Literature DB >> 22483632

Computational analysis of structure-based interactions and ligand properties can predict efflux effects on antibiotics.

Aurijit Sarkar1, Kelcey C Anderson, Glen E Kellogg.   

Abstract

AcrA-AcrB-TolC efflux pumps extrude drugs of multiple classes from bacterial cells and are a leading cause for antimicrobial resistance. Thus, they are of paramount interest to those engaged in antibiotic discovery. Accurate prediction of antibiotic efflux has been elusive, despite several studies aimed at this purpose. Minimum inhibitory concentration (MIC) ratios of 32 β-lactam antibiotics were collected from literature. 3-Dimensional Quantitative Structure-Activity Relationship on the β-lactam antibiotic structures revealed seemingly predictive models (q(2)=0.53), but the lack of a general superposition rule does not allow its use on antibiotics that lack the β-lactam moiety. Since MIC ratios must depend on interactions of antibiotics with lipid membranes and transport proteins during influx, capture and extrusion of antibiotics from the bacterial cell, descriptors representing these factors were calculated and used in building mathematical models that quantitatively classify antibiotics as having high/low efflux (>93% accuracy). Our models provide preliminary evidence that it is possible to predict the effects of antibiotic efflux if the passage of antibiotics into, and out of, bacterial cells is taken into account--something descriptor and field-based QSAR models cannot do. While the paucity of data in the public domain remains the limiting factor in such studies, these models show significant improvements in predictions over simple LogP-based regression models and should pave the path toward further work in this field. This method should also be extensible to other pharmacologically and biologically relevant transport proteins.
Copyright © 2012 Elsevier Masson SAS. All rights reserved.

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Year:  2012        PMID: 22483632      PMCID: PMC3340532          DOI: 10.1016/j.ejmech.2012.03.008

Source DB:  PubMed          Journal:  Eur J Med Chem        ISSN: 0223-5234            Impact factor:   6.514


  58 in total

1.  Contributions of the AmpC beta-lactamase and the AcrAB multidrug efflux system in intrinsic resistance of Escherichia coli K-12 to beta-lactams.

Authors:  A Mazzariol; G Cornaglia; H Nikaido
Journal:  Antimicrob Agents Chemother       Date:  2000-05       Impact factor: 5.191

2.  Paramyxovirus receptor-binding molecules: engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site.

Authors:  Matteo Porotto; Micaela Fornabaio; Olga Greengard; Matthew T Murrell; Glen E Kellogg; Anne Moscona
Journal:  J Virol       Date:  2006-02       Impact factor: 5.103

3.  Intrinsic resistance of Escherichia coli to mureidomycin A and C due to expression of the multidrug efflux system AcrAB-TolC: comparison with the efflux systems of mureidomycin-susceptible Pseudomonas aeruginosa.

Authors:  Naomasa Gotoh; Takeshi Murata; Toru Ozaki; Tadashi Kimura; Akiko Kondo; Takeshi Nishino
Journal:  J Infect Chemother       Date:  2003-03       Impact factor: 2.211

Review 4.  Antibiotic efflux pumps.

Authors:  F Van Bambeke; E Balzi; P M Tulkens
Journal:  Biochem Pharmacol       Date:  2000-08-15       Impact factor: 5.858

5.  A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study.

Authors:  Edward W Yu; Julio R Aires; Gerry McDermott; Hiroshi Nikaido
Journal:  J Bacteriol       Date:  2005-10       Impact factor: 3.490

6.  Molecular graphics approach to bacterial AcrB protein-beta-lactam antibiotic molecular recognition in drug efflux mechanism.

Authors:  Rudolf Kiralj; Márcia M C Ferreira
Journal:  J Mol Graph Model       Date:  2006-01-06       Impact factor: 2.518

7.  Roles of TolC-dependent multidrug transporters of Escherichia coli in resistance to beta-lactams.

Authors:  Kunihiko Nishino; Junko Yamada; Hidetada Hirakawa; Takahiro Hirata; Akihito Yamaguchi
Journal:  Antimicrob Agents Chemother       Date:  2003-09       Impact factor: 5.191

8.  Overexpression of marA, soxS, or acrAB produces resistance to triclosan in laboratory and clinical strains of Escherichia coli.

Authors:  L M McMurry; M Oethinger; S B Levy
Journal:  FEMS Microbiol Lett       Date:  1998-09-15       Impact factor: 2.742

9.  Genes acrA and acrB encode a stress-induced efflux system of Escherichia coli.

Authors:  D Ma; D N Cook; M Alberti; N G Pon; H Nikaido; J E Hearst
Journal:  Mol Microbiol       Date:  1995-04       Impact factor: 3.501

10.  CmeABC functions as a multidrug efflux system in Campylobacter jejuni.

Authors:  Jun Lin; Linda Overbye Michel; Qijing Zhang
Journal:  Antimicrob Agents Chemother       Date:  2002-07       Impact factor: 5.191

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  1 in total

1.  How to deal with low-resolution target structures: using SAR, ensemble docking, hydropathic analysis, and 3D-QSAR to definitively map the αβ-tubulin colchicine site.

Authors:  Chenxiao Da; Susan L Mooberry; John T Gupton; Glen E Kellogg
Journal:  J Med Chem       Date:  2013-09-09       Impact factor: 7.446

  1 in total

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