1. Abstract
Streptococcus pneumoniae (Pnc) is one of the leading pathogens in the world. Attachment to respiratory mucosal and lung surfaces is presumed to be involved in carriage, in disease and in the interaction with macrophages initiating innate immune responses. We hypothesized that bacterial adhesins mediate Pnc adhesion and host cell invasiveness. Initial studies have focused on the purification of cell wall and membrane proteins using fetuin affinity chromatography, SDS PAGE and western blot analysis probed with pooled healthy human sera. Using a Pnc clinical isolate, and a gpt mutant we have detected I0-lectin proteins isolated from the cell wall and adherent to the affinity column and 15 lectins isolated from membrane extracts. The fetuin-captured lectins agglutinated rabbit erythrocytes. 15 proteins in the cell wall and 18 proteins in the membrane that failed to bind to the fetuin column did not agglutinate rabbit erythrocytes. Further purification of the cell wall and membrane fetuin-separated fractions was achieved via anion exchange FPLC, was verified by SDS PAGE. These proteins maintained their agglutinating activity, and were subsequently tested for their ability to interfere with Pnc adhesion and invasion of epithelial cells in culture. Additional biochemical, immunological and molecular techniques are being used in attempt to identify relevant proteins.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Alonso De Velasco E. A., Verheul F.M., Verhoef J., Scippe H. 1995. Streptococcus pneumoniae: virulence factors, pathogenesis, and vaccine. Microbiol. Rev. 59:591–603.
Austerian R and Gold J. 1964. Pneumococcal bacteremia with special reference to bacteremic pneumococcal pneumonia. Ann. Intern. Med. 60:759–776.
Austrian R. 1986 Some aspects of the pneumococcal carrier state. J. Antimicrob. Chemother. 18(suppl A):35–45.
Avery O.T., Goebel W.F. 1929. Chemo-immunologic studies on conjugate carbohydrate-proteins. II Immunological specificity synthetic sugar-protein antigens. J. Exp. Med. 50:533–550.
Center for disease control and prevention. 1995 Pneumonia and Influenza death rate-United States 1979–1994. Morbid. Mortal. Weekly Rep. 44:535–537.
Cowan M.J., Ammann A.J., Wara D.W, Howie V.M., Schultz L., Diyle N., Kaplan M. 1978. Pneumococcal polysaccharide immunization in infants and children. Pediatrics. 62:721–727.
Cundel D; Gerard N; Gerard C; Idapaan-Hiekkila I; Tuomanen E. Streptococcus pneumoniae anchors to activated eukaryotic cells by the receptor to platelets activating factor. Nature. 377:435–438.
Cundel D; Tuomanen E.I. 1994. Receptor specificity of adherence of Strptococcus pneunzoniae to human type II pneumocytes and vascular endothelial cells in vitro. Microbiol. Pathog. 17:361–374.
Kaythy H., Eskola J. 1996. New vaccines for the prevention of pneumococcal infections. Emerg. Infect, Dis. 2:289–298.
McDaniels LL.S; Sheffield J.S; Siatlo E; Yother J; Crain M.J; Brils D.E. 1992. Molecular localization of variable and conserve regions of PspA and identification of additional PspA homologous sequences in Streptococcus pneumoniae. Microb. Pathog. 13:261–269.
Robins J. B., Austrian R, Lee C.J., Rastogi S.C., Schiffman G., Henrichsen J., Makela P.H., Broome C.V., Facklam R.R., Tiesjema R.H., Parke, Jr. J.C. 1983. Considerations for formulating the second generation of pneumococal capsular polysaccharide vaccine with emphasis on the cross-reactive type within the groups. J. Infect. Dis. 148:1136–1159.
Ronda C; Garcia J; Garcia E; Sanchez-Puelles J; Lopez R. 1987. Biological role of the pneumococcal amidase: cloning of the LytA gene. Eur. J. Biochem. 164:621–624.
Rosenow C; Ryan P; Weiser J; Johnson S Fountan P; Ortqvist A; Masure H. 1997. Contribution of a novel choline binding protein to adherence, colonization and immunogenicity. Infect. Immun. 25:819–829
Sampson J; O’Connor R; Stinson A, Tharpe J, Russel H. 1994. Cloning and nucleotide sequence analysis of PsaA, the Sreptococcus pneumoniae gene encoding a 37-kilodalton protein homologous to previously reported Streptococcus sp.adhesins. Infect. Immun. 62:319–324.
Shapiro E.S., Berg A.T., Austrian R., Scroeder D., Parcells V., Margolis A., Adair R.K., Clemmens J.D. 1991. Protective efficacy of polyvalent pneumococcal polysaccharide vaccine. N. Engl. J. Med. 325:1453–1460.
Thuomanen E.I., Austrian R., Masure H.R. 1995. Pathogenenesis of pneumococcal infection. N. Engl. J. Med. 332:1280–1284.
Thuomanen E. I. 1997. The biology of pneumococcal infection. Ped. Res. 42:253–258.
Weiser J; Austrian R; Streenivasan P; Masure H. 1994. Phase variation in pneumococcal opacity: relationship between colonial morphology and the nasopharyngeal colonization. Infec. Immun. 62:2582–2486.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2002 Kluwer Academic Publishers
About this chapter
Cite this chapter
Shani-Sekler, M. et al. (2002). Initial Steps in Streptococcus pneumoniae Interaction with and Pathogenicity to the Host. In: Keisari, Y., Ofek, I. (eds) The Biology and Pathology of Innate Immunity Mechanisms. Advances in Experimental Medicine and Biology, vol 479. Springer, Boston, MA. https://doi.org/10.1007/0-306-46831-X_6
Download citation
DOI: https://doi.org/10.1007/0-306-46831-X_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-0-306-46409-6
Online ISBN: 978-0-306-46831-5
eBook Packages: Springer Book Archive