By Itzhak Ofek
Attachment to host cells or tissues is usually step one within the institution of bacterial infections. a posh array of popularity, attachment, and virulence components is taken with this strategy, which fresh study has enormously illuminated. This complete and authoritative quantity discusses the categorical telephone and tissue-specific affinities of pathogenic microorganisms, together with bioinorganic surfaces similar to enamel, and is a vital reference for researchers and scholars of host-pathogen interactions.
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Extra resources for Bacterial Adhesion to Cells and Tissues
In most cases, both the microbe and the substratum possess highly heterogeneous surface characteristics. The equation that analyzes the adsorption of a gas onto a relatively simple surface may not be amenable to such complex systems as those involving microorganisms. It must be kept in mind, however, that the firm adhesion of a microorganism to a surface represents a composite of interactions at the molecular level. It is emphasized that certain kinds of information can be gained by various plots from adhesion experiments (Table 2-5).
Polypeptide chain -I. Negative I positive charge _PElrioheral glycoprotein Integral glycoprotein Glycolipid ~embrane '< ( '< '<'< '< i '< '< } 6~6 6bb~66 ~~yer Hydrophobic stretch Peripheral protein I CYTOPLASM I Figure 3-1 . Idealized representation of the surface of an animal cell membrane. Bacteria may bind to the cell coat, peripheral glycoproteins, integral glycoproteins, or glycoJipids. Adapted from Ofek et al. (1985). between the two classes of membrane constituents is sometimes difficult to resolve and very often they are referred to as nonintegral membrane constituents.
1984). Depending on the sizes and numbers of their hydrophobic regions, the membrane glycoproteins may display low to moderate solubility in detergent-free aqueous solutions. Unlike glycolipids, the integral glycoproteins in isolated form do not reassociate or "coat" cell membranes, but can be reassembled into liposomes (Eytan, 1982). The orientation of the reconstituted glycoproteins is, however, symmetrical in that half of the molecules insert with the glycosylated part facing outwardly and half facing inwardly.