Fucosylated Clusterin in semen promotes the uptake of stressed-damaged proteins to dendritic cells via DC-SIGN

MERLOTTI IPPÓLITO, ANTONELLA; DANTAS, EZEQUIEL; VARESE, AUGUSTO; REMES LENICOV, FEDERICO; CAUDANA, P; NUÑEZ, N; NIBORSKI, L; SEDLIK, C; PIAGGIO, ELIANE; GEFFNER, JORGE; AMIGORENA, SEBASTIAN; SABATTE, JUAN

Marsella

Workshop; 2nd Workshop on Dendritic Cell Biology Labex DCBIOL; 2015

Centre d'Immunologie de Marseille-Luminy.

Clusterin is one of the major extracellular chaperones. It interacts with a variety of stressed proteins to prevent their aggregation, guiding them for receptor-mediated endocytosis and intracellular degradation. The concentration of clusterin in semen is almost 20-fold higher than that found in serum, raising the question about the role of seminal plasma clusterin in reproduction. No previous studies have analyzed wheter seminal clusterin has chaperone activity. We have previously shown that seminal plasma clusterin, but not serum clusterin, expresses an extreme abundance of fucosylated glycans. These motifs enable seminal plasma clusterin to bind to DC-SIGN with very high affinity. We propose that semen clusterin might target extracellular stressed proteins to DC-SIGN on dendritic cells (DCs), regulating immune response to antigens present on semen. We have shown that seminal plasma clusterin interacts with stressed proteins, inhibits their aggregation (P