The putative penicillin-binding proteins 1 and 2 are important for viability, growth and cell morphology of Brucella melitensis

Veterinary Microbiology

Volumn 133, Issue 4, 2009, Pages 387-393

  Bandara, Aloka B ^a   Schurig, Gerhardt G ^a   Sriranganathan, Nammalwar ^a   Prasad, Rajeev ^a   Boyle, Stephen M ^a  

^a CENTER FOR MOLECULAR MEDICINE AND INFECTIOUS DISEASES   (United States)

Author keywords

Cell wall; Glycosyl transferase; Penicillin binding proteins; Peptidoglycan; Transpeptidase

Indexed keywords

ANIMALS; BRUCELLA MELITENSIS; CELL LINE; GENE EXPRESSION REGULATION, BACTERIAL; MACROPHAGES; MICE; MICE, INBRED BALB C; PENICILLIN-BINDING PROTEINS;

BACILLUS (BACTERIUM); BACTERIA (MICROORGANISMS); BRUCELLA MELITENSIS; MUS;

EID: 58149093389     PISSN: 03781135     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetmic.2008.07.019     Document Type: Article

References (24)

1. Altschul S., Gish W., Miller W., Myers E., and Lipman D. Basic local alignment search tool. J. Mol. Biol. 215 (1990) 403-410
2. Banai M., Adams L.G., Frey M., Pugh R., and Ficht T.A. The myth of Brucella L-forms and possible involvement of Brucella penicillin binding proteins in pathogenicity. Vet. Microbiol. 90 (2002) 263-279
3. Bandara A.B., Sriranganathan N., Schurig G.G., and Boyle S.M. Carboxyl-terminal protease regulates Brucella suis morphology in culture and persistence in macrophages and mice. J. Bacteriol. 187 16 (2005) 5767-5775
4. Delvacchio V.G., Kapartal V., and Patra R.J. The genome sequence of the facultative intracellular pathogen Brucella melitensis. Proc. Natl. Acad. Sci. U.S.A. 99 (2001) 443-448
5. Höltje J.-V. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62 (1998) 181-203
6. Kato J.-I., Suzuki H., and Hirota Y. Dispensability of either penicillin-binding protein-1a or -1b involved in the essential process for cell elongation in Escherichia coli. Mol. Genet. 200 (1985) 272-277
7. Lentner M., and Bishop T. Experimental Design and Analysis. Second edition (1993), Valley Book Company, Blacksburg, VA
8. McPherson D.C., and Popham D.L. Peptidoglycan synthesis in the absence of class A penicillin-binding proteins in Bacillus subtilis. J. Bacteriol. 185 (2003) 1423-1431
9. McQuiston J.R., Schurig G.G., Sriranganathan N., and Boyle S.M. Transformation of Brucella species with suicide and broad host-range plasmids. Methods Mol. Biol. 47 (1995) 143-148
10. Nanninga N. Morphogenesis of Escherichia coli. Microbiol. Mol. Biol. Rev. 62 (1998) 110-129
11. Nelson D.E., and Young K.D. Penicillin binding protein 5 affects cell diameter, contour, and morphology of Escherichia coli. J. Bacteriol. 182 (2000) 1714-1721
12. Nelson D.E., and Young K.D. Contributions of PBP 5 and DD-carboxypeptidase penicillin binding proteins to maintenance of cell shape in Escherichia coli. J. Bacteriol. 183 (2001) 3055-3064
13. Nelson D.E., Ghosh A.S., Paulson A.L., and Young K.D. Contribution of membrane-binding and enzymatic domains of penicillin binding protein 5 to maintenance of uniform cellular morphology of Escherichia coli. J. Bacteriol. 184 (2002) 3630-3639
14. Popham D.L., and Setlow P. Cloning, nucleotide sequence, and mutagenesis of the Bacillus subtilis ponA operon, which codes for penicillin-binding protein (PBP) 1 and a PBP-related factor. J. Bacteriol. 177 (1995) 326-335
15. Popham D.L., and Setlow P. Phenotypes of Bacillus subtilis mutants lacking multiple class A high-molecular-weight penicillin-binding proteins. J. Bacteriol. 178 (1996) 2079-2085
16. Ried J.L., and Colmer A. An npt-sacB-sacR cartridge for constructing directed, unmarked mutations in gram-negative bacteria by marker exchange-eviction mutagenesis. Gene 57 (1987) 239-246
17. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd ed. (1989), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
18. Schurig G.G., Roop R.M., Bagchi T., Boyle S.M., Buhrman D., and Sriranganathan N. Biological properties of RB51: a stable rough strain of Brucella abortus. Vet. Microbiol. 28 (1991) 171-188
19. Spratt B.G. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. U.S.A. 72 (1975) 2999-3003
20. Spratt B.G. Properties of the penicillin-binding proteins of Escherichia coli K12. Eur. J. Biochem. 72 (1977) 341-352
21. Spratt B.G., and Pardee A.B. Penicillin-binding proteins and cell shape in Escherichia coli. Nature 254 (1975) 516-517
22. Wei Y., Havasy T., McPherson D.C., and Popham D.L. Rod shape determination by the Bacillus subtilis class B penicillin-binding proteins encoded by pbpA and pbpH. J. Bacteriol. 185 (2003) 4717-4726
23. Young K.D. Approaching the physiological functions of penicillin-binding proteins in Escherichia coli. Biochimie 83 (2001) 99-102
24. Yousif S.Y., Broome-Smith J.K., and Spratt B.G. Lysis of Escherichia coli by beta-lactam antibiotics: deletion analysis of the role of penicillin-binding proteins 1A and 1B. J. Gen. Microbiol. 131 (1985) 2839-2845