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

Spratt, Brian G.

doi:10.1073/pnas.72.8.2999

Cited by 863 publications

(812 citation statements)

References 19 publications

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“…When added to a wild-type E. coli culture, the cells become spherical (Lund and Tybring, 1972), and, although the optical density increases for many generations, cell division stops rather quickly, at least in rich medium (Vinella et al, 1993). The loss of rod shape in the presence of mecillinam implies that PBP2 is required for lateral elongation of the peptidoglycan cell wall (Spratt, 1975). The cell division block was interpreted as a regulatory effect because certain mutants are able to grow and divide on plates and in liquid culture in the complete absence of PBP2 (Ogura et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli

Navarro

Robin

D’Ari

et al. 1998

Molecular Microbiology

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Section: Introductionmentioning

confidence: 99%

Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli

Navarro

Robin

D’Ari

et al. 1998

Molecular Microbiology

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“…Mecillinam is a p-lactam antibiotic which, by binding specifically to PBP2 and by specific inhibition of lateral wall elongation (Spratt, 1975;Satta e t al., 1981), transforms Gram-negative rods into cocci, which are incapable of further division [see also Fig. lb, parent strain GC27001.…”

Section: Effect Of Mecillinam On E Coli Strains Carrying the Lov Mutmentioning

confidence: 99%

“…More recently, D'Ari and co-workers (Bouloc e t al., 1988(Bouloc e t al., , 1989 (Spratt, 1975; Satta e t a/., l781)], cells become cocci which then continue to divide. The lov-I mutation (also known as argS20I) is located in the argJ gene; it affects tRNA synthetase and confers mecillinam resistance (Bouloc e t al., 1787).…”

Section: Introductionmentioning

confidence: 99%

Modified peptidoglycan chemical composition in shape-altered Escherichia coli

Signoretto

Stefano²,

Canepari³

1996

Microbiology

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Peptidoglycan synthesis and its fine chemical composition were studied in dividing cocci of Escherichia coli carrying the low1 mutation and in which the coccal shape was obtained either by mecillinam treatment or by transferring a pbpA mutation (penicillin-binding protein 2-phenotype), as compared to normal rods and non-dividing cocci. Synchronously dividing cocci showed peptidoglycan synthesis only in the cell cycle phase corresponding to cell septation. During the phase corresponding to lateral wall elongation, peptidoglycan synthesis was strongly reduced. This type of synthesis suggests that the dividing cocci consisted only of the two poles. Analysis of the muropeptide composition revealed a specific fourfold increase in the tetratetra-tetra trimer in dividing cocci as compared to non-dividing cocci or parental rods. We postulate that, in E. coli, the chemical composition of septa1 peptidoglycan differs from that of lateral wall peptidoglycan.

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“…In the last few decades, research on P-lactam antibiotics has concentrated mainly on identification of their molecular targets (26,27,33). However, antibacterial effects in vivo may also be due in part to other changes associated with the cell surface and to reduction in the synthesis of virulence factors.…”

mentioning

confidence: 99%

Protein antigens of encapsulated Klebsiella pneumoniae surface exposed after growth in the presence of subinhibitory concentrations of cephalosporins

Kadurugamuwa¹,

Anwar²,

Brown³

et al. 1985

Antimicrob Agents Chemother

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It recently has been reported by us that cephalosporins, at a concentration below that influencing growth rate, reduced the prQduction of enterochelin and capsule formation of iron-depleted Klejsiella pneumoniae. We now report on the antigenicity of the outer membrane components and surface-exposed protein antigens of iron-depleted cells grown in the presencp or absence of cephalosporins. All major outer membrane proteins, including iron-regulated membrane proteins, were immunogenic. Encapsulated K. pneumoniae grown in antibiotic-free media had three protein antigens (60, 35.5, and 32.5 kilodaltons) exposed on the surface that were accessible to antibodies. Growth of the same cultures in the presence of subinhibitory concentrations of cephalosporins resulted in the exposure of a greater number of protein antigenic determinants, including iron-regulated membrane proteins, which become readily accessible to antibodies. It was also found that immunoblotting was generally more sensitive than conventional staining of the acrylamide gel with Coomnassie blue in the detection of proteins.

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

Cited by 863 publications

References 19 publications

Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli

Analysis of the effect of ppGpp on the ftsQAZ operon in Escherichia coli

Modified peptidoglycan chemical composition in shape-altered Escherichia coli

Protein antigens of encapsulated Klebsiella pneumoniae surface exposed after growth in the presence of subinhibitory concentrations of cephalosporins

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