PURIFICATION OF A CELL-ASSOCIATED HEMAGGLUTININ FROM SHIGELLA-DYSENTERIAE TYPE-1

A cell-associated hemagglutinin (HA) was isolated and purified from a clinical isolate of Shigella dysenteriae type 1 by affinity chromatogr aphy on a fetuin-agarose column. The purified hemagglutinin produced a single-stained protein band of around 66 kDa in sodium dodecyl sulpha te polyacrylamide gel electrophoresis (SDS-PAGE). In an immunodiffusio n test, HA-antisera produced a single precipitin band against the puri fied HA without exhibiting any reactivity towards lipopolysaccharide ( LPS) of S. dysenteriae type 1 strain. Inhibition of the hemagglutinati on by the glycoproteins fetuin, asialofetuin and a sugar derivative N- acetyl-neuraminic acid but not by simple sugars, suggested the specifi c requirement of complex carbohydrate for binding. Electron micrograph s of the purified HA revealed a morphology typical of globular protein .