A mouse seminal vesicle‐secreted lysozyme c‐like protein modulates sperm capacitation

Lysozyme (LYZ) c‐like proteins are primarily present in the testis and epididymis of male reproductive tissues. Here, we report a novel member of the c‐type LYZ family, the seminal vesicle‐secreted LYZ c‐like protein (SVLLP). Three forms of SVLLP were purified from mouse seminal vesicle secretions and characterized as glycoproteins with the same protein core but different N‐linked glycans. SVLLP is structurally similar to c‐type LYZ proteins. Only one of the 20 invariant residues was altered in the consensus sequence of c‐type LYZs; however, the changed residue (N53S) is one of two essential catalytic residues. LYZ activity assays demonstrated that the three glycoforms of SVLLP lacked enzyme activity. SVLLP is primarily expressed in seminal vesicles. Immunohistochemistry revealed that it occurs in the luminal fluid and mucosal epithelium of the seminal vesicles. Testosterone is not the primary regulator for its expression in the seminal vesicle. SVLLP binds to sperm and suppresses bovine serum albumin‐induced sperm capacitation, inhibits the acrosome reaction, and blocks sperm–oocyte interactions in vitro, suggesting that SVLLP is a sperm capacitation inhibitor. We report a novel member of the c‐type lysozyme (LYZ) family, the seminal vesicle‐secreted LYZ c‐like protein (SVLLP). The change in one of the two essential catalytic residues causes SVLLP lack of LYZ activity. SVLLP is the first c‐type LYZ‐like protein that is not expressed in the testis or epididymis but predominantly expressed in seminal vesicles and involved in the inhibition of sperm capacitation in vitro.