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 Fumagalli, O. Articles by Oelschlaeger, T. A. Search for Related Content PubMed PubMed Citation Articles by Fumagalli, O. Articles by Oelschlaeger, T. A.

 Previous Article  |  Next Article 

Infect. Immun., Nov 1997, 4445-4451, Vol 65, No. 11
Copyright © 1997, American Society for Microbiology

N-glycosylated proteins are involved in efficient internalization of Klebsiella pneumoniae by cultured human epithelial cells

O Fumagalli, BD Tall, C Schipper and TA Oelschlaeger
Institut fur Molekulare Infektionsbiologie, Wurzburg, Germany.

Klebsiella pneumoniae obtained from patients with urinary tract infections is able to invade cultured human epithelial cells. The internalization process is dependent upon both microfilaments and microtubules. To better understand the interaction of these invasive bacteria with the host cell receptor(s), bladder, lung, and ileocecal epithelial cells were infected with K. pneumoniae in the presence of various lectins possessing multiple glycan specificities. It was found that the N-acetylglucosamine (GlcNAc)-specific lectins concanavalin A, Datura stramonium agglutinin, and wheat germ agglutinin significantly inhibited the invasion of K. pneumoniae into these cells but did not interfere with the internalization of an invasive strain of Salmonella typhimurium. Conversely, internalization of K. pneumoniae but not S. typhimurium was also significantly inhibited when the bacteria were pretreated with GlcNAc or chitin hydrolysate, a GlcNAc polymer, prior to the gentamicin invasion assay. Other carbohydrates such as glucose, galactose, mannose, fucose, and N-acetylneuraminic acid had no inhibitory effects on K. pneumoniae uptake. Furthermore, internalization of K. pneumoniae but not S. typhimurium by HCT8 cells was also significantly inhibited when eukaryotic protein glycosylation was interrupted by tunicamycin or when host N-linked surface glycans were removed by pretreatment with N-glycosidase F. These studies suggest that a N-glycosylated protein receptor is involved in the internalization of K. pneumoniae by human epithelial cells in vitro. The results also indicate that internal GlcNAc residues might be a carbohydrate component of the receptor.

This article has been cited by other articles:

• Sahly, H., Navon-Venezia, S., Roesler, L., Hay, A., Carmeli, Y., Podschun, R., Hennequin, C., Forestier, C., Ofek, I. (2008). Extended-Spectrum {beta}-Lactamase Production Is Associated with an Increase in Cell Invasion and Expression of Fimbrial Adhesins in Klebsiella pneumoniae. Antimicrob. Agents Chemother. 52: 3029-3034 [Abstract] [Full Text]  
• Hess, P., Altenhofer, A., Khan, A. S., Daryab, N., Kim, K. S., Hacker, J., Oelschlaeger, T. A. (2004). A Salmonella fim Homologue in Citrobacter freundii Mediates Invasion In Vitro and Crossing of the Blood-Brain Barrier in the Rat Pup Model. Infect. Immun. 72: 5298-5307 [Abstract] [Full Text]  
• Sahly, H., Podschun, R., Oelschlaeger, T. A., Greiwe, M., Parolis, H., Hasty, D., Kekow, J., Ullmann, U., Ofek, I., Sela, S. (2000). Capsule Impedes Adhesion to and Invasion of Epithelial Cells by Klebsiella pneumoniae. Infect. Immun. 68: 6744-6749 [Abstract] [Full Text]  
• Folders, J., Tommassen, J., van Loon, L. C., Bitter, W. (2000). Identification of a Chitin-Binding Protein Secreted by Pseudomonas aeruginosa. J. Bacteriol. 182: 1257-1263 [Abstract] [Full Text]  
• Krimmer, V., Merkert, H., von Eiff, C., Frosch, M., Eulert, J., Löhr, J. F., Hacker, J., Ziebuhr, W. (1999). Detection of Staphylococcus aureus and Staphylococcus epidermidis in Clinical Samples by 16S rRNA-Directed In Situ Hybridization. J. Clin. Microbiol. 37: 2667-2673 [Abstract] [Full Text]