Accession Number : ADA308369

Title :   Fabrication of High Affinity Synthetic Ligands for Microbes.

Descriptive Note : Final rept. 26 Sep 94-25 Nov 95,

Corporate Author : JOHNS HOPKINS UNIV BALTIMORE MD SCHOOL OF MEDICINE

Personal Author(s) : Schnaar, Ronald L.

PDF Url : ADA308369

Report Date : 16 FEB 1996

Pagination or Media Count : 28

Abstract : To define their carbohydrate binding specificity, a variety of Vibrio cholera strains were tested for their ability to (a) hemagglutinate red blood cells in a carbohydrate-inhibitable manner; (b) bind radiolabeled multivalent carbohydrate ligands; and (c) aggregate in response to multivalent carbohydrates. Although hemagglutination and aggregation were demonstrated, reproducible carbohydrate specificity was not apparent. Binding of E. histolytica membranes to specific carbohydrates was characterized. High affinity binding to clustered, multivalent GalNAc residues was demonstrated. Highest affinity was obtained when >%O GalNAc residues were synthetically clustered by covalently attaching them to a carrier protein (bovine serum albumin). Binding of GalNAc to the E. histolytica lectin required the 3- and 4-position hydroxyls, as demonstrated using synthetic deoxy analogs of GalNAc. BGlcNAc-specific hexosaminidase was characterized in E. histolytica membranes.

Descriptors :   *FABRICATION, *LIGANDS, *TOXINS AND ANTITOXINS, *ENTAMOEBA HISTOLYTICA, *VIBRIO CHOLERAE, PROTEINS, WATER POLLUTION, CLUSTERING, CONTAMINANTS, MEMBRANES, INFECTIOUS DISEASES, ERYTHROCYTES, BOVINES, CARBOHYDRATES, SERUM ALBUMIN, BLOOD CELLS, HEMAGGLUTINATION TESTS.

Subject Categories : Microbiology
      Toxicology

Distribution Statement : APPROVED FOR PUBLIC RELEASE