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Salivary gland homogenate (SGH) from the female mosquitoes  Anopheles gambiae ,  An. stephensi ,  An. freeborni ,  An. dirus  and  An. albimanus  were found to exhibit hemagglutinating (lectin) activity. Lectin activity was not found for male  An. gambiae , or female  Ae aegypti ,  Culex quinquefasciatus ,  Phlebotomus duboscqi , and  Lutzomyia longipalpis . With respect to species-specificity,  An. gambiae  SGH agglutinates red blood cells (RBC) from humans, horse, sheep, goat, pig, and cow; it is less active for rats RBC, and not detectable for guinea-pigs or chicken RBC. Notably, lectin activity was inhibited by low concentrations of dextran sulfate 50–500 K, fucoidan, heparin, laminin, heparin sulfate proteoglycan, sialyl-containing glycans ( e.g.  3′-sialyl Lewis X, and 6′-sialyl lactose), and gangliosides ( e.g.  GM3, GD1, GD1b, GTB1, GM1, GQ1B), but not by simple sugars. These results imply that molecule(s) in the salivary gland target sulfated glycans. SGH from  An. gambiae  was also found to promote agglutination of HL-60 cells which are rich in sialyl Lewis X, a glycan that decorates PSGL-1, the neutrophils receptor that interacts with endothelial cell P-selectin. Accordingly, SGH interferes with HL-60 cells adhesion to immobilized P-selectin. Because  An. gambiae  SGH expresses galectins, one member of this family (herein named Agalectin) was expressed in  E. coli . Recombinant Agalectin behaves as a non-covalent homodimer. It does not display lectin activity, and does not interact with 500 candidates tested in a Glycan microarray. Gel-filtration chromatography of the SGH of  An. gambiae  identified a fraction with hemagglutinating activity, which was analyzed by 1D PAGE followed by in-gel tryptic digestion, and nano-LC MS/MS. This approach identified several genes which emerge as candidates for a lectin targeting sulfated glycans, the first with this selectivity to be reported in the SGH of a blood-sucking arthropod. The role of salivary molecules (sialogenins) with lectin activity is discussed in the context of inflammation, and parasite-vector-host interactions.

Evidence for a Lectin Specific for Sulfated Glycans in the Salivary Gland of the Malaria Vector, Anopheles gambiae