High-affinity interaction between fibronectin and the group B streptococcal C5a peptidase is unaffected by a naturally occurring four-amino-acid deletion that eliminates peptidase activity

Infection and Immunity

Volumn 74, Issue 10, 2006, Pages 5739-5746

  Tamura, Glen S ^a   Hull, James R ^b   Oberg, Michael D ^a   Castner, David G ^b,c  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

^b University of Washington   (United States)

^c University of Washington   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; AMINO ACID; COMPLEMENT COMPONENT C5A; FIBRONECTIN; PEPTIDASE; RECOMBINANT ENZYME;

ARTICLE; BACTERIAL VIRULENCE; BACTERIUM ADHERENCE; BINDING AFFINITY; DELETION MUTANT; DISSOCIATION CONSTANT; ENZYME ACTIVITY; ENZYME KINETICS; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; STREPTOCOCCUS AGALACTIAE; SURFACE PLASMON RESONANCE;

ADHESINS, BACTERIAL; AMINO ACID SEQUENCE; ENDOPEPTIDASES; FIBRONECTINS; GENETIC COMPLEMENTATION TEST; RECOMBINANT PROTEINS; SEQUENCE DELETION; STREPTOCOCCUS AGALACTIAE; SURFACE PLASMON RESONANCE;

EID: 33749257523     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.00241-06     Document Type: Article

References (35)

1. Anderson, E. T., M. G. Wetherell, L. A. Winter, S. B. Olmsted, P. P. Cleary, and Y. V. Matsuka. 2002. Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes. Eur. J. Biochem. 269:4839-4851.
2. Baker, C. J. 1997. Group B streptococcal infections. Clin. Perinatol. 24:P59-P70.
3. Baugh, L., and V. Vogel. 2004. Structural changes of fibronectin adsorbed to model surfaces probed by fluorescence resonance energy transfer. J. Biomed. Mater. Res. A 69:525-534.
4. Beckmann, C., J. D. Waggoner, T. O. Harris, G. S. Tamura, and C. E. Rubens. 2002. Identification of novel adhesins from group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding. Infect. Immun. 70:2869-2876.
5. Bohnsack, J. F., S. Takahashi, L. Hammitt, D. V. Miller, A. A. Aly, and E. E. Adderson. 2000. Genetic polymorphisms of group B streptococcus scpB alter functional activity of a cell-associated peptidase that inactivates C5a. Infect. Immun. 68:5018-5025.
6. Chaffin, D. O., and C. E. Rubens. 1998. Blue/white screening of recombinant plasmids in gram-positive bacteria by interruption of alkaline phosphatase gene (phoZ) expression. Gene 219:91-99.
7. Cheng, Q., S. Debol, H. Lam, R. Eby, L. Edwards, Y. Matsuka, S. B. Olmsted, and P. P. Cleary. 2002. Immunization with C5a peptidase or peptidase-type III polysaccharide conjugate vaccines enhances clearance of group B streptococci from lungs of infected mice. Infect. Immun. 70:6409-6415.
8. Chmouryguina, I., A. Suvorov, P. Ferrieri, and P. P. Cleary. 1996. Conservation of the C5a peptidase genes in group A and B streptococci. Infect. Immun. 64:2387-2390.
9. Cleary, P. P., J. Handley, A. N. Suvorov, A. Podbielski, and P. Ferrieri. 1992. Similarity between the group B and A streptococcal C5a peptidase genes. Infect. Immun. 60:4239-4244.
10. Courtney, H. S., I. Ofek, W. A. Simpson, D. L. Hasty, and E. H. Beachey. 1986. Binding of Streptococcus pyogenes to soluble and insoluble fibronectin. Infect. Immun. 53:454-459.
11. Ensenberger, M. G., B. R. Tomasini-Johansson, J. Sottile, V. Ozeri, E. Hanski, and D. F. Mosher. 2001. Specific interactions between F1 adhesin of Streptococcus pyogenes and N-terminal modules of fibronectin. J. Biol. Chem. 276:35606-35613.
12. Farley, MF M. 2001. Group B streptococcal disease in nonpregnant adults. Clin. Infect. Dis. 33:556-561.
13. Fink, D. L., B. A. Green, and J. W. St. Geme III. 2002. The Haemophilus influenzae Hap autotransporter binds to fibronectin, laminin, and collagen IV. Infect. Immun. 70:4902-4907.
14. Green, R. J., R. A. Frazier, K. M. Shakesheff, M. C. Davies, C. J. Roberts, and S. J. Tendler. 2000. Surface plasmon resonance analysis of dynamic biological interactions with biomaterials. Biomaterials 21:1823-1835.
15. Kreikemeyer, B., S. Oehmcke, M. Nakata, R. Hoffrogge, and A. Podbielski. 2004. Streptococcus pyogenes fibronectin-binding protein F2: expression profile, binding characteristics, and impact on eukaryotic cell interactions. J. Biol. Chem. 279:15850-15859.
16. Laarmann, S., D. Cutter, T. Juehne, S. J. Barenkamp, and J. W. St. Geme. 2002. The Haemophilus influenzae Hia autotransporter harbours two adhesive pockets that reside in the passenger domain and recognize the same host cell receptor. Mol. Microbiol. 46:731-743.
17. Lowrance, J. H., D. L. Hasty, and W. A. Simpson. 1988. Adherence of Streptococcus sanguis to conformationally specific determinants in fibronectin. Infect. Immun. 56:2279-2285.
18. Massey, R. C., S. R. Dissanayeke, B. Cameron, D. Ferguson, T. J. Foster, and S. J. Peacock. 2002. Functional blocking of Staphylococcus aureus adhesins following growth in ex vivo media. Infect. Immun. 70:5339-5345.
19. McCafferty, M. H., M. Lepow, T. M. Saba, E. Cho, H. Meuwissen, J. White, and S. F. Zuckerbrod. 1983. Normal fibronectin levels as a function of age in the pediatric population. Pediatr. Res. 17:482-485.
20. McElroy, M. C., D. J. Cain, C. Tyrrell, T. J. Foster, and C. Haslett. 2002. Increased virulence of a fibronectin-binding protein mutant of Staphylococcus aureus in a rat model of pneumonia. Infect. Immun. 70:3865-3873.
21. Menendez, R., V. Marco, V. Rubio, and A. Sole. 1995. Quantification of fibronectin in bronchoalveolar lavage fluid and in lung parenchyma: differences between smokers and non-smokers. Respiration 62:312-316.
22. Myszka, D. G., and T. A. Morton. 1998. CLAMP: a biosensor kinetic data analysis program. Trends Biochem. Sci. 23:149-150.
23. Nakamura, T., A. Amano, I. Nakagawa, and S. Hamada. 1999. Specific interactions between Porphyromonas gingivalis fimbriae and human extracellular matrix proteins. FEMS Microbiol. Lett. 175:267-272.
24. Narasimhan, C., and C. S. Lai. 1989. Conformational changes of plasma fibronectin detected upon adsorption to solid substrates: a spin-label study. Biochemistry 28:5041-5046.
25. Schrag, S. J., S. Zywicki, M. M. Farley, A. L. Reingold, L. H. Harrison, L. B. Lefkowitz, J. L. Hadler, R. Danila, P. R. Cieslak, and A. Schuchat. 2000. Group B streptococcal disease in the era of intrapartum antibiotic prophylaxis. N. Engl. J. Med. 342:15-20.
26. Signas, C., G. Raucci, K. Jonsson, P. E. Lindgren, G. M. Anantharamaiah, M. Hook, and M. Lindberg. 1989. Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides. Proc. Natl. Acad. Sci. USA 86:699-703.
27. Spellerberg, B., E. Rozdzinski, S. Martin, J. Weber-Heynemann, N. Schnitzler, R. Lutticken, and A. Podbielski. 1999. Lmb, a protein with similarities to the LraI adhesin family, mediates attachment of Streptococcus agalactiae to human laminin. Infect. Immun. 67:871-878.
28. Tamura, G. S., J. M. Kuypers, S. Smith, H. Raff, and C. E. Rubens. 1994. Adherence of group B streptococci to cultured epithelial cells: roles of environmental factors and bacterial surface components. Infect. Immun. 62:2450-2458.
29. Tamura, G. S., and A. Nittayajarn. 2000. Group B streptococci and other gram-positive cocci bind to cytokeratin 8. Infect. Immun. 68:2129-2134.
30. Tamura, G. S., A. Nittayajarn, and D. L. Schoentag. 2002. A glutamine transport gene, glnQ, is required for fibronectin adherence and virulence of group B streptococci. Infect. Immun. 70:2877-2885.
31. Tamura, G. S., and C. E. Rubens. 1995. Group B streptococci adhere to a variant of fibronectin attached to a solid phase. Mol. Microbiol. 15:581-589.
32. Ugarova, T. P., C. Zamarron, Y. Veklich, R. D. Bowditch, M. H. Ginsberg, J. W. Weisel, and E. F. Plow. 1995. Conformational transitions in the cell binding domain of fibronectin. Biochemistry 34:4457-4466.
33. van der Flier, M., N. Chhun, T. M. Wizemann, J. Min, J. B. McCarthy, and E. I. Tuomanen. 1995. Adherence of Streptococcus pneumoniae to immobilized fibronectin. Infect. Immun. 63:4317-4322.
34. Yang, K. D., N. H. Augustine, L. A. Gonzalez, J. F. Bohnsack, and H. R. Hill. 1988. Effects of fibronectin on the interaction of polymorphonuclear leukocytes with unopsonized and antibody-opsonized bacteria. J. Infect. Dis. 158:823-830.
35. Zhou, X. Z., J. M. Whiteley, J. A. Hoch, and K. I. Varughese. 1997. Purification and preliminary crystallographic studies on the sporulation response regulatory phosphotransferase protein, Spo0B, from Bacillus subtilis. Proteins 27:597-600.