Identification of genetic determinants and enzymes involved with the amidation of glutamic acid residues in the peptidoglycan of Staphylococcus aureus

PLoS Pathogens

Volumn 8, Issue 1, 2012, Pages

  Figueiredo, Teresa A ^a   Sobral, Rita G ^a,b   Ludovice, Ana Madalena ^a,b   de Almeida, João Manuel Feio ^b   Bui, Nhat K ^c   Vollmer, Waldemar ^c   de Lencastre, Hermínia ^a,d   Tomasz, Alexander ^d  

^a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^b UNIVERSIDADE NOVA DE LISBOA   (Portugal)

^c NEWCASTLE UNIVERSITY   (United Kingdom)

^d ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMIC ACID; PEPTIDOGLYCAN; AMIDASE; BACTERIAL PROTEIN;

AMIDATION; ARTICLE; BACTERIAL GENE; BACTERIAL GENOME; BACTERIAL GROWTH; BACTERIAL STRAIN; GATD GENE; GENE IDENTIFICATION; GROWTH INHIBITION; MURT GENE; NONHUMAN; STAPHYLOCOCCUS AUREUS; AMINO ACID SEQUENCE; GENETICS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; NORTHERN BLOTTING; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

STAPHYLOCOCCUS AUREUS;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BLOTTING, NORTHERN; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; GENES, BACTERIAL; GLUTAMIC ACID; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; PEPTIDOGLYCAN; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; STAPHYLOCOCCUS AUREUS;

EID: 84857491427     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1002508     Document Type: Article

References (28)

1. Smith CA, (2006) Structure, function and dynamics in the mur family of bacterial cell wall ligases. J Mol Biol 362: 640-655.
2. Bera A, Herbert S, Jakob A, Vollmer W, Gotz F, (2005) Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol Microbiol 55: 778-787.
3. Vollmer W, Blanot D, de Pedro MA, (2008) Peptidoglycan structure and architecture. FEMS Microbiol Rev 32: 149-167.
4. Ornelas-Soares A, de Lencastre H, de Jonge B, Gage D, Chang YS, et al. (1993) The peptidoglycan composition of a Staphylococcus aureus mutant selected for reduced methicillin resistance. J Biol Chem 268: 26268-26272.
5. UniProtConsortium (2010) Ongoing and future developments at the Universal Protein Resource. Nucleic Acids Res 39: D214-219.
6. Zdobnov EM, Apweiler R, (2001) InterProScan-an integration platform for the signature-recognition methods in InterPro. Bioinformatics 17: 847-848.
7. Notredame C, Higgins DG, Heringa J, (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 302: 205-217.
8. Bryson K, McGuffin LJ, Marsden RL, Ward JJ, Sodhi JS, et al. (2005) Protein structure prediction servers at University College London. Nucleic Acids Res 33: W36-38.
9. Galperin MY, Grishin NV, (2000) The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase. Proteins 41: 238-247.
10. Sobral RG, Ludovice AM, de Lencastre H, Tomasz A, (2006) Role of murF in cell wall biosynthesis: isolation and characterization of a murF conditional mutant of Staphylococcus aureus. J Bacteriol 188: 2543-2553.
11. Kraemer GR, Iandolo JJ, (1990) High-frequency transformation of Staphylococcus aureus by electroporation. Curr Microb 21: 373-376.
12. Oshida T, Tomasz A, (1992) Isolation and characterization of a Tn551-autolysis mutant of Staphylococcus aureus. J Bacteriol 174: 4952-4959.
13. Grkovic S, Brown MH, Hardie KM, Firth N, Skurray RA, (2003) Stable low-copy-number Staphylococcus aureus shuttle vectors. Microbiology 149: 785-794.
14. Sobral RG, Ludovice AM, Gardete S, Tabei K, De Lencastre H, et al. (2003) Normally functioning murF is essential for the optimal expression of methicillin resistance in Staphylococcus aureus. Microb Drug Resist 9: 231-241.
15. Crisostomo MI, Vollmer W, Kharat AS, Inhulsen S, Gehre F, et al. (2006) Attenuation of penicillin resistance in a peptidoglycan O-acetyl transferase mutant of Streptococcus pneumoniae. Mol Microbiol 61: 1497-1509.
16. de Jonge BL, Chang YS, Gage D, Tomasz A, (1992) Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain. The role of penicillin binding protein 2A. J Biol Chem 267: 11248-11254.
17. Bui NK, Gray J, Schwarz H, Schumann P, Blanot D, et al. (2009) The peptidoglycan sacculus of Myxococcus xanthus has unusual structural features and is degraded during glycerol-induced myxospore development. J Bacteriol 191: 494-505.
18. Kohlrausch U, Holtje JV, (1991) One-step purification procedure for UDP-N-acetylmuramyl-peptide murein precursors from Bacillus cereus. FEMS Microbiol Lett 62: 253-257.
19. Herbert S, Bera A, Nerz C, Kraus D, Peschel A, et al. (2007) Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci. PLoS Pathog 3: e102.
20. Siewert G, Strominger JL, (1968) Biosynthesis of the peptidoglycan of bacterial cell walls. XI. Formation of the isoglutamine amide group in the cell walls of Staphylococcus aureus. J Biol Chem 243: 783-790.
21. Massiere F, Badet-Denisot MA, (1998) The mechanism of glutamine-dependent amidotransferases. Cell Mol Life Sci 54: 205-222.
22. Gustafson J, Strassle A, Hachler H, Kayser FH, Berger-Bachi B, (1994) The femC locus of Staphylococcus aureus required for methicillin resistance includes the glutamine synthetase operon. J Bacteriol 176: 1460-1467.
23. De Lencastre H, Wu SW, Pinho MG, Ludovice AM, Filipe S, et al. (1999) Antibiotic resistance as a stress response: complete sequencing of a large number of chromosomal loci in Staphylococcus aureus strain COL that impact on the expression of resistance to methicillin. Microb Drug Resist 5: 163-175.
24. Bera A, Biswas R, Herbert S, Kulauzovic E, Weidenmaier C, et al. (2007) Influence of wall teichoic acid on lysozyme resistance in Staphylococcus aureus. J Bacteriol 189: 280-283.
25. Boneca IG, (2005) The role of peptidoglycan in pathogenesis. Curr Opin Microbiol 8: 46-53.
26. Wolfert MA, Roychowdhury A, Boons GJ, (2007) Modification of the structure of peptidoglycan is a strategy to avoid detection by nucleotide-binding oligomerization domain protein 1. Infect Immun 75: 706-713.
27. Kraus D, Kalbacher H, Buschmann J, Berger-Bachi B, Gotz F, et al. (2007) Muropeptide modification-amidation of peptidoglycan D-glutamate does not affect the proinflammatory activity of Staphylococcus aureus. Infect Immun 75: 2084-2087.
28. Kern T, Giffard M, Hediger S, Amoroso A, Giustini C, et al. (2010) Dynamics characterization of fully hydrated bacterial cell walls by solid-state NMR: evidence for cooperative binding of metal ions. J Am Chem Soc 132: 10911-10919.