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Biology of Reproduction 64, 805-811 (2001)
© 2001 Society for the Study of Reproduction, Inc.


Regular Article

Cloning of Rainbow Trout Egg Envelope Proteins: Members of a Unique Group of Structural Proteins1

Sven Johan Hyllnera,b, Liselotte Westerlundc, Per-Erik Olsson2,,c, and Arndt Schopend,e

a Department of Biochemistry and Molecular Biology, University of Medicine and Dentistry of New Jersey, Newark, New Jersey 07103 b Scandinavian QC Laboratories, Medicinaregatan 3A, SE-413 46 Göteborg, Sweden c Department of Cell and Molecular Biology, Unit of Physiology, Umeå University, SE-901 87 Umeå, Sweden d Roche Institute of Molecular Biology, Hoffman-LaRoche, Nutley, New Jersey 07110 e Gemini Consulting, D-61352 Bad Homburg, Germany

ABSTRACT

All vertebrate eggs are surrounded by an extracellular envelope that protects the egg and is vital for a successful fertilization. The terminology and functions of the egg envelope vary in different vertebrate groups, but the envelope itself is consistently composed of a few major proteins that are deposited around the oocyte during oocyte growth. Here, we describe the deduced amino acid sequences and tissue expression patterns of the three major egg envelope proteins for rainbow trout (Oncorhynchus mykiss). All three vitelline envelope proteins (VEPs) are expressed in the livers of both male and female fish, with higher expression in females. In addition, VEP{gamma} mRNA is also detected in the female gonads. To our knowledge, this is the first time that expression of a VEP protein gene has been demonstrated to occur in more than one organ. Sequence comparison reveals that all three VEP proteins share distinct homology with their amphibian, avian, and mammalian counterparts. Whereas mammalian zona pellucida protein 3 isoforms contain two conserved serines needed for sperm binding, these are not conserved in teleost species, in which sperm entry is restricted to the micropyle. Besides the difference in VEP{gamma} sperm-binding function, the high sequence homology suggests that the egg envelope proteins from these distinct vertebrate groups share a common ancestry and form a unique group of structural proteins.

FOOTNOTES

First decision: 10 May 2000.

1 Supported by the Swedish Council for Forestry and Agricultural Research (S.J.H.), Boehringer Ingelheim Fonds (A.S.), and the Centre for Environmental Research, Umeå, Sweden (P.-E.O.).

2 Correspondence. FAX: 46 90 786 6691; per-erik.olsson{at}biology.umu.se




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