Expanded profiling of β-lactam selectivity for penicillin-binding proteins in Streptococcus pneumoniae D39.

ABSTRACT: Penicillin-binding proteins (PBPs) are integral to bacterial cell division as they mediate the final steps of cell wall maturation. Selective fluorescent probes are useful for understanding the role of individual PBPs, including their localization and activity during growth and division of bacteria. For the development of new selective probes for PBP imaging, several β-lactam antibiotics were screened, as they are known to covalently bind PBP in vivo. The PBP inhibition profiles of 16 commercially available β-lactam antibiotics were evaluated in an unencapsulated derivative of the D39 strain of Streptococcus pneumoniae, IU1945. These β-lactams have not previously been characterized for their PBP inhibition profiles in S. pneumoniae and these data a

SUBMITTER: Sharan D 

PROVIDER: S-EPMC9115913 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature