Plasmid-specified FemABX-like immunity factor in Staphylococcus sciuri DD 4747

FEMS Microbiology Letters

Volumn 249, Issue 2, 2005, Pages 227-231

  Heath, Lucie S ^a   Gargis, Shaw R ^a   Smithberg, S Rochelle ^a   Johnson, Heather P ^b   Heath, Harry E ^a   LeBlanc, Paul A ^a   Sloan, Gary L ^a  

^a UNIVERSITY OF ALABAMA   (United States)

^b WESTERN KENTUCKY UNIVERSITY   (United States)

Author keywords

FemABX like immunity factor; Lysostaphin resistance; Peptidoglycan modification; Staphylococcus sciuri

Indexed keywords

BACTERIAL PROTEIN; FEMABX-LIKE PROTEIN; LYSOSTAPHIN; N ACETYLMURAMOYLALANINE AMIDASE; PEPTIDOGLYCAN; PROTEINASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL STRAIN; GENE FUNCTION; GENE REPLICATION; GENETIC RECOMBINATION; IMMUNITY; MULTIGENE FAMILY; NONHUMAN; OPEN READING FRAME; PLASMID; PRIORITY JOURNAL; SHUTTLE VECTOR; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS SCIURI;

BACTERIAL PROTEINS; BASE SEQUENCE; DNA PRIMERS; DNA, BACTERIAL; DRUG RESISTANCE, MICROBIAL; ENDOPEPTIDASES; OPEN READING FRAMES; PLASMIDS; RESTRICTION MAPPING; STAPHYLOCOCCUS;

STAPHYLOCOCCUS SCIURI;

EID: 23644460681     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2005.06.019     Document Type: Article

References (23)

1. S. Rohrer, and B. Berger-Bächi FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and β-lactam resistance in Gram-positive cocci Antimicrob. Agents Chemother. 47 2003 837 846
2. G.L. Sloan, J.M. Robinson, and W.E. Kloos Identification of Staphylococcus staphylolyticus NRRL B-2628 as a biovar of Staphylococcus simulans Int. J. Syst. Bacteriol. 32 1982 170 174
3. H.E. Heath, L.S. Heath, J.D. Nitterauer, K.E. Rose, and G.L. Sloan Plasmid-encoded lysostaphin endopeptidase resistance of Staphylococcus simulans biovar staphylolyticus Biochem. Biophys. Res. Commun. 160 1989 1106 1109
4. H.P. DeHart, H.E. Heath, L.S. Heath, P.A. LeBlanc, and G.L. Sloan The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross-bridges in Staphylococcus simulans and Staphylococcus aureus Appl. Environ. Microbiol. 61 1995 1475 1479
5. G. Thumm, and F. Götz Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus Mol. Microbiol. 23 1997 1251 1265
6. K. Ehlert, M. Tschierske, C. Mori, W. Schröder, and B. Berger-Bächi Site-specific serine incorporation by Lif and Epr into positions 3 and 5 of the staphylococcal peptidoglycan interpeptide bridge J. Bacteriol. 182 2000 2635 2638
7. S. Rohrer, and B. Berger-Bächi Application of a bacterial two-hybrid system for the analysis of protein-protein interactions between FemABX family proteins Microbiology 149 2003 2733 2738
8. M. Sugai, T. Fujiwara, K. Ohta, H. Komatsuzawa, M. Ohara, and H. Suginaka epr, which encodes glycylglycine endopeptidase resistance, is homologous to femAB and affects serine content of peptidoglycan cross-bridges in Staphylococcus capitis and Staphylococcus aureus J. Bacteriol. 179 1997 4311 4318
9. S.A. Beatson, G.L. Sloan, and R.S. Simmonds Zoocin A immunity factor: a femA-like gene found in a group C streptococcus FEMS Microbiol. Lett. 163 1998 73 77
10. M. Beukes, and J.W. Hastings Self-protection against cell wall hydrolysis in Streptococcus milleri NMSCC 061 and analysis of the millericin B operon Appl. Environ. Microbiol. 67 2001 3888 3896
11. W.E. Kloos, D.N. Ballard, J.A. Webster, R.J. Hubner, A. Tomasz, I. Couto, G.L. Sloan, H.P. DeHart, F. Fiedler, K. Schubert, H. De Lencastre, I.S. Sanches, H.E. Heath, P.A. LeBlanc, and A. Ljungh Ribotype delineation and description of Staphylococcus sciuri subspecies and their potential as reservoirs for methicillin resistance and staphylolytic enzyme genes Int. J. Syst. Bacteriol. 47 1997 313 323
12. R.P. Novick Genetic systems in staphylococci Meth. Enzymol. 204 1991 587 636
13. C.Y. Lee, and J.J. Iandolo Integration of staphylococcocal phage L54a occurs by site-specific recombination: structural analysis of the attachment sites Proc. Natl. Acad. Sci. USA 83 1986 5474 5478
14. J. Perez-Casal, M.G. Caparon, and J.R. Scott Mry, a trans-acting positive regulator of the M protein gene of Streptococcus pyogenes with similarity to the receptor proteins of two-component regulatory systems J. Bacteriol. 173 1991 2617 2624
15. J.M. Robinson, H.E. Heath, and G.L. Sloan Lack of pleiotropic compensation in hypoproducing variants of Staphylococcus simulans biovar staphylolyticus J. Gen. Microbiol. 133 1987 253 257
16. J.E. Sambrook, E.F. Fritsch, and T. Maniatis Molecular Cloning: A Laboratory Manual second ed. 1989 Cold Spring Harbor Laboratory Press Cold Spring Harbor Laboratory, NY
17. L.S. Heath, G.L. Sloan, and H.E. Heath A simple and generally applicable procedure for releasing DNA from bacterial cells Appl. Environ. Microbiol. 51 1986 1138 1140
18. T.A. Hall BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT Nucl. Acids. Symp. Ser. 41 1999 95 98
19. S.F. Altschul, T.F. Madden, A.A. Schäffer, J. Zhang, Z. Zhang, W. Miller, and D.J. Lipman Gapped BLAST and PSI-BLAST: a new generation of protein database search programs Nucl. Acids Res. 25 1997 3389 3402
20. S. Schenk, and R.A. Laddaga Improved method for electroporation of Staphylococcus aureus FEMS Microbiol. Lett. 94 1992 133 138
21. U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature (London) 227 1970 680 685
22. V.C. Neumann, H.E. Heath, P.A. LeBlanc, and G.L. Sloan Extracellular proteolytic activation of bacterial peptidoglycan hydrolases of Staphylococcus simulans biovar staphylolyticus FEMS Microbiol. Lett. 110 1993 205 212
23. J.D. Nitterauer, H.E. Heath, L.S. Heath, P.A. LeBlanc, and G.L. Sloan Characteristics of extracellular protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus FEMS Microbiol. Lett. 84 1991 23 26