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N ‐linked mannose glycoconjugates on shrimp thrombospondin, pm TSP‐II, and their involvement in the sperm acrosome reaction
Author(s) -
Timklay Wauranittha,
Magerd Sirilug,
Sato Chihiro,
Somrit Monsicha,
Watthammawut Atthaboon,
Senarai Thanyaporn,
Weerachatyanukul Wattana,
Kitajima Ken,
Asuvapongpatana Somluk
Publication year - 2019
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.23122
Subject(s) - glycoconjugate , shrimp , biology , penaeus monodon , acrosome reaction , lectin , sperm , mannose , glycoprotein , glycosylation , biochemistry , microbiology and biotechnology , genetics , fishery
Glycoconjugates in egg extracellular matrices are known to serve several functions in reproductive processes. Here, the presence of N ‐linked mannose (Man) glycoconjugates on shrimp thrombospondin ( pm TSP‐II) and their physiological functions were investigated in the black tiger shrimp Penaeus monodon . A molecular analysis of pm TSP‐II demonstrated anchorage sites for N ‐linked glycans in both the chitin‐binding and TSP3 domains. The presence of Man residues was verified by concanavalin A lectin histochemistry on the purified fraction of pm TSP‐II (250 kDa with protease inhibitor). The function of the Man glycoconjugates was evident by the Con A interference with the pm TSP‐II‐induced acrosome reaction (AR) as well as by the ability to recover the induction of the AR by the inclusion of Mans in the treatment mixture. In addition, the recombinant proteins of the three signature pm TSP‐II domains expressed in E. coli (lacking glycosylation) and mannosidase‐treated pm TSP‐II showed a minimal ability to initiate the AR response. Together, these results provide evidence of the pivotal role that Man‐linked pm TSP‐II plays in modulating the shrimp sperm AR, a novel role for a TSP family protein in shrimp reproductive biology.