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Hfq mutation confers increased cephalosporin resistance in Klebsiella pneumoniae [PDF]
Archives of Biological Sciences, 2017 Klebsiella pneumoniae (K. pneumoniae), is an opportunistic pathogen raising significant public health concerns owing to its multi-drug resistance. Hfq, one of the main RNA-binding proteins, is a key post-transcriptional regulator.
Li Xinran +7 more
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Penicillin-binding proteins in Actinobacteria [PDF]
The Journal of Antibiotics, 2014 Because some Actinobacteria, especially Streptomyces species, are β-lactam-producing bacteria, they have to have some self-resistant mechanism. The β-lactam biosynthetic gene clusters include genes for β-lactamases and penicillin-binding proteins (PBPs), suggesting that these are involved in self-resistance. However, direct evidence for the involvement
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Penicillin‐Binding Protein Imaging Probes [PDF]
Current Protocols in Chemical Biology, 2013 ABSTRACTPenicillin‐binding proteins (PBPs) are membrane‐associated proteins involved in the biosynthesis of peptidoglycan (PG), the main component of bacterial cell walls. These proteins were discovered and named for their affinity to bind the β‐lactam antibiotic penicillin.
Ozden, Kocaoglu, Erin E, Carlson
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mSphere, 2019 Penicillin-binding proteins (PBPs) are essential for bacterial cell wall biosynthesis, and several are clinically validated antibacterial targets of β-lactam antibiotics.
Srijan Ranjitkar +6 more
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Affinity of cefoperazone for penicillin-binding proteins [PDF]
Antimicrobial Agents and Chemotherapy, 1980 Cefoperazone (T-1551, CFP) a new semisynthetic cephalosporin, has a broad spectrum of antibacterial activity. We investigated the affinity of CFP to penicillin-binding proteins (PBPs) and the inhibition of peptidoglycan synthesis by CFP. CFP had high affinities for Escherichia coli PBP-3, -1Bs, -2, and -1A, in descending order, and low affinities for ...
N, Matsubara +4 more
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Emerging Infectious Diseases, 2003 Streptococcus pneumoniae and Neisseria meningitidis have very similar mechanisms of resistance to penicillin G. Although penicillin resistance is now common in S. pneumoniae, it is still rare in N. meningitidis.
L. Temime +3 more
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Resistance to β-lactam antibiotics conferred by point mutations in penicillin-binding proteins PBP3, PBP4 and PBP6 in Salmonella enterica. [PDF]
PLoS ONE, 2014 Penicillin-binding proteins (PBPs) are enzymes responsible for the polymerization of the glycan strand and the cross-linking between glycan chains as well as the target proteins for β-lactam antibiotics.
Song Sun, Maria Selmer, Dan I Andersson
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Penicillin-binding proteins in Borrelia burgdorferi [PDF]
Journal of Bacteriology, 1990 Penicillin-binding proteins were identified in Borrelia burgdorferi membranes. A 94-kilodalton penicillin-binding protein was the first to be labeled with tritiated penicillin and was the first band to disappear in a competition experiment. Its binding ability was destroyed when membranes were preboiled. In addition, several of these penicillin-binding
C, Urban +4 more
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Journal of BacteriologyThe aminoacyltransferase MurM is an important penicillin resistance determinant in Streptococcus pneumoniae. This enzyme attaches a serine or alanine to the side chain of lysine, the third residue of the pentapeptide of lipid II, resulting in branched ...
Ragnhild Sødal Gjennestad +7 more
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Antibiotics, 2021 Peptidoglycan (PG) is essential for bacterial survival and maintaining cell shape. The rod-shaped model bacterium Escherichia coli has a set of seven endopeptidases that remodel the PG during cell growth.
Jinglan Wang +4 more
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