Lectin binding analysis of Argas polonicus tissue glycoproteins

Proteins of the Malpighian tubules (MT), midgut tissue (MG), salivary glands (SG), internal reproductive organs (RO), epidermis (EP), cerebral ganglion (CG), rectal ampulla (RA) and larval homogenate (LA) of Argas (Argas) polonicus were studied for their antigenicity and lecin affinity using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), immunoblotting, lectin affinoblotting and enzyme-linked lectin sorbentassay (ELLSA) techniques. A glycoprotein of 305 kDA was found in all tissues studied. All low molecular weight antigenic proteins recognized by anti-larval immune pigeon serum, except for one of 35 kDA, i.e. the 19-, 21-, 23-, 27-, 34-, and 46- kDa proteins, were shown to be glycoproteins. The glycosylation was shown to be N-linked in all of these antigens, but O-type glycosylation was also demonstrated in the 34-kDa glycoprotein. The correlation between the glycosylation and antigenicity of these proteins is also discussed.