elkins, C., Spinola, S. M. (2001). DsrA-Deficient Mutant of Haemophilus ducreyi Is Impaired in Its Ability To Infect Human Volunteers. Infect. Immun. 69: 1488-1491 [Abstract] [Full Text]  
• Wada, A., Mikkola, R., Kurland, C. G., Ishihama, A. (2000). Growth Phase-Coupled Changes of the Ribosome Profile in Natural Isolates and Laboratory Strains of Escherichia coli. J. Bacteriol. 182: 2893-2899 [Abstract] [Full Text]  
• Sandt, C. H., Hill, C. W. (2000). Four Different Genes Responsible for Nonimmune Immunoglobulin-Binding Activities within a Single Strain of Escherichia coli. Infect. Immun. 68: 2205-2214 [Abstract] [Full Text]