Cellular Localization of the Galactose-Binding Lectin from Human Serum

E. M. Rapoport^1*, M. V. Nekrasov¹, S. V. Khaidukov¹, E. V. Svirshchevskaya¹, L. S. Zhigis¹, L. V. Kozlov², T. N. Batalova², V. P. Zubov¹, and N. V. Bovin¹

¹Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117871 Russia; fax: (095) 335-1011; E-mail: rapoport@mail.ibch.ru

²Gabrichevsky Institute of Epidemiology and Microbiology, ul. Admirala Makarova 10, Moscow, 125212 Russia; fax: (095) 452-1830; E-mail: kozlovlv@orc.ru

^* To whom correspondence should be addressed.

Received March 28, 2000; Revision received May 31, 2000

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An SL2 lectin was isolated from human serum and characterized previously; cellular localization of the lectin was studied using polyclonal rabbit antibodies. According to cytofluorimetry, anti-SL2 antibodies bound only to lymphocytes and monocytes but not to other blood cells. Antibodies bound to Jurkat T cell lymphoma but did not interact with IM-9 cells of B cell origin. Moreover, the Jurkat cells bound oligosaccharides having the highest affinity to SL2 (GalNAcalpha_and Fucalpha1-2Gal), and this interaction was inhibited by anti-SL2 antibodies. Lysis of the Jurkat cells with subsequent electrophoresis and Western blotting indicates that anti-SL2 antibodies recognized a 14-kD protein.

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KEY WORDS: lectin, carbohydrates, antibodies, blood cells

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