1887

Abstract

PBP5, PBP6 and DacD, encoded by , and , respectively, share substantial amino acid identity and together constitute ~50 % of the total penicillin-binding proteins of . PBP5 helps maintain intrinsic β-lactam resistance within the cell. To test if PBP6 and DacD play simlar roles, we deleted and individually, and in combination with , from 2443 and compared β-lactam sensitivity of the mutants and the parent strain. β-Lactam resistance was complemented by wild-type, but not -carboxypeptidase-deficient PBP5, confirming that enzymic activity of PBP5 is essential for β-lactam resistance. Deletion of and expression of PBP6 during exponential or stationary phase did not alter β-lactam resistance of a mutant. Expression of DacD during mid-exponential phase partially restored β-lactam resistance of the mutant. Therefore, PBP5 -carboxypeptidase activity is essential for intrinsic β-lactam resistance of and DacD can partially compensate for PBP5 in this capacity, whereas PBP6 cannot.

Funding
This study was supported by the:
  • Indian Council for Medical Research (ICMR)
  • Department of Biotechnology (DBT), Government of India
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2011-09-01
2021-05-16
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