Skip to main content
Infection and Immunity logoLink to Infection and Immunity
. 1995 Mar;63(3):757–761. doi: 10.1128/iai.63.3.757-761.1995

Relationship between colonial morphology and adherence of Streptococcus pneumoniae.

D R Cundell 1, J N Weiser 1, J Shen 1, A Young 1, E I Tuomanen 1
PMCID: PMC173067  PMID: 7868244

Abstract

Phase variants in colonial opacity of pneumococci differ in the ability to colonize the nasopharynx of infant rats. To explain this observation at a cellular level, we compared the ability of opacity variants to adhere to buccal epithelial cells, type II pneumocytes, or vascular endothelial cells and to the glycoconjugates that represent the cognate receptors at each of these sites. The transparent phenotype was associated with enhanced adherence to buccal cells (approximately 100%) and their receptor relative to that of the opaque variants. Only modest differences in adherence (< 45%) were demonstrated to resting lung and vascular cells. In contrast, adherence of transparent variants increased by 90% to lung cells stimulated with interleukin-1 and by 130% to endothelial cells stimulated with tumor necrosis factor. In contrast, cytokine stimulation did not influence the adherence of opaque pneumococci. This difference correlated with the unique ability of transparent variants to adhere to immobilized GlcNAc and to cells bearing transfected platelet-activating factor receptors. These results suggest that the mechanism of enhanced colonization of the nasopharynx in vivo by transparent as compared with opaque phase variants involves a greater ability to adhere to both GlcNAc beta 1-3Gal on buccal epithelial cells and GlcNAc and PAF receptors on cytokine-activated, as opposed to resting, lung and endovascular cells.

Full Text

The Full Text of this article is available as a PDF (204.0 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andersson B., Dahmén J., Frejd T., Leffler H., Magnusson G., Noori G., Edén C. S. Identification of an active disaccharide unit of a glycoconjugate receptor for pneumococci attaching to human pharyngeal epithelial cells. J Exp Med. 1983 Aug 1;158(2):559–570. doi: 10.1084/jem.158.2.559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Andersson B., Eriksson B., Falsen E., Fogh A., Hanson L. A., Nylén O., Peterson H., Svanborg Edén C. Adhesion of Streptococcus pneumoniae to human pharyngeal epithelial cells in vitro: differences in adhesive capacity among strains isolated from subjects with otitis media, septicemia, or meningitis or from healthy carriers. Infect Immun. 1981 Apr;32(1):311–317. doi: 10.1128/iai.32.1.311-317.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cabellos C., MacIntyre D. E., Forrest M., Burroughs M., Prasad S., Tuomanen E. Differing roles for platelet-activating factor during inflammation of the lung and subarachnoid space. The special case of Streptococcus pneumoniae. J Clin Invest. 1992 Aug;90(2):612–618. doi: 10.1172/JCI115900. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chao W., Olson M. S. Platelet-activating factor: receptors and signal transduction. Biochem J. 1993 Jun 15;292(Pt 3):617–629. doi: 10.1042/bj2920617. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Geelen S., Bhattacharyya C., Tuomanen E. The cell wall mediates pneumococcal attachment to and cytopathology in human endothelial cells. Infect Immun. 1993 Apr;61(4):1538–1543. doi: 10.1128/iai.61.4.1538-1543.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. 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]
  7. Kunz D., Gerard N. P., Gerard C. The human leukocyte platelet-activating factor receptor. cDNA cloning, cell surface expression, and construction of a novel epitope-bearing analog. J Biol Chem. 1992 May 5;267(13):9101–9106. [PubMed] [Google Scholar]
  8. Lee K. K., Sheth H. B., Wong W. Y., Sherburne R., Paranchych W., Hodges R. S., Lingwood C. A., Krivan H., Irvin R. T. The binding of Pseudomonas aeruginosa pili to glycosphingolipids is a tip-associated event involving the C-terminal region of the structural pilin subunit. Mol Microbiol. 1994 Feb;11(4):705–713. doi: 10.1111/j.1365-2958.1994.tb00348.x. [DOI] [PubMed] [Google Scholar]
  9. Pennington J. E. Treating respiratory infections in the era of cost control. Am Fam Physician. 1986 Feb;33(2):153–160. [PubMed] [Google Scholar]
  10. Swanson J. Colony opacity and protein II compositions of gonococci. Infect Immun. 1982 Jul;37(1):359–368. doi: 10.1128/iai.37.1.359-368.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Swanson J. Studies on gonococcus infection. XII. Colony color and opacity varienats of gonococci. Infect Immun. 1978 Jan;19(1):320–331. doi: 10.1128/iai.19.1.320-331.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Weiser J. N., Austrian R., Sreenivasan P. K., Masure H. R. Phase variation in pneumococcal opacity: relationship between colonial morphology and nasopharyngeal colonization. Infect Immun. 1994 Jun;62(6):2582–2589. doi: 10.1128/iai.62.6.2582-2589.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Weiser J. N. Relationship between colony morphology and the life cycle of Haemophilus influenzae: the contribution of lipopolysaccharide phase variation to pathogenesis. J Infect Dis. 1993 Sep;168(3):672–680. doi: 10.1093/infdis/168.3.672. [DOI] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES