Differential protein expression in phenotypic variants of Streptococcus pneumoniae

Infection and Immunity

Volumn 68, Issue 8, 2000, Pages 4604-4610

  Overweg, Karin ^a   Pericone, Chris D ^b   Verhoef, Gerridina G C ^a   Weiser, Jeffrey N ^b   Meiring, Hugo D ^c   De Jong, Ad P J M ^c   De Groot, Ronald ^a   Hermans, Peter W M ^a,d  

^a SOPHIA CHILDREN S HOSPITAL   (Netherlands)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c NATIONAL INSTITUTE FOR PUBLIC HEALTH AND THE ENVIRONMENT   (Netherlands)

^d ERASMUS UNIVERSITY ROTTERDAM   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; HYDROGEN PEROXIDE; ISOMERASE; PROTEIN; PROTEINASE;

ARTICLE; BACTERIAL COLONIZATION; BACTERIAL VIRULENCE; ENZYME ACTIVITY; LACTOBACILLUS CASEI; MASS SPECTROMETRY; NASOPHARYNX; PATHOGENESIS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN ELECTROPHORESIS; PROTEIN EXPRESSION; SEQUENCE HOMOLOGY; STREPTOCOCCUS PNEUMONIAE; WESTERN BLOTTING;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; ENDOPEPTIDASES; GENE EXPRESSION PROFILING; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDE ELONGATION FACTORS; PHENOTYPE; PROTEIN PROCESSING, POST-TRANSLATIONAL; PYRUVATE OXIDASE; SEQUENCE ANALYSIS, PROTEIN; STREPTOCOCCUS PNEUMONIAE; VARIATION (GENETICS);

EID: 0033929389     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.8.4604-4610.2000     Document Type: Article

References (34)

1. Altschul, S. F., G. W. Miller, E. W. Myers, and D. J. Lipman. 1990. Basic local alignment search tool. J. Mol. Biol. 251:403-410.
2. Avery, O. T., C. M. MacLeod, and M. McCarty. 1944. Studies on the chemical nature of the substance inducing transformation of pneumococcal types. Induction of transformation by a desoxyribonucleic acid fraction isolated from pneumococcus type III. J. Exp. Med. 79:137-158.
3. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
4. Condon, S. 1987. Responses of lactic acid bacteria to oxygen. FEMS Microbiol. Rev. 46:269-280.
5. Cundell, D. R., N. P. Gerard, C. Gerard, I. Idanpaan-Heikkila, and E. I. Tuomanen. 1995. Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor. Nature 377:435-438.
6. Duane, P. G., J. B. Rubins, H. R. Weissel, and E. N. Janoff. 1993. Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells. Infect. Immun. 61:4392-4397.
7. Gevaert, K., J. Verschelde, M. Puype, J. van Damme, M. Goethals, S. de Boeck, and J. Vanderkerckhove. 1996. Structural analysis and identification of gel-purified proteins in the femtomole range, using a novel computer program for peptide sequence assignment, by matrix-assisted laser desorption ionization-reflection time-of-flight-mass spectrometry. Electrophoresis 17:918-924.
8. Haandrikman, A. J., J. Kok, and G. Venema. 1991. Lactococcal proteinase maturation protein PrtM is a lipoprotein. J. Bacteriol. 173:4517-4525.
9. Hammerschmidt, S., G. Bethe, P. H. Remane, and G. S. Chhatwal. 1999. Identification of pneumococcal surface protein A as a lactoferrin-binding protein of Streptococcus pneumoniae. Infect. Immun. 67:1683-1687.
10. Hammerschmidt, S., A. Muller, H. Sillman, M. Muhlenhoff, R. Borrow, et al. 1996. Capsule phase variation in Neisseria meningitidis serogroup B by slipped-strand mispairing in the polysialyltransferase gene (siaD): correlation with bacterial invasion and the outbreak of meningococcal disease. Mol. Microbiol. 20:1211-1220.
11. Holck, A., and H. Naes. 1992. Cloning, sequencing and expression of the gene encoding the cell-envelope-associated proteinase from Lactobacillus paracasei subsp. paracasei NCDO 151. J. Gen. Microbiol. 138:1353-1364.
12. Kim, J. O., S. Romero-Steiner, U. B. S. Sorensen, J. Blom, M. Carvalho, S. Barnard, G. Carlone, and J. N. Weiser. 1999. Relationship between cell surface carbohydrates and intrastrain variation on opsonophagocytosis of Streptococcus pneumoniae. Infect. Immun. 67:2327-2333.
13. Kim, J. O., and J. N. Weiser. 1998. Association of intrastrain phase variation in quantity of capsular polysaccharide and teichoic acid with the virulence of Streptococcus pneumoniae. J. Infect. Dis. 177:368-377.
14. Mann, M., and M. Wilm. 1994. Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal. Chem. 66:4390-4399.
15. McCaul, T. F., T. Hackstadt, and J. C. Williams. 1981. Ultrastructural and biological aspects of Coxiella burnetii under physical disruptions., p. 267. In W. Burgdorfer and R. L. Anacker (ed.), Rickettsiae and rickettsial disease. Academic Press, Inc., New York, N.Y.
16. Meiring, H. D., B. M. Barroso, E. van der Heeft, G. J. ten Hove, and A. P. J. M. de Jong. 1999. Sheathless Nanoflow HPLC-ESI/MS(n) in proteome research and MHC bound peptide identification. In Proceedings of the 47th ASMS Conference on Mass Spectrometry and Allied Topics.
17. Overweg, K., A. Kerr, M. Sluijter, M. H. Jackson, T. J. Mitchell, A. P. J. M. de Jong, R. de Groot, and P. W. M. Hermans, 2000. The putative proteinase maturation protein A of Streptococcus pneumoniae is a conserved surface protein with potential to elicit protective immune responses. Infect. Immun. 68:4180-4188.
18. Pick, E., and Y. Keisari. 1980. A simple colorimetric method for the measurement of hydrogen peroxide produced by cells in culture. J. Immunol. Methods 38:161-170.
19. Rabilloud, T., C. Valette, and J. J. Lawrence. 1994. Sample application by in-gel rehydration improves the resolution of two-dimensional electrophoresis with immobilized pH gradients in the first dimension. Electrophoresis 15:1552-1558.
20. Rider, M. H., M. Puype, J. van Damme, K. Gevaert, S. de Boeck, J. D'Alayer, H. H. Rasmussen, J. E. Cells, and J. Vanderkerckhove. 1995. An agarose-based gel-concentration system for microsequence and mass spectrometric characterization of proteins previously purified in polyacrylamide gels starting at low picomole levels. Eur. J. Biochem. 230:258-265.
21. Ring, A., J. N. Weiser, and E. I. Tuomanen. 1998. Pneumococcal trafficking across the blood-brain barrier. Molecular analysis of a novel bidirectional pathway. J. Clin. Investig. 102:347-360.
22. Rosenow, C., P. Ryan, J. N. Weiser, S. Johnson, P. Fontan, A. Ortqvist, and H. R. Masure. 1997. Contribution of novel choline-binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae. Mol. Microbiol. 25:819-829.
23. Rudd, K. E., H. J. Sofia, E. V. Koonin, G. Plunkett II, S. Lazar, and P. E. Rouveire. 1995. A new family of peptidyl-prolyl isomerases. Trends Biochem. Sci. 20:12-14.
24. Saluja, S. K., and J. N. Weiser. 1995. The genetic basis of colony opacity in Streptococcus pneumoniae: evidence for the effect of box elements on the frequency of phenotypic variation. Mol. Microbiol. 16:215-227.
25. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
26. Seshadri, R., L. R. Hendrix, and J. E. Samuel. 1999. Differential expression of translational elements by life cycle variants of Coxiella burnetii. Infect. Immun. 67:6026-6033.
27. Spellerberg, B., D. R. Cundell, J. Sandros, B. J. Pearce, I. Idanpaan-Heikkila, C. Rosenow, and H. R. Masure. 1996. Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae. Mol. Microbiol. 19:803-813.
28. Tu, A. T., R. L. Fulgham, M. A. McCrory, D. E. Briles, and A. J. Szalai. 1999. Pneumococcal surface protein A inhibits complement activation by Streptococcus pneumoniae. Infect. Immun. 67:4720-4724.
29. van der Heeft, E., G. J. ten Hove, C. A. Herberts, H. D. Meiring, C. A. C. M. van Els, and A. P. J. M. de Jong. 1998. A microcapillary column switching system HPLC-electrospray ionization MS system for the direct identification of peptides presented by major histocompatibility complex class I molecules. Anal. Chem. 70:3742-3751.
30. Vos, P., M. van Asseldonk, F. van Jeveren, R. Siezen, G. Simons, and W. M. de Vos. 1989. A maturation protein is essential for production of active forms of Lactococcus lactis SK11 serine protease located in or secreted from the cell envelope. J. Bacteriol. 171:2795-2802.
31. Weiser, J. N. 1998. Phase variation in colony opacity by Streptococcus pneumoniae. Microb. Drug Resist. 4:129-135.
32. Weiser, J. N. 1993. Relationship between colony morphology and the life cycle of Haemophilus influenzae: The contribution of lipopolysaccharide phase variation to pathogenesis. J. Infect. Dis. 168:672-680.
33. Weiser, J. N., R. Austrian, P. K. Sreenivasan, and H. R. Masure. 1994. Phase variation in pneumococcal opacity: relationship between colonial morphology and nasopharyngeal colonization. Infect. Immun. 62:2582-2589.
34. Weiser, J. N., Z. Markievticz, E. I. Tuomanen, and J. H. Wani. 1996. Relationship between phase variation in colony morphology, intrastrain variation in cell wall physiology, and nasopharyngeal colonization by Streptococcus pneumoniae. Infect. Immun. 64:2240-2245.