Vitelline‐coat lysin: Comparison of lysins among three species in the genus Tegula

Abstract

Vitelline-coat lysins from two species of marine mollusc of the genus Tegula, Tegula lischkei and Tegula sp., were purified and their properties compared with those of Tegula pfeifferi. Cross-reaction tests among these three species proved that the lysin action on the vitelline coat was species specific. Each of the lysins from these three species is a single, basic polypeptide with a molecular weight of 16000-17000 and an isoelectric point of pH 10.5. All of them share a common antibody recognition site(s) for the anti-T. pfeifferi lysin antibody. Their amino acid sequences were analyzed using intact lysins and peptides separated by reverse phase high-performance liquid chromatography after V8 proteinase digestion. The amino acid sequences of the N-terminus (Nos 1-66) from the three species showed 98% homology, and those of the C-terminus (Nos 91-118) showed 89% homology. It was concluded that the species specificity of the vitelline coat lysin appears to be determined by a sequence of 24 residues (Nos 67-90) in the middle region of the molecule.

Histological Description of the Male and Female Gonads in Tegula eiseni, T. funebralis, T. aureotincta, T. gallina and T. regina from Bahia Tortugas, B.C.S., Mexico

“…At the specific level, lysins in the acrosomic vesicle dissolve the chorion of mature oocytes, interacting with the lysin receptor on the surface of the oocyte, with which they are associated by coevolution. These factors are determinant for genetic isolation between sibling species coexisting in very close areas (Dohmen, 1983;Haino-Fukushima et al, 1999).…”

Egg and sperm recognition systems during fertilization

“…2001). Also, the mechanisms of species‐specific binding of molluscan lysins to respective lysin‐receptors, referred to as VERL, a vitelline envelope receptor for lysin, as well as their dissolving mechanisms have been extensively studied (Haino‐Fukushima et al. 1999; Lyon & Vacquier 1999; Kresge et al.…”

The Tegula Tango: A Coevolutionary Dance of Interacting, Positively Selected Sperm and Egg Proteins

“…Upon contact with the VE, a glycoproteinaceous layer that surrounds the egg, lysin is released and proceeds to dissolve a hole in the VE via a nonenzymatic mechanism (Haino-Fukushima 1974;Lewis et al 1982). This VE dissolution is highly species-specific in both Tegula (Haino 1971;Haino-Fukushima et al 1999;Hellberg and Vacquier 1999) and Haliotis (Vacquier et al 1990). Positive selection promotes the rapid interspecific divergence of lysin in both abalone (Lee and Vacquier 1995) and Tegula (Hellberg and Vacquier 1999), although variation within species is very low (Metz et al 1998b;Clark et al 2009).…”