Literature DB >> 22457311

The 2011 Garrod Lecture: From penicillin-binding proteins to molecular epidemiology.

Brian G Spratt1.   

Abstract

In this review, based on my Garrod Lecture to the British Society for Antimicrobial Chemotherapy, I have given a brief outline of my career over the past 40 years, starting with research in the 1970s into the properties and functions of penicillin-binding proteins (PBPs), leading to the identification of the high molecular mass PBPs as the physiological targets of penicillin, and subsequent studies showing the emergence of low-affinity PBPs in penicillin-resistant clinical isolates by inter-species recombination and the generation of mosaic PBP genes. The studies of clinical isolates of gonococci, meningococci and pneumococci with PBP-mediated resistance to penicillin led to new interests in molecular epidemiology and the population and evolutionary biology of bacterial pathogens. The development (with colleagues) of multilocus sequence typing provided a method for the unambiguous characterization of bacterial strains that has proved to be very widely used, but the recent remarkable (and ongoing) developments in DNA sequencing technologies have provided the prospect of being able routinely to use whole genome sequences to characterize pathogen isolates. These developments will soon have major implications for diagnostic microbiology, outbreak investigations and our ability to follow the spread of strains of community-acquired and nosocomial pathogens at local, national and international levels. However, there are major barriers to be overcome, particularly with respect to how the avalanche of genome sequence data will be stored so that its transformative potential for molecular epidemiology and international public health are fully realized.

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Year:  2012        PMID: 22457311      PMCID: PMC3370820          DOI: 10.1093/jac/dks109

Source DB:  PubMed          Journal:  J Antimicrob Chemother        ISSN: 0305-7453            Impact factor:   5.790


  37 in total

1.  Penicillin-binding proteins and cell shape in E. coli.

Authors:  B G Spratt; A B Pardee
Journal:  Nature       Date:  1975-04-10       Impact factor: 49.962

2.  Database-driven multi locus sequence typing (MLST) of bacterial pathogens.

Authors:  M S Chan; M C Maiden; B G Spratt
Journal:  Bioinformatics       Date:  2001-11       Impact factor: 6.937

3.  Rapid sequence-based identification of gonococcal transmission clusters in a large metropolitan area.

Authors:  Iona M C Martin; Catherine A Ison; David M Aanensen; Kevin A Fenton; Brian G Spratt
Journal:  J Infect Dis       Date:  2004-03-31       Impact factor: 5.226

4.  The relative contributions of recombination and mutation to the divergence of clones of Neisseria meningitidis.

Authors:  E J Feil; M C Maiden; M Achtman; B G Spratt
Journal:  Mol Biol Evol       Date:  1999-11       Impact factor: 16.240

5.  Escherichia coli resistance to beta-lactam antibiotics through a decrease in the affinity of a target for lethality.

Authors:  B G Spratt
Journal:  Nature       Date:  1978-08-17       Impact factor: 49.962

6.  Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12.

Authors:  B G Spratt
Journal:  Proc Natl Acad Sci U S A       Date:  1975-08       Impact factor: 11.205

7.  Covalent affinity chromatography of penicillin-binding components from bacterial membranes.

Authors:  P M Blumberg; J L Strominger
Journal:  Methods Enzymol       Date:  1974       Impact factor: 1.600

8.  Penicillin-binding proteins of multiply antibiotic-resistant South African strains of Streptococcus pneumoniae.

Authors:  S Zighelboim; A Tomasz
Journal:  Antimicrob Agents Chemother       Date:  1980-03       Impact factor: 5.191

9.  Temperature-sensitive cell division mutants of Escherichia coli with thermolabile penicillin-binding proteins.

Authors:  B G Spratt
Journal:  J Bacteriol       Date:  1977-07       Impact factor: 3.490

10.  Multiple changes of penicillin-binding proteins in penicillin-resistant clinical isolates of Streptococcus pneumoniae.

Authors:  R Hakenbeck; M Tarpay; A Tomasz
Journal:  Antimicrob Agents Chemother       Date:  1980-03       Impact factor: 5.191

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  6 in total

Review 1.  Constructing and deconstructing the bacterial cell wall.

Authors:  Jed F Fisher; Shahriar Mobashery
Journal:  Protein Sci       Date:  2019-11-20       Impact factor: 6.725

2.  Neutral β-Lactams Inactivate High Molecular Mass Penicillin-Binding Proteins of Class B1, Including PBP2a of MRSA.

Authors:  Kinjal Dave; Timothy Palzkill; R F Pratt
Journal:  ACS Med Chem Lett       Date:  2013-12-16       Impact factor: 4.345

Review 3.  Penicillin-binding proteins in Actinobacteria.

Authors:  Hiroshi Ogawara
Journal:  J Antibiot (Tokyo)       Date:  2014-10-29       Impact factor: 2.649

Review 4.  β-Lactam Resistance Mechanisms: Gram-Positive Bacteria and Mycobacterium tuberculosis.

Authors:  Jed F Fisher; Shahriar Mobashery
Journal:  Cold Spring Harb Perspect Med       Date:  2016-05-02       Impact factor: 6.915

5.  Human Streptococcus agalactiae strains in aquatic mammals and fish.

Authors:  Christian M J Delannoy; Margaret Crumlish; Michael C Fontaine; Jolinda Pollock; Geoff Foster; Mark P Dagleish; James F Turnbull; Ruth N Zadoks
Journal:  BMC Microbiol       Date:  2013-02-18       Impact factor: 3.605

6.  Biochemical and Structural Analysis of a Novel Esterase from Caulobacter crescentus related to Penicillin-Binding Protein (PBP).

Authors:  Bum Han Ryu; Tri Duc Ngo; Wanki Yoo; Sojeong Lee; Boo-Young Kim; Euijoo Lee; Kyeong Kyu Kim; T Doohun Kim
Journal:  Sci Rep       Date:  2016-12-01       Impact factor: 4.379

  6 in total

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