Abstract
The adherence of Pseudomonas aeruginosa PAO1 to primary cultures of cystic fibrosis nasal polyp (CFNP), normal human nasal polyp (NHNP), and immortalized CF and normal cell lines was studied. PAO1 bound significantly more to primary CFNP cells than to NHNP cells as the mean adherence +/- standard deviation of 5 x 10(7) CFU of 35S-labeled bacteria per ml per well was 15.09 x 10(6) +/- 4.25 x 10(6) CFU/ml per well and 7.62 x 10(6) +/- 2.11 x 10(6) CFU/ml per well, respectively (Mann-Whitney U test, P less than 0.0001). There was no significant difference in PAO1 adherence to the immortalized CF and normal cell lines. The primary CFNP cells had more receptors (115 per cell) than did NHNP cells (34 per cell). P. aeruginosa binding to CFNP was blocked by GlcNAc, NeuAc, L-Fuc, and D-Gal, while binding to NHNP was blocked only by GlcNAc, suggesting that receptors on the two cell types were qualitatively different. Pseudomonas supernatants containing protease, phospholipase C, and neuraminidase activity increased adherence to CFNP and NHNP cells. The Pseudomonas exoproducts modified epithelial cell glycoconjugates, as characterized by binding of fluorescein isothiocyanate-labeled lectins and the release of sialic acid. There was minimal release of fibronectin by the bacterial supernatants. The affinity of P. aeruginosa for CF epithelial cells appeared to be due to an increased number of receptors and modification of the epithelial cell surface by P. aeruginosa exoproducts that exposed asialoganglioside binding sites.
Full text
PDF






Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Anderson M. P., Rich D. P., Gregory R. J., Smith A. E., Welsh M. J. Generation of cAMP-activated chloride currents by expression of CFTR. Science. 1991 Feb 8;251(4994):679–682. doi: 10.1126/science.1704151. [DOI] [PubMed] [Google Scholar]
- Baker N. R., Minor V., Deal C., Shahrabadi M. S., Simpson D. A., Woods D. E. Pseudomonas aeruginosa exoenzyme S is an adhesion. Infect Immun. 1991 Sep;59(9):2859–2863. doi: 10.1128/iai.59.9.2859-2863.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Baker N., Hansson G. C., Leffler H., Riise G., Svanborg-Edén C. Glycosphingolipid receptors for Pseudomonas aeruginosa. Infect Immun. 1990 Jul;58(7):2361–2366. doi: 10.1128/iai.58.7.2361-2366.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Barasch J., Kiss B., Prince A., Saiman L., Gruenert D., al-Awqati Q. Defective acidification of intracellular organelles in cystic fibrosis. Nature. 1991 Jul 4;352(6330):70–73. doi: 10.1038/352070a0. [DOI] [PubMed] [Google Scholar]
- Boucher R. C., Cheng E. H., Paradiso A. M., Stutts M. J., Knowles M. R., Earp H. S. Chloride secretory response of cystic fibrosis human airway epithelia. Preservation of calcium but not protein kinase C- and A-dependent mechanisms. J Clin Invest. 1989 Nov;84(5):1424–1431. doi: 10.1172/JCI114316. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Chi E., Mehl T., Nunn D., Lory S. Interaction of Pseudomonas aeruginosa with A549 pneumocyte cells. Infect Immun. 1991 Mar;59(3):822–828. doi: 10.1128/iai.59.3.822-828.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cozens A. L., Yezzi M. J., Chin L., Simon E. M., Friend D. S., Gruenert D. C. Chloride ion transport in transformed normal and cystic fibrosis epithelial cells. Adv Exp Med Biol. 1991;290:187–196. doi: 10.1007/978-1-4684-5934-0_19. [DOI] [PubMed] [Google Scholar]
- Fishman P. H., Brady R. O. Biosynthesis and function of gangliosides. Science. 1976 Nov 26;194(4268):906–915. doi: 10.1126/science.185697. [DOI] [PubMed] [Google Scholar]
- Frizzell R. A., Rechkemmer G., Shoemaker R. L. Altered regulation of airway epithelial cell chloride channels in cystic fibrosis. Science. 1986 Aug 1;233(4763):558–560. doi: 10.1126/science.2425436. [DOI] [PubMed] [Google Scholar]
- Govan J. R., Harris G. S. Pseudomonas aeruginosa and cystic fibrosis: unusual bacterial adaptation and pathogenesis. Microbiol Sci. 1986 Oct;3(10):302–308. [PubMed] [Google Scholar]
- Gruenert D. C., Basbaum C. B., Welsh M. J., Li M., Finkbeiner W. E., Nadel J. A. Characterization of human tracheal epithelial cells transformed by an origin-defective simian virus 40. Proc Natl Acad Sci U S A. 1988 Aug;85(16):5951–5955. doi: 10.1073/pnas.85.16.5951. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hakomori S. Aberrant glycosylation in cancer cell membranes as focused on glycolipids: overview and perspectives. Cancer Res. 1985 Jun;45(6):2405–2414. [PubMed] [Google Scholar]
- Holloway B. W., Krishnapillai V., Morgan A. F. Chromosomal genetics of Pseudomonas. Microbiol Rev. 1979 Mar;43(1):73–102. doi: 10.1128/mr.43.1.73-102.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Johnson G. D., Nogueira Araujo G. M. A simple method of reducing the fading of immunofluorescence during microscopy. J Immunol Methods. 1981;43(3):349–350. doi: 10.1016/0022-1759(81)90183-6. [DOI] [PubMed] [Google Scholar]
- Kartner N., Hanrahan J. W., Jensen T. J., Naismith A. L., Sun S. Z., Ackerley C. A., Reyes E. F., Tsui L. C., Rommens J. M., Bear C. E. Expression of the cystic fibrosis gene in non-epithelial invertebrate cells produces a regulated anion conductance. Cell. 1991 Feb 22;64(4):681–691. doi: 10.1016/0092-8674(91)90498-n. [DOI] [PubMed] [Google Scholar]
- Kawaguchi T., Matsumoto I., Osawa T. Studies on hemagglutinins from Maackia amurensis seeds. J Biol Chem. 1974 May 10;249(9):2786–2792. [PubMed] [Google Scholar]
- Kerem E., Corey M., Kerem B. S., Rommens J., Markiewicz D., Levison H., Tsui L. C., Durie P. The relation between genotype and phenotype in cystic fibrosis--analysis of the most common mutation (delta F508). N Engl J Med. 1990 Nov 29;323(22):1517–1522. doi: 10.1056/NEJM199011293232203. [DOI] [PubMed] [Google Scholar]
- Krivan H. C., Roberts D. D., Ginsburg V. Many pulmonary pathogenic bacteria bind specifically to the carbohydrate sequence GalNAc beta 1-4Gal found in some glycolipids. Proc Natl Acad Sci U S A. 1988 Aug;85(16):6157–6161. doi: 10.1073/pnas.85.16.6157. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Li M., McCann J. D., Liedtke C. M., Nairn A. C., Greengard P., Welsh M. J. Cyclic AMP-dependent protein kinase opens chloride channels in normal but not cystic fibrosis airway epithelium. Nature. 1988 Jan 28;331(6154):358–360. doi: 10.1038/331358a0. [DOI] [PubMed] [Google Scholar]
- Mason C. M., Bawdon R. E., Pierce A. K., Dal Nogare A. R. Fibronectin is not detectable on the intact buccal epithelial surface of normal rats or humans. Am J Respir Cell Mol Biol. 1990 Dec;3(6):563–570. doi: 10.1165/ajrcmb/3.6.563. [DOI] [PubMed] [Google Scholar]
- Pier G. B. Pulmonary disease associated with Pseudomonas aeruginosa in cystic fibrosis: current status of the host-bacterium interaction. J Infect Dis. 1985 Apr;151(4):575–580. doi: 10.1093/infdis/151.4.575. [DOI] [PubMed] [Google Scholar]
- Ramphal R., Carnoy C., Fievre S., Michalski J. C., Houdret N., Lamblin G., Strecker G., Roussel P. Pseudomonas aeruginosa recognizes carbohydrate chains containing type 1 (Gal beta 1-3GlcNAc) or type 2 (Gal beta 1-4GlcNAc) disaccharide units. Infect Immun. 1991 Feb;59(2):700–704. doi: 10.1128/iai.59.2.700-704.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ramphal R., Houdret N., Koo L., Lamblin G., Roussel P. Differences in adhesion of Pseudomonas aeruginosa to mucin glycopeptides from sputa of patients with cystic fibrosis and chronic bronchitis. Infect Immun. 1989 Oct;57(10):3066–3071. doi: 10.1128/iai.57.10.3066-3071.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ramphal R., Koo L., Ishimoto K. S., Totten P. A., Lara J. C., Lory S. Adhesion of Pseudomonas aeruginosa pilin-deficient mutants to mucin. Infect Immun. 1991 Apr;59(4):1307–1311. doi: 10.1128/iai.59.4.1307-1311.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rommens J. M., Iannuzzi M. C., Kerem B., Drumm M. L., Melmer G., Dean M., Rozmahel R., Cole J. L., Kennedy D., Hidaka N. Identification of the cystic fibrosis gene: chromosome walking and jumping. Science. 1989 Sep 8;245(4922):1059–1065. doi: 10.1126/science.2772657. [DOI] [PubMed] [Google Scholar]
- Saiman L., Cacalano G., Prince A. Pseudomonas cepacia adherence to respiratory epithelial cells is enhanced by Pseudomonas aeruginosa. Infect Immun. 1990 Aug;58(8):2578–2584. doi: 10.1128/iai.58.8.2578-2584.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Saiman L., Ishimoto K., Lory S., Prince A. The effect of piliation and exoproduct expression on the adherence of Pseudomonas aeruginosa to respiratory epithelial monolayers. J Infect Dis. 1990 Mar;161(3):541–548. doi: 10.1093/infdis/161.3.541. [DOI] [PubMed] [Google Scholar]
- Saiman L., Sadoff J., Prince A. Cross-reactivity of Pseudomonas aeruginosa antipilin monoclonal antibodies with heterogeneous strains of P. aeruginosa and Pseudomonas cepacia. Infect Immun. 1989 Sep;57(9):2764–2770. doi: 10.1128/iai.57.9.2764-2770.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shibuya N., Goldstein I. J., Broekaert W. F., Nsimba-Lubaki M., Peeters B., Peumans W. J. The elderberry (Sambucus nigra L.) bark lectin recognizes the Neu5Ac(alpha 2-6)Gal/GalNAc sequence. J Biol Chem. 1987 Feb 5;262(4):1596–1601. [PubMed] [Google Scholar]
- Taatjes D. J., Roth J., Peumans W., Goldstein I. J. Elderberry bark lectin--gold techniques for the detection of Neu5Ac (alpha 2,6) Gal/GalNAc sequences: applications and limitations. Histochem J. 1988 Sep;20(9):478–490. doi: 10.1007/BF01002646. [DOI] [PubMed] [Google Scholar]
- WARREN L. The thiobarbituric acid assay of sialic acids. J Biol Chem. 1959 Aug;234(8):1971–1975. [PubMed] [Google Scholar]
- Woods D. E., Bass J. A., Johanson W. G., Jr, Straus D. C. Role of adherence in the pathogenesis of Pseudomonas aeruginosa lung infection in cystic fibrosis patients. Infect Immun. 1980 Dec;30(3):694–699. doi: 10.1128/iai.30.3.694-699.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Woods D. E., Straus D. C., Johanson W. G., Jr, Bass J. A. Role of fibronectin in the prevention of adherence of Pseudomonas aeruginosa to buccal cells. J Infect Dis. 1981 Jun;143(6):784–790. doi: 10.1093/infdis/143.6.784. [DOI] [PubMed] [Google Scholar]


