Identification and structural basis of binding to host lung glycogen by streptococcal virulence factors (original) (raw)

• Manco, S. et al. Pneumococcal neuraminidases A and B both have essential roles during infection of the respiratory tract and sepsis. Infect. Immun. 74, 4014–4020 (2006).
  Article CAS Google Scholar
• Soong, G. et al. Bacterial neuraminidase facilitates mucosal infection by participating in biofilm production. J. Clin. Invest. 116, 2297–2305 (2006).
  Article CAS Google Scholar
• Hava, D.L. & Camilli, A. Large-scale identification of serotype 4 Streptococcus pneumoniae virulence factors. Mol. Microbiol. 45, 1389–1406 (2002).
  CAS PubMed PubMed Central Google Scholar
• Boraston, A.B., Bolam, D.N., Gilbert, H.J. & Davies, G.J. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem. J. 382, 769–781 (2004).
  Article CAS Google Scholar
• Lammerts van Bueren, A., Finn, R., Ausio, J. & Boraston, A.B. Alpha-glucan recognition by a new family of carbohydrate-binding modules found primarily in bacterial pathogens. Biochemistry 43, 15633–15642 (2004).
  Article Google Scholar
• Tomasz, A. New faces of an old pathogen: emergence and spread of multidrug-resistant Streptococcus pneumoniae. Am. J. Med. 107, 55S–62S (1999).
  Article CAS Google Scholar
• Cunningham, M.W. Pathogenesis of group A streptococcal infections. Clin. Microbiol. Rev. 13, 470–511 (2000).
  Article CAS Google Scholar
• Cengiz, A.B. et al. Fatal necrotizing pneumonia caused by group A streptococcus. J. Paediatr. Child Health 40, 69–71 (2004).
  Article CAS Google Scholar
• Morozumi, M. et al. Simultaneous detection of pathogens in clinical samples from patients with community-acquired pneumonia by real-time PCR with pathogen-specific molecular beacon probes. J. Clin. Microbiol. 44, 1440–1446 (2006).
  Article CAS Google Scholar
• Shelburne, S.A., III et al. Maltodextrin utilization plays a key role in the ability of group A Streptococcus to colonize the oropharynx. Infect. Immun. 74, 4605–4614 (2006).
  Article CAS Google Scholar
• Bongaerts, R.J., Heinz, H.P., Hadding, U. & Zysk, G. Antigenicity, expression, and molecular characterization of surface-located pullulanase of Streptococcus pneumoniae. Infect. Immun. 68, 7141–7143 (2000).
  Article CAS Google Scholar
• Hytonen, J., Haataja, S. & Finne, J. Streptococcus pyogenes glycoprotein-binding strepadhesin activity is mediated by a surface-associated carbohydrate-degrading enzyme, pullulanase. Infect. Immun. 71, 784–793 (2003).
  Article CAS Google Scholar
• Hytonen, J., Haataja, S. & Finne, J. Use of flow cytometry for the adhesion analysis of Streptococcus pyogenes mutant strains to epithelial cells: investigation of the possible role of surface pullulanase and cysteine protease, and the transcriptional regulator Rgg. BMC Microbiol. 6, 18 (2006).
  Article Google Scholar
• Kriegshauser, G. & Liebl, W. Pullulanase from the hyperthermophilic bacterium Thermotoga maritima: purification by beta-cyclodextrin affinity chromatography. J. Chromatogr. B Biomed. Sci. Appl. 737, 245–251 (2000).
  Article CAS Google Scholar
• Mikami, B. et al. Crystal structure of pullulanase: evidence for parallel binding of oligosaccharides in the active site. J. Mol. Biol. 359, 690–707 (2006).
  Article CAS Google Scholar
• Sorimachi, K., Le Gal-Coeffet, M.F., Williamson, G., Archer, D.B. & Williamson, M.P. Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. Structure 5, 647–661 (1997).
  Article CAS Google Scholar
• Boraston, A.B. et al. A structural and functional analysis of alpha-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition. J. Biol. Chem. 281, 587–598 (2006).
  Article CAS Google Scholar
• Boraston, A.B., Kwan, E., Chiu, P., Warren, R.A. & Kilburn, D.G. Recognition and hydrolysis of noncrystalline cellulose. J. Biol. Chem. 278, 6120–6127 (2003).
  Article CAS Google Scholar
• Lammerts van Bueren, A. & Boraston, A.B. The structural basis of alpha-glucan recognition by a family 41 carbohydrate-binding module from Thermotoga maritima. J. Mol. Biol. published online 11 October 2006 (doi:10.1016/j.jmb.2006.10.018).
• Sorimachi, K. et al. Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy. J. Mol. Biol. 259, 970–987 (1996).
  Article CAS Google Scholar
• Sakon, J., Irwin, D., Wilson, D.B. & Karplus, P.A. Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca. Nat. Struct. Biol. 4, 810–818 (1997).
  Article CAS Google Scholar
• Weaver, T.E. & Conkright, J.J. Function of surfactant proteins B and C. Annu. Rev. Physiol. 63, 555–578 (2001).
  Article CAS Google Scholar
• Glasser, S.W. et al. Pneumonitis and emphysema in sp-C gene targeted mice. J. Biol. Chem. 278, 14291–14298 (2003).
  Article CAS Google Scholar
• Cundell, D.R. & Tuomanen, E.I. Receptor specificity of adherence of Streptococcus pneumoniae to human type-II pneumocytes and vascular endothelial cells in vitro. Microb. Pathog. 17, 361–374 (1994).
  Article CAS Google Scholar
• Kadioglu, A. et al. Use of green fluorescent protein in visualisation of pneumococcal invasion of broncho-epithelial cells in vivo. FEMS Microbiol. Lett. 194, 105–110 (2001).
  Article CAS Google Scholar
• Ridsdale, R. & Post, M. Surfactant lipid synthesis and lamellar body formation in glycogen-laden type II cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 287, L743–L751 (2004).
  Article CAS Google Scholar
• Rannels, S.R., Rannels, S.L., Sneyd, J.G. & Loten, E.G. Fetal lung development in rats with a glycogen storage disorder. Am. J. Physiol. 260, L419–L427 (1991).
  CAS PubMed Google Scholar
• Rooney, S.A. Regulation of surfactant secretion. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 129, 233–243 (2001).
  Article CAS Google Scholar
• Jounblat, R. et al. Binding and agglutination of Streptococcus pneumoniae by human surfactant protein D (SP-D) vary between strains, but SP-D fails to enhance killing by neutrophils. Infect. Immun. 72, 709–716 (2004).
  Article CAS Google Scholar
• Barik, S. Site-directed mutagenesis in vitro by megaprimer PCR. Methods Mol. Biol. 57, 203–215 (1996).
  CAS PubMed Google Scholar
• Boraston, A.B. et al. Binding specificity and thermodynamics of a family 9 carbohydrate-binding module from Thermotoga maritima xylanase 10A. Biochemistry 40, 6240–6247 (2001).
  Article CAS Google Scholar
• Ficko-Blean, E. & Boraston, A.B. Cloning, recombinant production, crystallization and preliminary X-ray diffraction studies of a family 84 glycoside hydrolase from Clostridium perfringens. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. 61, 834–836 (2005).
  Article CAS Google Scholar
• Mach, H., Middaugh, C.R. & Lewis, R.V. Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Anal. Biochem. 200, 74–80 (1992).
  Article CAS Google Scholar
• Tomme, P., Boraston, A., Kormos, J.M., Warren, R.A. & Kilburn, D.G. Affinity electrophoresis for the identification and characterization of soluble sugar binding by carbohydrate-binding modules. Enzyme Microb. Technol. 27, 453–458 (2000).
  Article CAS Google Scholar
• Sigurskjold, B.W., Altman, E. & Bundle, D.R. Sensitive titration microcalorimetric study of the binding of Salmonella O-antigenic oligosaccharides by a monoclonal antibody. Eur. J. Biochem. 197, 239–246 (1991).
  Article CAS Google Scholar
• Pflugrath, J.W. The finer things in X-ray diffraction data collection. Acta Crystallogr. D Biol. Crystallogr. 55, 1718–1725 (1999).
  Article CAS Google Scholar
• Schneider, T.R. & Sheldrick, G.M. Substructure solution with SHELXD. Acta Crystallogr. D Biol. Crystallogr. 58, 1772–1779 (2002).
  Article Google Scholar
• Evans, G. & Bricogne, G. Triiodide derivatization and combinatorial counter-ion replacement: two methods for enhancing phasing signal using laboratory Cu Kalpha X-ray equipment. Acta Crystallogr. D Biol. Crystallogr. 58, 976–991 (2002).
  Article Google Scholar
• Cowtan, K.D. & Zhang, K.Y. Density modification for macromolecular phase improvement. Prog. Biophys. Mol. Biol. 72, 245–270 (1999).
  Article CAS Google Scholar
• Perrakis, A., Morris, R. & Lamzin, V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6, 458–463 (1999).
  Article CAS Google Scholar
• Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126–2132 (2004).
  Article Google Scholar
• Murshudov, G.N., Vagin, A.A. & Dodson, E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53, 240–255 (1997).
  Article CAS Google Scholar
• Vagin, A. & Teplyakov, A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56, 1622–1624 (2000).
  Article CAS Google Scholar
• Brunger, A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472–475 (1992).
  Article CAS Google Scholar
• Read, R.J. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A 42, 140–149 (1986).
  Article Google Scholar