scholarly journals 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

2018 ◽  
Vol 11 (1) ◽  
Author(s):  
Idrissa Diawara ◽  
Kaotar Nayme ◽  
Khalid Katfy ◽  
Abouddihaj Barguigua ◽  
Mohamed Kettani-Halabi ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Amino Acid ◽  
Binding Proteins ◽  
Pediatric Patients ◽  
Amino Acid Motif ◽  
Penicillin Binding Proteins

scholarly journals Increasing Ceftriaxone Resistance and Multiple Alterations of Penicillin-Binding Proteins among Penicillin-Resistant Streptococcus pneumoniae Isolates in Taiwan

2007 ◽  
Vol 51 (9) ◽  
pp. 3404-3406 ◽  
Author(s):  
Cheng-Hsun Chiu ◽  
Lin-Hui Su ◽  
Yhu-Chering Huang ◽  
Jui-Chia Lai ◽  
Hsiu-Ling Chen ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Amino Acid ◽  
Binding Proteins ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Penicillin Binding Proteins

ABSTRACT The rate of nonsusceptibility of penicillin-resistant Streptococcus pneumoniae strains to ceftriaxone increased significantly in Taiwan in 2005. Approximately 90% of the ceftriaxone-nonsusceptible isolates were found to be of four major serotypes (serotypes 6B, 14, 19F, and 23F). Seven amino acid alterations in the penicillin-binding protein 2B transpeptidase-encoding region specifically contributed to the resistance.

scholarly journals Susceptibility of Methicillin-Resistant Staphylococcus aureus to Five Quinazolinone Antibacterials

2019 ◽  
Vol 64 (1) ◽  
Author(s):  
Sara Ceballos ◽  
Choon Kim ◽  
Yuanyuan Qian ◽  
Shahriar Mobashery ◽  
Mayland Chang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Binding Proteins ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Methicillin Resistant ◽  
Content Type ◽  
Penicillin Binding Proteins

ABSTRACT The in vitro activities of five quinazolinone antibacterials, compounds Q1 to Q5, were tested against 210 strains of methicillin-resistant Staphylococcus aureus (MRSA). The MIC50/MIC90 values (in μg/ml) were as follows: Q1, 0.5/2; Q2, 1/4; Q3, 2/4; Q4, 0.06/0.25; and Q5, 0.125/0.5. Several strains with high MIC values (from 8 to >32 μg/ml) for some of these compounds exhibited amino acid changes in the penicillin-binding proteins, which are targeted by these antibacterials.

scholarly journals Capsule Homology Does Not Increase the Frequency of Transformation of Linked Penicillin Binding Proteins PBP 1a and PBP 2x in Streptococcus pneumoniae

2005 ◽  
Vol 49 (4) ◽  
pp. 1591-1592 ◽  
Author(s):  
Krzysztof Trzciński ◽  
Adam MacNeil ◽  
Keith P. Klugman ◽  
Marc Lipsitch
Keyword(s):  
Streptococcus Pneumoniae ◽  
Binding Proteins ◽  
Penicillin Resistance ◽  
Penicillin Binding Proteins ◽  
Transformation Rates

ABSTRACT Penicillin resistance is mainly confined to a limited number of Streptococcus pneumoniae serotypes. Given linkage between the capsular biosynthesis locus and two penicillin binding proteins, we tested whether capsule homology increases transformation rates of penicillin resistance. Transformation rates in homologous donor-recipient pairs were no higher than expected, falsifying this hypothesis.

High Prevalence of Streptococcus pneumoniae with Mutations in pbp1a, pbp2x, and pbp2b Genes of Penicillin-Binding Proteins in the Nasopharynx in Children in Japan

ORL ◽  
2006 ◽  
Vol 68 (3) ◽  
pp. 139-145 ◽  
Author(s):  
Muneki Hotomi ◽  
Dewan S. Billal ◽  
Jun Shimada ◽  
Masaki Suzumoto ◽  
Kazuma Yamauchi ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Binding Proteins ◽  
Penicillin Binding Proteins ◽  
High Prevalence

scholarly journals Diversity of Substitutions within or Adjacent to Conserved Amino Acid Motifs of Penicillin-Binding Protein 2X in Cephalosporin-Resistant Streptococcus pneumoniaeIsolates

1999 ◽  
Vol 43 (5) ◽  
pp. 1252-1255 ◽  
Author(s):  
Yasuko Asahi ◽  
Yasuo Takeuchi ◽  
Kimiko Ubukata
Keyword(s):  
Streptococcus Pneumoniae ◽  
Amino Acid ◽  
Three Dimensional ◽  
Crystallographic Structure ◽  
Amino Acid Substitutions ◽  
Penicillin Binding Protein ◽  
Amino Acid Motif ◽  
Dna Fragment ◽  
High Level ◽  
Level Resistance

ABSTRACT The sequence of an approximately 1.1-kb DNA fragment of thepbp2x gene, which encodes the transpeptidase domain, was determined for 35 clinical isolates of Streptococcus pneumoniae for which the cefotaxime (CTX) MICs varied. Strains with substitutions within a conserved amino acid motif changing STMK to SAFK and a Leu-to-Val change just before the KSG motif were highly resistant to CTX (MIC, ≧2 μg/ml). Strains with substitutions adjacent to SSN or KSG motifs had low-level resistance. The amino acid substitutions were plotted on the three-dimensional crystallographic structure of the transpeptidase domain of PBP2X. Transformants containing pbp2x from strains with high-level CTX resistance increased the CTX MIC from 0.016 μg/ml to 0.5 to 1.0 μg/ml.

Molecular characteristics of penicillin-binding protein 2b, 2x, and 1a sequences in penicillin-nonsusceptible Streptococcus pneumoniae isolates in Shenyang, China

2008 ◽  
Vol 54 (6) ◽  
pp. 489-494 ◽  
Author(s):  
Su Fei Tian ◽  
Yun Zhuo Chu ◽  
Bai Yi Chen
Keyword(s):  
Streptococcus Pneumoniae ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Dna Sequences ◽  
Multilocus Sequence Typing ◽  
Molecular Characteristics ◽  
Penicillin Binding Protein ◽  
Genetic Changes ◽  
Penicillin Binding Proteins ◽  
Amino Acid Profiles

The aim of this sudy was to investigate the nature of the amino acid motifs found in penicillin-binding proteins (PBP) 2b, 2x, and 1a of penicillin-nonsusceptible Streptococcus pneumoniae isolates from Shenyang, China, and to obtain information regarding the prevalence of alterations within the motifs or in positions flanking the motifs. For 18 clinical isolates comprising 4 penicillin-susceptible S. pneumoniae, 5 penicillin-intermediate S. pneumoniae, and 9 penicillin-resistant S. pneumoniae. the DNA sequences of PBP2b, PBP2x, and PBP1a transpeptidase domains were determined and then genotyped by multilocus sequence typing. Sequence analysis revealed that most penicillin-nonsusceptible S. pneumoniae isolates (penicillin MIC ≥ 1.5 μg/mL and cefotaxime MIC ≥ 2 μg/mL) shared identical PBP2b, PBP2x, and PBP1a amino acid profiles. Most penicillin-resistant S. pneumoniae isolates were ST320 (4-16-19-15-6-20-1), the double-locus variant of the Taiwan19F-14 clone. This study will serve as a basis for future monitoring of genetic changes associated with the emergence and spread of β-lactam resistance in Shenyang, China.

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