2018
DOI: 10.1002/iub.1761
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β‐lactam resistance: The role of low molecular weight penicillin binding proteins, β‐lactamases and ld‐transpeptidases in bacteria associated with respiratory tract infections

Abstract: Disruption of peptidoglycan (PG) biosynthesis in the bacterial cell wall by β-lactam antibiotics has transformed therapeutic options for bacterial infections. These antibiotics target the transpeptidase domains in penicillin binding proteins (PBPs), which can be classified into high and low molecular weight (LMW) counterparts. While the essentiality of the former has been extensively demonstrated, the physiological roles of LMW PBPs remain poorly understood. Herein, we review the function of LMW PBPs, β-lactam… Show more

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Cited by 11 publications
(10 citation statements)
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References 136 publications
(177 reference statements)
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“…Deletion of dacC decreased resistance to ampicillin. There are other examples where loss of a peptidoglycan carboxypeptidase leads to increased β-lactam resistance ( 38 40 ). In some of these cases, it appears to cause a shift to 3-3 cross-linking of the peptide side chains of peptidoglycan, which is carried out by Ldts.…”
Section: Discussionmentioning
confidence: 99%
“…Deletion of dacC decreased resistance to ampicillin. There are other examples where loss of a peptidoglycan carboxypeptidase leads to increased β-lactam resistance ( 38 40 ). In some of these cases, it appears to cause a shift to 3-3 cross-linking of the peptide side chains of peptidoglycan, which is carried out by Ldts.…”
Section: Discussionmentioning
confidence: 99%
“…Despite ongoing research, a clear correlation between certain PBP modifications (such as PBP5 or PBP7) and the emergence of a frank BL resistance has not been established. This suggests that PBPs are part of a more complex system influencing antibiotic resistance [74,78].…”
Section: Penicillin-binding Protein Mutationsmentioning
confidence: 99%
“…This gene is closely located to other unique genes: a gene with unknown function (HRE58_12725) and two transposase genes (HRE58_12730, HRE58_12735), flanked by a perfect 26-bp inverted repeat (IR) sequence, supporting their acquisition by horizontal gene transfer (Supplementary figure 2). LMW-PBPs are important enzymes involved in cell-wall recycling and considered the major molecular targets for β-lactam antibiotics [47]. Alterations in the structure of LMW-PBPs are associated with reduced susceptibility to penicillin and other β-lactams and can induce the expression of β-lactamases [47][48][49].…”
Section: Pangenome Analysismentioning
confidence: 99%
“…LMW-PBPs are important enzymes involved in cell-wall recycling and considered the major molecular targets for β-lactam antibiotics [47]. Alterations in the structure of LMW-PBPs are associated with reduced susceptibility to penicillin and other β-lactams and can induce the expression of β-lactamases [47][48][49]. The presence of an LMW-PBP composite transposon likely confers a competitive advantage for S. maltophilia UENF-4GII to thrive in microbial communities containing penicillin.…”
Section: Pangenome Analysismentioning
confidence: 99%