A novel PBP3 substitution in Haemophilus influenzae confers reduced aminopenicillin susceptibility.

ABSTRACT:

Background

Identification and characterization of non-typeable Haemophilus influenzae (NTHi) with reduced susceptibility to β-lactam antibiotics due to mutations in penicillin binding protein 3 (PBP3) is a clinical challenge. We analyzed a blood isolate, NTHi93-57485, that was categorized as aminopenicillin resistant but lacked key amino acid substitutions in PBP3 that have previously been associated with reduced aminopenicillin susceptibility. The significance of an alternative amino acid substitution (Y528H) in this isolate was examined.

Results

Site-directed mutagenesis of a β-lactam susceptible H. influenzae (NTHi3655) was performed to introduce the Y528H substitution into wild-type ftsI (encoding for PBP3). Disc diffusion screening and broth microdilution determination

SUBMITTER: Thegerstrom J 

PROVIDER: S-EPMC5984330 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature