December 2010

[JBC] Generating Carbohydrate Antibodies

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Biobits - carbohydrate antibodies

Antiglycan mAbs S1 and S2 can inhibit the binding of labeled leukocytes to HEVs (outlined with dotted line) in peripheral lymph nodes.

Cell-surface glycans play roles in a variety of immune functions, and to understand those functions, it is important to define which glycans are expressed on a cell surface at a given place and time. Monoclonal antibodies against glycans are problematic, however, as many different types of glycans are expressed intrinsically in animals. In this study, the researchers developed an efficient method of creating anticarbohydrate mAbs by immunizing mice that lack the enzymes to synthesize target glycans, specifically two N-acetylglucosamine-6-O-sulfotransferases. These mAbs, called S1 and S2, could bind to high endothelial venules in lymphoid tissue; S1 bound primarily to sulfated O-glycans, whereas S1 bound to both sulfated N- and O-glycans. The binding of S1 or S2 to leukocytes resulted in significant decreases in lymphocyte homing to lymph nodes and also decreased leukocyte adhesion to HEVs. These studies suggest that sulfated N- and O-glycans cooperate in lymphocyte homing and immune surveillance and provide a link between glycan structure and cell trafficking to secondary lymphoid organs. Considering the importance of glycan structures in other immune functions, the use of anticarbohydrate mAbs should become an increasingly important methodology.

Novel Anticarbohydrate Antibodies Reveal the Cooperative Function of Sulfated N- and O-Glycans in Lymphocyte Homing

Jotaro Hirakawa, Koichiro Tsuboi, Kaori Sato, Motohiro Kobayashi, Sota Watanabe, Atsushi Takakura, Yasuyuki Imai, Yuki Ito, Minoru Fukuda and Hiroto Kawashima

J. Biol. Chem., published online Oct. 7, 2010


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