Post-translational Modification of Feline Alpha1-acid Glycoprotein in Retrovirus (fiv, Felv) Affected Cats

Introduction AGP (Alpha1-acid glycoprotein) is considered one of the major acute phase proteins in cats. In humans, AGP is a heavily glycosylated protein that undergoes several modifications of its glycan moiety during acute and chronic inflammatory pathologies. In this communication we present the feline AGP’s glycan moiety modifications in the course of two very frequent feline diseases, the feline acquired viral immunodeficiency (FIV-associated) and the feline leukemia virus (FeLV) associated lymphoma. The glycan moiety of fAGP was investigated by means of the binding of its oligosaccharides residues with specific lectins. Four lectins were used: Sambucus nigra agglutinin I (SNAI) and Maackia amurensis agglutinin (MAA) lectins were used to detect sialic acid residues, Aleuria aurantia lectin (AAL) was used to detect L-fucose residues and Concanavalin A (ConA) was used to evaluate branching degree. In order to determine the possible number and position of oligosaccharide chains, the cdna sequence of fagp was also determined.