Decreased sensitivity to polymyxin B in colicin K tolerant cells of Escherichia coli K-12 in the presence of colicin K

1973 ◽  
Vol 19 (3) ◽  
pp. 345-351 ◽  
Author(s):  
L. G. Mathieu ◽  
D. Legault-Hetu

Cells refractory to the lethal effect of colicin K were selected from a sensitive Escherichia coli K-12 strain. They could still be lysed by bacteriophage T6 which is thought to share with colicin K common receptor sites on the bacterial cell wall. Incubation of these cells for 30 min in a colicin K preparation considerably reduced its subsequent activity on the sensitive parent strain. When these tolerant cells were exposed to polymyxin B in the presence of colicin K, the lethal activity of the polymyxin was decreased significantly as compared with that exerted by the antibiotic in the absence of colicin K. In the colicin K sensitive wild strain, the combined lethal effect of the bacteriocin and of the antibiotic was not smaller than that of either inhibitor alone. Examination with the fluorescence microscope of cells stained with acridine orange showed that colicin K tolerant cells incubated with polymyxin B had undergone greater morphological changes than similar cells treated with polymyxin B in the presence of colicin K. Leakage of materials absorbing at 260 nm was greatest for the cells exposed to polymyxin B alone. The results suggest that in colicin K tolerant cells of E. coli derived from a sensitive strain, the bacteriocin might compete with polymyxin B for sites of attachment on the bacterial cell wall or mask some of the envelope phospholipids which are believed to react with polymyxin B.

2007 ◽  
Vol 190 (5) ◽  
pp. 1831-1834 ◽  
Author(s):  
Adeline Derouaux ◽  
Benoît Wolf ◽  
Claudine Fraipont ◽  
Eefjan Breukink ◽  
Martine Nguyen-Distèche ◽  
...  

ABSTRACT The monofunctional peptidoglycan glycosyltransferase (MtgA) catalyzes glycan chain elongation of the bacterial cell wall. Here we show that MtgA localizes at the division site of Escherichia coli cells that are deficient in PBP1b and produce a thermosensitive PBP1a and is able to interact with three constituents of the divisome, PBP3, FtsW, and FtsN, suggesting that MtgA may play a role in peptidoglycan assembly during the cell cycle in collaboration with other proteins.


1969 ◽  
Vol 25 (3) ◽  
pp. 331-332 ◽  
Author(s):  
V. Obdržálek ◽  
J. Šmarda ◽  
O. Čech ◽  
J. Adler

Author(s):  
Manfred E. Bayer

Bacterial viruses adsorb specifically to receptors on the host cell surface. Although the chemical composition of some of the cell wall receptors for bacteriophages of the T-series has been described and the number of receptor sites has been estimated to be 150 to 300 per E. coli cell, the localization of the sites on the bacterial wall has been unknown.When logarithmically growing cells of E. coli are transferred into a medium containing 20% sucrose, the cells plasmolize: the protoplast shrinks and becomes separated from the somewhat rigid cell wall. When these cells are fixed in 8% Formaldehyde, post-fixed in OsO4/uranyl acetate, embedded in Vestopal W, then cut in an ultramicrotome and observed with the electron microscope, the separation of protoplast and wall becomes clearly visible, (Fig. 1, 2). At a number of locations however, the protoplasmic membrane adheres to the wall even under the considerable pull of the shrinking protoplast. Thus numerous connecting bridges are maintained between protoplast and cell wall. Estimations of the total number of such wall/membrane associations yield a number of about 300 per cell.


2002 ◽  
Vol 22 (1-2) ◽  
pp. 209-222 ◽  
Author(s):  
Bénédicte Flambard

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