Effect of switching time scale of receptor activity on chemotactic performance of Escherichia coli

Author(s):  
Shobhan Dev Mandal ◽  
Sakuntala Chatterjee
1954 ◽  
Vol 9 (6) ◽  
pp. 398-406 ◽  
Author(s):  
Wolfhard Weidel ◽  
Gebhard Koch ◽  
Friedrich Lohss

Dissociation in 90% phenol uncovers a layer of the Coli B-cell membrane showing the typical antiviral specificity of the receptor for phages T3, T4 and T7. Chemical analysis proved glucose, glucosamine and a yet unknown carbohydrate, probably a heptose, to be components of the receptor material, which amounts to about 13% of the dry weight of the whole membrane.Analogous material obtained from the membrane of B/3,4,7, a B-mutant resistant against phages T3, T4 and T7, has no activity against these phages and contains glucosamine and small amounts of glucose, but no heptose.In view of similar findings of Jesaitis and Goebel with T3,4,7 - receptor material from Shigella Sonnei, the rôle of the heptose as a characteristic and functionally indispensable component of lipocarbohydrates with receptor activity against T3, T4 and T7 is discussed.


2003 ◽  
Vol 69 (11) ◽  
pp. 6515-6519 ◽  
Author(s):  
Joseph F. Jones ◽  
Jason D. Feick ◽  
Daniel Imoudu ◽  
Nkiru Chukwumah ◽  
Margot Vigeant ◽  
...  

ABSTRACT The adhesion of nonflagellated Escherichia coli strain K-12 to polystyrene (PS) latex spheres or glass capillaries has been observed by using several techniques. Attention was focused on the orientation of the rod-shaped bacteria as they adhered to the surfaces in 100 mM phosphate-buffered saline. Data show that PS particles adhered to the ends of the bacteria more than 90% of the time. Moreover, the PS particles adhered to one end only, never to both. Similarly, for experiments with bacteria adhering to glass, the bacteria adhered on their ends. In order to determine whether the end of a bacterium had a different charge density from that of the middle, rotational electrophoresis experiments were used. These experiments indicated no measurable charge nonuniformity. In order to examine how strongly adhered the bacteria were to the PS particles, differential electrophoresis was used. Almost always, bacteria were found to be irreversibly adhered to the PS spheres. The cause of the oriented adhesion is not likely due to surface lipopolysaccharides (LPS), since the three strains of K-12 that were used, each having a different length of LPS, showed similar behavior. The results are discussed in terms of bacterial cell polarity. The data indicate that nanodomains on the bacterial ends are important for adhesion and that the time scale for irreversible adhesion is short.


Biochemistry ◽  
1990 ◽  
Vol 29 (24) ◽  
pp. 5694-5698 ◽  
Author(s):  
Paul F. Heelis ◽  
Tadashi Okamura ◽  
Aziz Sancar

2004 ◽  
Vol 186 (19) ◽  
pp. 6643-6646 ◽  
Author(s):  
Louisa Liberman ◽  
Howard C. Berg ◽  
Victor Sourjik

ABSTRACT Bacterial chemoreceptors are embedded in the inner cell membrane in tight clusters. We show that changes in receptor methylation that generate large changes in kinase activity have relatively little effect on cluster morphology. Thus, changes in receptor activity do not appear to be mediated by changes in receptor-kinase assembly.


1998 ◽  
Vol 66 (4) ◽  
pp. 1613-1621 ◽  
Author(s):  
Philippe A. Grange ◽  
Alan K. Erickson ◽  
Timothy J. Anderson ◽  
David H. Francis

ABSTRACT We have previously identified two mucin-type sialoglycoproteins from porcine intestinal epithelial cells with approximate molecular masses of 210 (intestinal mucin-type glycoprotein IMTGP-1) and 240 kDa (IMTGP-2) as receptors for the K88ab and K88ac fimbrial adhesins ofEscherichia coli. These receptors are detected in intestinal brush border membrane preparations from pigs with adhesive phenotypes but not from pigs with nonadhesive phenotypes and are postulated to be important determinants of the susceptibility of pigs to K88ab+ and K88ac+ enterotoxigenic E. coli infections. Using exoglycosidase digestion studies, we have now determined that β-linked galactose is an important component in the recognition of IMTGP-1 and IMTGP-2 by the K88ac adhesin. In addition, we observed a differential distribution of the K88ac adhesin binding activity of IMTGP-1 and IMTGP-2 along the crypt-villus axis, suggesting that receptor activity is dependent on the maturation state of the intestinal epithelial cells. Brush borders from immature intestinal epithelial cells possessed the highest concentrations of IMTGP-1 and IMTGP-2 receptor activity, with a progressive decrease in receptor activity as the cells mature. To characterize the differences in the carbohydrate moieties of IMTGP-1 and IMTGP-2, we developed a procedure for purifying the receptors, using phenol extraction followed by serial lectin affinity chromatography. Carbohydrate compositional analysis of the purified receptors indicated that the carbohydrate moieties of IMTGP-1 and IMTGP-2 consist of both N- and O-glycans containing galactose, glucose, sialic acid, mannose,N-acetylgalactosamine, N-acetylglucosamine, and fucose. The major difference between the two receptors is that IMTGP-2 contains a higher percentage of monosaccharides (mannose and glucose) commonly found in N-glycans.


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