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Gene Review

SP_1937  -  autolysin

Streptococcus pneumoniae TIGR4

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Disease relevance of SP_1937


High impact information on SP_1937

  • Several pneumococcal proteins including pneumococcal surface proteins A and C, hyaluronate lyase, pneumolysin, autolysin, pneumococcal surface antigen A, choline binding protein A, and two neuraminidase enzymes are being investigated as potential vaccine or drug targets [7].
  • Pneumococci carrying defined mutations in the genes encoding any one of at least three pneumococcal proteins (the toxin pneumolysin, the major pneumococcal autolysin, and pneumococcal surface protein A) have significantly reduced virulence [8].
  • The first crystal structure of a choline binding domain, from the toxin-releasing enzyme pneumococcal major autolysin (LytA), reveals a novel solenoid fold consisting exclusively of beta-hairpins that stack to form a left-handed superhelix [9].
  • Activation of an inactive form of autolysin by in vitro incubation with choline-containing cell walls is also inhibited by lipoteichoic acid [1].
  • Choline-containing pneumococcal cell wals are sensitive to autolysin, whereas ethanolamine-containing walls are not [10].

Chemical compound and disease context of SP_1937


Biological context of SP_1937


Anatomical context of SP_1937


Associations of SP_1937 with chemical compounds


Other interactions of SP_1937


Analytical, diagnostic and therapeutic context of SP_1937



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  2. Ofloxacin-like antibiotics inhibit pneumococcal cell wall-degrading virulence factors. Fernández-Tornero, C., García, E., de Pascual-Teresa, B., López, R., Giménez-Gallego, G., Romero, A. J. Biol. Chem. (2005) [Pubmed]
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  14. Autolysin-targeted LightCycler assay including internal process control for detection of Streptococcus pneumoniae DNA in clinical samples. Sheppard, C.L., Harrison, T.G., Morris, R., Hogan, A., George, R.C. J. Med. Microbiol. (2004) [Pubmed]
  15. Specific recognition of choline residues in the cell wall teichoic acid by the N-acetylmuramyl-L-alanine amidase of Pneumococcus. Höltje, J.V., Tomasz, A. J. Biol. Chem. (1975) [Pubmed]
  16. The puzzle of zmpB and extensive chain formation, autolysis defect and non-translocation of choline-binding proteins in Streptococcus pneumoniae. Bergé, M., García, P., Iannelli, F., Prère, M.F., Granadel, C., Polissi, A., Claverys, J.P. Mol. Microbiol. (2001) [Pubmed]
  17. Penicillin tolerance genes of Streptococcus pneumoniae: the ABC-type manganese permease complex Psa. Novak, R., Braun, J.S., Charpentier, E., Tuomanen, E. Mol. Microbiol. (1998) [Pubmed]
  18. Genosensor based on a platinum(II) complex as electrocatalytic label. Hernández-Santos, D., González-García, M.B., Costa-García, A. Anal. Chem. (2005) [Pubmed]
  19. The role of pneumolysin and autolysin in the pathology of pneumonia and septicemia in mice infected with a type 2 pneumococcus. Canvin, J.R., Marvin, A.P., Sivakumaran, M., Paton, J.C., Boulnois, G.J., Andrew, P.W., Mitchell, T.J. J. Infect. Dis. (1995) [Pubmed]
  20. Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Tomasz, A., Waks, S. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  21. Roles of autolysin and pneumolysin in middle ear inflammation caused by a type 3 Streptococcus pneumoniae strain in the chinchilla otitis media model. Sato, K., Quartey, M.K., Liebeler, C.L., Le, C.T., Giebink, G.S. Infect. Immun. (1996) [Pubmed]
  22. Protoplast formation and leakage of intramembrane cell components: induction by the competence activator substance of pneumococci. Seto, H., Tomasz, A. J. Bacteriol. (1975) [Pubmed]
  23. Abnormal physiological properties and altered cell wall composition in Streptococcus pneumoniae grown in the presence of clavulanic acid. Severin, A., Severina, E., Tomasz, A. Antimicrob. Agents Chemother. (1997) [Pubmed]
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  25. Contribution of the ATP-dependent protease ClpCP to the autolysis and virulence of Streptococcus pneumoniae. Ibrahim, Y.M., Kerr, A.R., Silva, N.A., Mitchell, T.J. Infect. Immun. (2005) [Pubmed]
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  30. Expression, crystallization and preliminary X-ray diffraction studies on the complete choline-binding domain of the major pneumococcal autolysin. Fernández-Tornero, C., Ramón, A., Fernández-Cabrera, C., Giménez-Gallego, G., Romero, A. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
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