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Ganglioside binding pattern of CD33-related siglecs
Eugenia Rapoport1, Ilya Mikhalyov, Jiquan Zhang
1Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia.
Abstract:
Our study deals with the interaction of CD33 related-siglecs-5,-7,-8,-9,-10 with gangliosides GT1b, GQ1b, GD3, GM2, GM3 and GD1a. Siglec-5 bound preferentially to GQ1b, but weakly to GT1b, whereas siglec-10 interacted only with GT1b ganglioside. Siglec-7 and siglec-9 displayed binding to gangliosides GD3, GQ1b and GT1b bearing a disialoside motif, though siglec-7 was more potent; besides, siglec-9 interacted also with GM3. Siglec-8 demonstrated low affinity to the gangliosides tested compared with other siglecs. Despite high structural similarity of CD33 related siglecs, they demonstrated different ganglioside selectivity, in particular to the Neu5Acalpha2-8Neu5Ac motif.