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Volumn 18, Issue 3, 2012, Pages 314-321

Mutations in Streptococcus pneumoniae penicillin-binding protein 2x: Importance of the C-terminal penicillin-binding protein and serine/threonine kinase-associated domains for beta-lactam binding

Author keywords

[No Author keywords available]

Indexed keywords

BOCILLIN FL; CEFOTAXIME; CEFUROXIME; PENICILLIN BINDING PROTEIN 2X; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 84862002474     PISSN: 10766294     EISSN: 19318448     Source Type: Journal    
DOI: 10.1089/mdr.2012.0022     Document Type: Article
Times cited : (36)

References (24)
  • 1
    • 4143062511 scopus 로고    scopus 로고
    • Development of an optical biosensor assay for detection of β - Lactam antibiotics in milk using the penicillin-binding protein 2x
    • Cacciatore, G., M. Petz, S. Rachid, R. Hakenbeck, and A.A. Bergwerff. 2004. Development of an optical biosensor assay for detection of β - lactam antibiotics in milk using the penicillin-binding protein 2x. Anal. Chim. Acta 520:105-115.
    • (2004) Anal. Chim. Acta , vol.520 , pp. 105-115
    • Cacciatore, G.1    Petz, M.2    Rachid, S.3    Hakenbeck, R.4    Bergwerff, A.A.5
  • 2
    • 0035044203 scopus 로고    scopus 로고
    • Fluorescent Bocillins: Synthesis and application in the detection of penicillin-binding proteins
    • Gee, K.R., H.C. Kang, T.I. Meier, G. Zhao, and L.C. Blaszczak. 2001. Fluorescent Bocillins: synthesis and application in the detection of penicillin-binding proteins. Electrophoresis 22:960-965.
    • (2001) Electrophoresis , vol.22 , pp. 960-965
    • Gee, K.R.1    Kang, H.C.2    Meier, T.I.3    Zhao, G.4    Blaszczak, L.C.5
  • 3
    • 0036898699 scopus 로고    scopus 로고
    • Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: Presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent
    • Goffin, C., and J.-M. Ghuysen. 2002. Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent. Microbiol. Mol. Biol. Rev. 66:706-738.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 706-738
    • Goffin, C.1    Ghuysen, J.-M.2
  • 4
    • 0034595512 scopus 로고    scopus 로고
    • The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: Implication in drug resistance
    • Gordon, E., N. Mouz, E. Duee, and O. Dideberg. 2000. The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance. J. Mol. Biol. 299:477-485.
    • (2000) J. Mol. Biol. , vol.299 , pp. 477-485
    • Gordon, E.1    Mouz, N.2    Duee, E.3    Dideberg, O.4
  • 5
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and M.C. Peitsch. 1997. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 6
    • 84858024596 scopus 로고    scopus 로고
    • Molecular mechanism of beta-lactam resistance in Streptococcus pneumoniae
    • Hakenbeck, R., R. Brückner, D. Denapaite, and P. Maurer. 2012. Molecular mechanism of beta-lactam resistance in Streptococcus pneumoniae. Future Microbiol. 7:395-410.
    • (2012) Future Microbiol. , vol.7 , pp. 395-410
    • Hakenbeck, R.1    Brückner, R.2    Denapaite, D.3    Maurer, P.4
  • 7
    • 0023093968 scopus 로고
    • Interaction of non-lytic b-lactams with penicillin-binding proteins in Streptococcus pneumoniae
    • Hakenbeck, R., S. Tornette, and N.F. Adkinson. 1987. Interaction of non-lytic b-lactams with penicillin-binding proteins in Streptococcus pneumoniae. J. Gen. Microbiol. 133:755-760.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 755-760
    • Hakenbeck, R.1    Tornette, S.2    Adkinson, N.F.3
  • 8
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis fo DNA fragments: Study of protein and DNA interaction
    • Higuchi, R., B. Krummel, and R.K. Saiki. 1988. A general method of in vitro preparation and specific mutagenesis fo DNA fragments: study of protein and DNA interaction. Nucleic Acids Res. 16:7351-7367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 9
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 10
    • 0000331730 scopus 로고
    • A study of the genetic material determining an enzyme activity in pneumococcus
    • Lacks, S., and R.D. Hotchkiss. 1960. A study of the genetic material determining an enzyme activity in pneumococcus. Biochim. Biophys. Acta 39:508-517.
    • (1960) Biochim. Biophys. Acta , vol.39 , pp. 508-517
    • Lacks, S.1    Hotchkiss, R.D.2
  • 11
    • 0023444805 scopus 로고
    • Penicillin-binding proteins in b-lactam-resistant laboratory mutants of Streptococcus pneumoniae
    • Laible, G., and R. Hakenbeck. 1987. Penicillin-binding proteins in b-lactam-resistant laboratory mutants of Streptococcus pneumoniae. Mol. Microbiol. 1:355-363.
    • (1987) Mol. Microbiol. , vol.1 , pp. 355-363
    • Laible, G.1    Hakenbeck, R.2
  • 12
    • 0025720144 scopus 로고
    • Five independent combinations of mutations can result in low-affinity penicillin- binding protein 2x of Streptococcus pneumoniae
    • Laible, G., and R. Hakenbeck. 1991. Five independent combinations of mutations can result in low-affinity penicillin- binding protein 2x of Streptococcus pneumoniae. J. Bacteriol. 173:6986-6990.
    • (1991) J. Bacteriol. , vol.173 , pp. 6986-6990
    • Laible, G.1    Hakenbeck, R.2
  • 13
    • 78651376345 scopus 로고    scopus 로고
    • Recognition of peptidoglycan and b-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae
    • Maestro, B., L. Novaková, D. Hesek, M. Lee, E. Leyva, S. Mobashery, J.M. Sanz, and P. Branny. 2011. Recognition of peptidoglycan and b-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae. FEBS Lett. 585:357-363.
    • (2011) FEBS Lett. , vol.585 , pp. 357-363
    • Maestro, B.1    Novaková, L.2    Hesek, D.3    Lee, M.4    Leyva, E.5    Mobashery, S.6    Sanz, J.M.7    Branny, P.8
  • 14
    • 33644785222 scopus 로고    scopus 로고
    • The CiaRH system of Streptococcus pneumoniae prevents lysis during stress induced by treatment with cell wall inhibitors and mutations in pbp2x involved in beta-lactam resistance
    • Mascher, T., M. Heintz, D. Zähner, M. Merai, and R. Hakenbeck. 2006. The CiaRH system of Streptococcus pneumoniae prevents lysis during stress induced by treatment with cell wall inhibitors and mutations in pbp2x involved in beta-lactam resistance. J. Bacteriol. 188:1959-1968.
    • (2006) J. Bacteriol. , vol.188 , pp. 1959-1968
    • Mascher, T.1    Heintz, M.2    Zähner, D.3    Merai, M.4    Hakenbeck, R.5
  • 15
    • 39149111919 scopus 로고    scopus 로고
    • Penicillin-Binding Protein 2x of Streptococcus pneumoniae: Three new mutational pathways for remodelling an essential enzyme into a resistance determinant
    • Maurer, P., B. Koch, I. Zerfaß, J. Krauß, M. van der Linden, J.-M. Frère, C. Contreras-Martel, and R. Hakenbeck. 2008. Penicillin-Binding Protein 2x of Streptococcus pneumoniae: Three new mutational pathways for remodelling an essential enzyme into a resistance determinant. J. Mol. Biol. 376:1403-1416.
    • (2008) J. Mol. Biol. , vol.376 , pp. 1403-1416
    • Maurer, P.1    Koch, B.2    Zerfaß, I.3    Krauß, J.4    Van Der Linden, M.5    Frère, J.-M.6    Contreras-Martel, C.7    Hakenbeck, R.8
  • 16
    • 79960964670 scopus 로고    scopus 로고
    • The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization
    • Mir, M., J. Asong, X. Li, J. Cardot, G.J. Boons, and R.N. Husson. 2011. The extracytoplasmic domain of the Mycobacterium tuberculosis Ser/Thr kinase PknB binds specific muropeptides and is required for PknB localization. PLoS Pathog. 7:e1002182.
    • (2011) PLoS Pathog. , vol.7
    • Mir, M.1    Asong, J.2    Li, X.3    Cardot, J.4    Boons, G.J.5    Husson, R.N.6
  • 17
    • 0029988098 scopus 로고    scopus 로고
    • X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme
    • Pares, S., N. Mouz, Y. Pétillot, R. Hakenbeck, and O. Dideberg. 1996. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nat. Struct. Biol. 3:284-289.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 284-289
    • Pares, S.1    Mouz, N.2    Pétillot, Y.3    Hakenbeck, R.4    Dideberg, O.5
  • 19
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis
    • Sauvage, E., F. Kerff, M. Terrak, J. Ayala, and P. Charlier. 2008. The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. FEMS Microbiol. Rev. 32: 234-258.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.4    Charlier, P.5
  • 20
    • 54549099189 scopus 로고    scopus 로고
    • A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments
    • Shah, I.M., M.H. Laaberki, D.L. Popham, and J. Dworkin. 2008. A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 135:486-496.
    • (2008) Cell , vol.135 , pp. 486-496
    • Shah, I.M.1    Laaberki, M.H.2    Popham, D.L.3    Dworkin, J.4
  • 21
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper, D.J., and J.L. Strominger. 1965. Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl. Acad. Sci. U. S. A. 54:1133-1141.
    • (1965) Proc. Natl. Acad. Sci. U. S. A. , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 22
    • 0036711089 scopus 로고    scopus 로고
    • The PASTA domain: A beta-lactam-binding domain
    • Yeats, C., R.D. Finn, and A. Bateman. 2002. The PASTA domain: a beta-lactam-binding domain. Trends Biochem. Sci. 27:438.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 438
    • Yeats, C.1    Finn, R.D.2    Bateman, A.3
  • 24
    • 62949215691 scopus 로고    scopus 로고
    • An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: Mutational analysis of Thr338
    • Zerfass, I., R. Hakenbeck, and D. Denapaite. 2009. An important site in PBP2x of penicillin-resistant clinical isolates of Streptococcus pneumoniae: mutational analysis of Thr338. Antimicrob. Agents Chemother. 53:1107-1115.
    • (2009) Antimicrob. Agents Chemother. , vol.53 , pp. 1107-1115
    • Zerfass, I.1    Hakenbeck, R.2    Denapaite, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.