Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Lectin microbial

Fig. 4 Enthalpy-entropy plot obtained by ITC measurement on a family of related microbial lectins interacting with natural and synthetic carbohydrates. Fig. 4 Enthalpy-entropy plot obtained by ITC measurement on a family of related microbial lectins interacting with natural and synthetic carbohydrates.
Mirelman, D., and Ofek, I. (1986). Introduction to microbial lectins and agglutinins. In "Microbial Lectins and Agglutinins" (D. Mirelman, ed.), pp. 1-19. John Wiley Sons Inc., New York, NY. [Pg.152]

Sandros, J., Rozdzinski, E., Zheng, J., Cowburn, D., and Tuomanen, E. (1994). Lectin domains in the toxin of Bordetella pertussis Selectin mimicry linked to microbial pathogenesis. Glycoconj.. 11,501-506. [Pg.156]

TSome microbial pathogens have lectins that mediate bacterial adhesion to host cells or toxin entry into cells. The bacterium believed responsible for most gastric ulcers, Helicobacter pylori, adheres to the inner surface of the stomach by interactions between bacterial membrane lectins and specific oligosaccharides of membrane glycoproteins of the gastric epithelial cells... [Pg.263]

Because they are easily accessible, glycans displayed on the surface of mammalian cells provide enormous opportunities to bind to many microbial pathogens, ranging from viruses to molecular toxins and from pathogenic bacteria to parasites. In multivalent binding, multiple interactions between ligands and various receptors are common (Fig. 16.1). One representative example is ricin—a versatile and durable A-B-type toxin—in which one of the protein chains (the B chain) is a lectin that interacts and binds terminal galactose (Gal) on the surface of eukaryotic cells with multivalent interactions to facilitate entry of the other peptide chain (the A chain) into the cell to cause cellular death via the catalytic... [Pg.426]

Microbial pathogens utilize different types of lectins for targeting the glycans on the surface of host cells. Many bacteria are covered with pili or fimbriae that contain a very special class of lectins known as adhesins because they play a role in attachment to epithelial cells. These lectins are monomeric and comprise only one binding site. Because the adhesins are repeated on the pilus, a larger number of adhesins on the bacterial surface create multivalent interaction with the host glycans. [Pg.440]

Cell walls are biochemically rather inert with reduced digestibility to many organisms because of their complex cellulose, pectin, and lignin molecules. Callose and lignin are often accumulated at the site of infection or wounding (6,7) and form a penetration barrier. Synthesis of inhibitory proteins (e.g., lectins, protease inhibitors) or enzymes (e.g., chitinase, lysozyme, hydrolases, nucleases) that could degrade microbial cell walls or other microbial constituents would be protective, as well as synthesis of peroxidase and phe-nolase, which could help inactivate phytotoxins produced by many bacteria and fungi. These proteins are either stored in the vacuole... [Pg.2]

Glycan arrays have been used to evaluate the specificity of numerous plant, animal, and microbial lectins. [Pg.47]

Some unusual aminosaccharides can have antibacterial and antibiotic effects this is the case of 3-amino-3-deoxy-D-glucose isolated from deep-sea bacteria (a Bacillus strain) collected at a depth of 4310 m [178]. More importantly, cellular receptors responsible for the adherence of microbes to eukaryotic cells are often lectin-type adhesins [179], and aminosaccharide treatment can result in the protection against microbial infections [ 180]. [Pg.2430]

The three-dimensional structure of TcTS was determined by crystallographic studies on a fully active TcTS mutant.145 147 It consists of two domains the N-terminal catalytic domain which forms a six-bladed [1 propeller, characteristic of microbial sialidases, connected through a long a helix to a C-terminal lectin-like domain which does not participate in the enzymatic reaction. The catalytic domain... [Pg.337]

Basinger, J.M., 2003. Ricin and peanut lectin transport and influence on microbial activity in soil, Ph.D. dissertation, Texas Tech University, Lubbock, TX. [Pg.98]

The largest number of microbial lectins characterized to date are from bacterial sources (Table 1). [Pg.480]

A major role of the microbial lectins is to mediate the adhesion of the organisms to host cells, an initial stage of infection. This has been extensively demonstrated both in uitro, in studies with isolated cells and cell cultures, and in uiuo in experimental animals. [Pg.495]

Mirelman, D. (Ed.) (1986) Microbial Lectins and Agglutinins. John Wiley and Sons, New York. [Pg.501]

Chapter 13. Microbial lectins and their glycoprotein receptors Nathan Sharon and Halina Lis. ... [Pg.685]

Cole BC, Knudtson KL, Oliphant A, Sawitzke AD, Pole A, Manohar M, Benson LS, Ahmed E, Atkin CL The sequence of the Mycoplasma arthritidis superantigen, MAM identification of functional domains and comparison with microbial superantigens and plant lectin mitogens. J Exp Med 1996 183 1105-1110. [Pg.176]

Mirelman, D. Microbial Lectins and Agglutins Properties and Biological Activity, D. Mirelman, Wiley-Interscience, Sons, New York, 1986. [Pg.25]

Markwell, M. A. K. Viruses as Hemagglutinins and Lectins. In Microbial Lectins and Agglutinins Properties and Biological Activity Mirelman, E., Ed. Wiley Series in Ecological and Applied Microbiology Wiley-Interscience Publication, John Wiley and Sons Publishing Co. New York, 1986 pp 21-53. [Pg.26]


See other pages where Lectin microbial is mentioned: [Pg.213]    [Pg.213]    [Pg.225]    [Pg.210]    [Pg.1844]    [Pg.326]    [Pg.76]    [Pg.290]    [Pg.203]    [Pg.212]    [Pg.171]    [Pg.11]    [Pg.123]    [Pg.571]    [Pg.47]    [Pg.172]    [Pg.1785]    [Pg.2428]    [Pg.2457]    [Pg.378]    [Pg.464]    [Pg.30]    [Pg.475]    [Pg.475]    [Pg.476]    [Pg.482]    [Pg.503]    [Pg.504]    [Pg.581]   
See also in sourсe #XX -- [ Pg.145 , Pg.427 , Pg.438 , Pg.456 , Pg.460 ]




SEARCH



© 2024 chempedia.info