Penicillin binding proteins of Vibriocholerae

Sengupta, Tapas K.; Chatterjee, Anadi N.; Das, Jyotirmoy

doi:10.1016/0006-291x(90)90808-z

Cited by 5 publications

(9 citation statements)

References 13 publications

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“…Eleven penicillin-binding proteins (PBPs) were detected in V. cholerae, and when they were compared with the PBPs of Eschenichia coli, several interesting differences were observed (23). The present report is an extension of the previous report (23) and describes several novel features in the interaction of betalactam antibiotics with V. cholerae.…”

mentioning

confidence: 59%

“…There was no significant difference between the kinetics of binding of PenX to PBPs of the resistant cells and that of the parental cells, indicating that the affinities of the PBPs of the resistant cells for PenX were similar to those of the parental cells (23). However, there was a significant difference between the resistant and wild-type cells in release of bound PenX from the low-molecular-weight PBPs (Fig.…”

Section: Methodsmentioning

confidence: 91%

“…While PBP 7 accounted for about 40% of the total radioactivity among the PBPs of wild-type cells (23), in resistant cells this PBP was present in a much smaller amount. Moreover, PBPs 2 and 3 were also present in smaller amounts in resistant cells than in wild-type cells.…”

Section: Methodsmentioning

confidence: 93%

“…To investigate whether the resistance to beta-lactam antibiotics was due to alteration in the penicillin-sensitive enzymes, the PBPs of the resistant cells were compared with those of the parental cells. Crude cell envelope fractions of both the parental and resistant cells were labeled with '25I-PenX and analyzed by SDS-PAGE and autoradiography (23). All 11 PBPs reported for the wild-type cells (23) could also be detected in the PenG-resistant cells and had molecular masses ranging from 22 to 97 kDa (Fig.…”

Section: Methodsmentioning

confidence: 99%

“…The PBPs of V. cholerae cells have been described elsewhere (23). To investigate whether the resistance to beta-lactam antibiotics was due to alteration in the penicillin-sensitive enzymes, the PBPs of the resistant cells were compared with those of the parental cells.…”

Section: Methodsmentioning

confidence: 99%

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Interaction of Vibrio cholerae cells with beta-lactam antibiotics: emergence of resistant cells at a high frequency

Sengupta

Chaudhuri

Majumdar

et al. 1992

Antimicrob Agents Chemother

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Unlike other gram-negative enteric bacteria, Vibrio cholerae cells were equally susceptible to penicillin and ampicillin and in general more susceptible than Escherichia coli to most of the beta-lactam antibiotics. The turbidity of penicillin-treated cultures continued to increase exponentially for about 3 h, although the cell viability declined rapidly within 30 min of penicillin addition. Prolonged treatment with beta-lactam antibiotics produced cells resistant to these antibiotics. A fluctuation test indicated that this resistance might be due to adaptive mutation. Cells resistant to a beta-lactam exhibited broad cross-resistance to other beta-lactam antibiotics. A new 12,000-Da outer membrane protein was detected both in beta-lactam-resistant cells and in wild-type cells growing in medium containing beta-lactam antibiotics. While the penicillin-resistant cells had all of the penicillin-binding proteins (PBPs) present in the parental cells, significant differences in the relative proportion of low-molecular-weight PBPs were seen. The low-molecular-weight PBPs from resistant cells seemed to form more stable complexes with penicillin than those from the parental strain.Vibrio cholerae, a noninvasive enteropathogen and the etiological agent of cholera, adheres to epithelial cells of the proximal small intestine and excretes a potent enterotoxin which causes severe diarrhea. Several models simulating the important features of the interaction between the bacterium and the epithelial surface have been proposed (8,11,15,26). The outer membrane of enteric gram-negative bacteria plays an important role in conferring resistance to bile salts and to host defense factors such as lysozyme and leukocyte proteins (19). Studies of the cell surface architecture of V. cholerae were thus considered necessary for a better understanding of the cell-cell interaction. It has recently been reported that the cell surface of a hypertoxinogenic strain of V. cholerae, 569B, has exposed phospholipids in the outer leaflet of the outer membrane and that these cells are highly sensitive to a wide range of chemicals in general and to hydrophobic compounds and neutral and anionic detergents in particular. The lipopolysaccharide (LPS) moiety has relatively less negative charge (21).Previous studies have indicated the relatively fragile nature of the murein network of V. cholerae (12, 13). These cells lyse rapidly in hypotonic media and in the presence of chelating agents such as Tris and EDTA (13). Purified outer membranes can be directly isolated from whole cells by treatment with protein denaturants such as urea at room temperature (12).These observations suggest that the murein network of V. cholerae is relatively weak and prompted us to examine the effect of beta-lactam antibiotics which inhibit the final stages of murein synthesis in V. cholerae. Eleven penicillin-binding proteins (PBPs) were detected in V. cholerae, and when they were compared with the PBPs of Eschenichia coli, several interesting differences were observed (23). The pres...

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mentioning

confidence: 59%

Section: Methodsmentioning

confidence: 91%

Section: Methodsmentioning

confidence: 93%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

Interaction of Vibrio cholerae cells with beta-lactam antibiotics: emergence of resistant cells at a high frequency

Sengupta

Chaudhuri

Majumdar

et al. 1992

Antimicrob Agents Chemother

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A Periplasmic Polymer Curves Vibrio cholerae and Promotes Pathogenesis

Bartlett

Bratton

Duvshani

et al. 2017

Cell

124

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Summary Pathogenic Vibrio cholerae remains a major human health concern. V. cholerae has a characteristic curved rod morphology, with a longer outer face and a shorter inner face. Previously, the mechanism and function of this curvature were unknown. Here we identify and characterize CrvA, the first curvature determinant in V. cholerae. CrvA self-assembles into filaments at the inner face of cell curvature. Unlike traditional cytoskeletons, CrvA localizes to the periplasm, and thus could be considered a periskeletal element. To quantify how curvature forms, we developed QuASAR (Quantitative Analysis of Sacculus Architecture Remodeling), which measures subcellular peptidoglycan dynamics. QuASAR reveals that CrvA asymmetrically patterns peptidoglycan insertion rather than removal, causing more material insertion into the outer face than the inner face. Furthermore, crvA is quorum regulated and CrvA-dependent curvature increases at high cell density. Finally, we demonstrate that CrvA promotes motility in hydrogels and confers an advantage in host colonization and pathogenesis.

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A 25-kDa β-Lactam-induced Outer Membrane Protein of Vibrio cholerae

Deb

Bhattacharyya

Das

1995

Journal of Biological Chemistry

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A 25-kDa outer membrane protein, induced following treatment of Vibrio cholerae cells with beta-lactam antibiotics and constituting about 8-10% of the total outer membrane proteins of beta-lactam-resistant mutants, has been purified to homogeneity. It is a basic (pI 8.5) protein rich in beta-sheet structure and is a homodimer, the monomers being held together by hydrophobic interactions. The effective hydrophobicity of the protein is low, and a large part of the protein is exposed on the surface of the outer membrane. The protein does not have beta-lactamase or autolytic activity and is not a penicillin-binding protein. The Stoke's radius of the 25-kDa protein (26 A) is comparable to the pore size of the V. cholerae OmpF-like porin. Proteoliposome swelling assay showed that the 25-kDa protein might block the pores of OmpF through which beta-lactam antibiotics normally enter the cells. Twenty-two amino acid residues from the N-terminal end of the 25-kDa protein have been sequenced, and a 32-mer oligonucleotide probe was synthesized using the amino acid residues 2-12. This probe was used to identify the gene encoding the 25-kDa protein. The beta-lactam-resistant cells are insensitive to changes in the osmolarity of the growth medium in contrast to the wild type cells which exhibit osmoregulation of OmpF and OmpC synthesis. All beta-lactam-resistant mutants examined are resistant to novobiocin.

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Penicillin binding proteins of Vibriocholerae

Cited by 5 publications

References 13 publications

Interaction of Vibrio cholerae cells with beta-lactam antibiotics: emergence of resistant cells at a high frequency

Interaction of Vibrio cholerae cells with beta-lactam antibiotics: emergence of resistant cells at a high frequency

A Periplasmic Polymer Curves Vibrio cholerae and Promotes Pathogenesis

A 25-kDa β-Lactam-induced Outer Membrane Protein of Vibrio cholerae

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