PubMed HealthSearch

PubMed · 43768

The function of fimbriae in Myxococcus xanthus. II. The role of fimbriae in cell-cell interactions.

Abstract

Anti-fimbriae antiserum specifically inhibited swarming but no gliding motility per se in Myxococcus xanthus. However, formation of motile aggregates on agar and clumps in liquid media correlated with the presence of fimbriae. Ethylenediaminetetraacetic acid which inhibited swarming also inhibited fimbriae formation. Direct electron-microscopic observations revealed that fimbriae establish contact with apposing cell surfaces. Intact but not depolymerized fimbriae exhibited hemagglutination activity against guinea pig erythrocytes. This activity was inhibited by mannose, N-acetyl-D-galactosamine, and to a lesser degree by fructose, raffinose, melibiose, and alpha-methyl-D-mannoside. It is concluded that fimbriae are organelles which function to establish and maintain intercellular contacts, perhaps by a lectin-like function, during the coordinated movement of cell aggregates' (swarming) in myxobacteria. This hypothesis is supported by the observations of other workers that genes determining movement of cells in groups also control fimbriation in M. xanthus.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

W J Dobson, H D McCurdy, T H MacRae. 1979. The function of fimbriae in Myxococcus xanthus. II. The role of fimbriae in cell-cell interactions.. https://doi.org/10.1139/m79-214

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Chitin synthase activity from the slime variant of Neurospora crassa.

Chitin synthase (UDP-2-acetamido-2-deoxy-D-glucose:chitin 4-beta-acetamidodeoxy-D-glucosyltransferase, EC 2.4.1.16) activity from the wall-less variant of Neurospora crassa (slime) was partially characterized. The slime enzyme activity was found to be similar to that reported for slime-like and wild-type chitin synthase activities with respect to the following: specific activity, particulate cell-fraction localization, activation by N-acetylglucosamine, apparent Km with respect to substrate, pH optimum and ion requirement. It appears that the phenotype of slime cannot be solely accounted for by the absence of chitin synthase enzyme activity.

Acetylglucosamine

Specific interaction of human Tamm-Horsfall gylcoprotein with leucoagglutinin, a lectin from Phaseolus vulgaris (red kidney bean).

Human Tamm-Horsfall glycoprotein inhibits lymphocyte transformation induced by leucoagglutinin and haemagglutinin from Phaseolus vulgaris (red kidney bean). The glycoprotein interacts with the two lectins, giving insoluble precipitates. The interaction with leucoagglutinin is highly specific, and the shape of the precipitin curve is that of an antigen-antibody reaction; precipitation is specifically inhibited by N-acetyl-D-galactosamine. Results are discussed, and it is suggested that inhibition of lymphocyte transformation is due to competition between human Tamm-Horsfall glycoprotein and carbohydrate receptors on lymphocytes for the two lectins. The interaction between human Tamm-Horsfall glycoprotein and Phaseolus vulgaris lectins has been used to develop a one-step procedure for the separation of the two lectins by affinity chromatography on (human Tamm-Horsfall-glycoprotein)-Sepharose.

Acetylglucosamine

Regulation of N-acetylglucosamine uptake in yeast.

Various yeasts have been investigated for their ability to grow on N-acetylglucosamine as the sole carbon source and only those which are associated with the disease, candidiasis, gave positive results. The yeasts unable to grow on N-acetylglucosamine lacked the capacity to transport the aminosugar across the cell membrane. In pathogenic yeasts, two systems of different affinity for substrate were found to operate in the uptake of N-acetylglucosamine. In glucose-grown cells a constitutive, low affinity uptake system was present, but upon addition of inducer, a specific high affinity uptake system was synthesized. Experiments with the inhibitors of macromolecule synthesis suggested that the synthesis of RNA and protein is necessary for induction whereas the synthesis of DNA is not. In glucose-grown Candida albicans cells which are devoid of N-acetylglucosamine enters into the cells as phosphorylated form using a constitutive uptake system. Uranyl acetate (0.01 mM) which binds to cell membrane-associated polyphosphates, inhibited completely the inducible uptake of N-acetylglucosamine. Labelling experiments, designed to determine the temporal sequence of appearance of N-acetylglucosamine in intracellular free sugar and sugar-phosphate pools, indicated that N-acetylglucosamine first appeared in the cells as pohosphorylated form. Similar results were obtained with Saccharomyces phosphorylated form. Similar results were obtained with Saccharomyces cerevisiae 3059 and some other yeasts which are devoid of N-acetylglucosamine kinase in both uninduced and induced conditions. These results are consistent with the model of van Steveninck that involves phosphorylation during transpost. Furthermore, inhibitors of energy metabolism (arsenate, azide and cyanide), proton conductor (m-chlorocarbonylcyanide phenylhydrazine) and dibenzyl diammonium ion (membrane permeable cation) inhibited the inducible N-acetylglucosamine uptake in C. albicans.

Acetylglucosamine