Analysis of amino acid motif of penicillin-binding proteins 1a, 2b, and 2x in invasive Streptococcus pneumoniae nonsusceptible to penicillin isolated from pediatric patients in Casablanca, Morocco

• Main Authors: Idrissa Diawara, Kaotar Nayme, Khalid Katfy, Abouddihaj Barguigua, Mohamed Kettani-Halabi, Houria Belabbes, Mohammed Timinouni, Khalid Zerouali, Naima Elmdaghri
• Format: Article
• Language: English
• Published: BMC 2018-08-01
• Series: BMC Research Notes
• Subjects: Streptococcus pneumoniae; Penicillin-binding proteins; β-lactams; Serotypes; Penicillin resistance; pbp gene
• Online Access: http://link.springer.com/article/10.1186/s13104-018-3719-5
• ISSN: 1756-0500

Abstract Objectives This study aimed to investigate the nature of the amino acid motifs found in PBPs of Streptococcus pneumoniae isolates in invasive diseases from pediatric patients at Casablanca, Morocco. Five penicillin-susceptible (PSSP), ten penicillin-intermediate (PISP), and fifteen penicillin-resistant S. pneumoniae (PRSP) were studied by PCR–RFLP and DNA sequencing of the pbp1a, − 2b, and − 2x genes. Results There were no changes in the conserved motifs of PBP1a, PBP2b and PBP2x for PSSP strains. Substitution close to PBP1a conserved motifs were found in all PRSP isolates and six/five PISP. Analysis of PBP2b showed that all but one of the 10 PISP strains and all PRSP had substitutions. Substitution close to PBP2x motifs showed that all but three of the 10 PISP strains and all PRSP had substitutions in tow conserved motifs. A total of 6, 11 and 10 genotypes were found after analysis of pbp1a, pbp2b, and pbp2x, respectively. The penicillin-nonsusceptible S. pneumoniae isolated in Casablanca share most amino acid substitutions of those reported worldwide, but they occurred among pneumococci with low level resistance to b-lactams.