LECTIN-BINDING CHARACTERISTICS OF MALE AND FEMALE SALIVARY-GLAND PROTEINS OF ANOPHELES-GAMBIAE - IDENTIFICATION AND CHARACTERIZATION OF FEMALE-SPECIFIC GLYCOPROTEINS

Male and female salivary gland proteins of Anopheles gambiae were anal yzed on blots of SDS gels by lectin binding in order to identify femal e specific glycoproteins. At least six major and several minor protein bands were identifiable in the total female gland proteins which were not visible in the male glands. The proximal lateral region of the fe male gland contained minor proteins which were similar in electrophore tic pattern to male salivary gland proteins. The distal lateral region and the median lobe each contained four different predominant protein bands. Western blot analysis with seven biotinylated lectins showed a distinct pattern of glycosylation between male and female salivary gl ands. Concanavalin agglutinin (Con A) and Dolichos biflorus agglutinin (DBA) bound to the highest number of male and female salivary gland g lycoproteins while Ricinus communis agglutinin (RCA) and wheat germ ag glutinin (WGA) showed the least binding, recognizing at least five fem ale specific salivary gland glycoproteins. Soybean agglutinin (SEA) an d peanut agglutinin (PNA) displayed a similarity in their binding patt ern and distinguished the most female specific glycoproteins. Con A bi nding of the different morphological regions of the female salivary gl and detected seven glycoproteins in the distal lateral region and four in the median lobe with trace amounts of glycoproteins in the proxima l regions, In contrast, SEA detected glycoproteins mostly in the media n lobe including eight female specific glycoproteins. Four out of the eight female specific glycoproteins were also found in the distal late ral region, Enzymatic deglycosylation followed by lectin binding showe d that salivary gland glycoproteins are predominantly asparagine linke d N-glycans with some possible O-linked glycans. (C) 1997 Elsevier Sci ence Ltd.