Specificity of mycoparasite attachment to the host cell surface

Publisher Website
Google Scholar
Abstract
The use of isolated cell wall fragments of Choanephora cucurbitarum (Berk. et Rav.) Thaxter (a host) and of Linderina pennispora Raper and Fennell (a nonhost) has provided not only a convenient method to quantify attachment of the parasite, Piptocephalis virginiana Leadbeater and Mercer, by the artificial inoculation and washing-off procedure, but also an excellent material for investigations of the molecular basis of specificity and host recognition. The parasite germ tubes are attached to the cell wall fragments of the host but not of the nonhost. Attachment was inhibited by the addition of sugars, chitobiose and chitotriose, and by treatment with acid or alkali indicating the involvement of proteins or glycoproteins in recognizing sugar residues at the cell surface. Both host and nonhost showed a positive binding reaction with fluorescent lectins specific for N-acetyl-D-glucosamine oligomer. The cell surface of the nonhost also contains D-galactose and N-acetyl-D-galactosamine residues as lectin binding sites. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of cell wall extracts of host and nonhost revealed 4 bands of glycoproteins common to both fungi and 2 were specific to the host.

This publication has 1 reference indexed in Scilit: