Rat zona pellucida glycoproteins: Molecular cloning and characterization of the three major components

Akatsuka, Kazuhiko; Yoshida-Komiya, Hiromi; Tulsiani, D. R. P.; Orgebin‐Crist, Marie‐Claire; Hiroi, Masahiko; Araki, Yoshihiko

doi:10.1002/(sici)1098-2795(199812)51:4<454::aid-mrd13>3.0.co;2-g

Cited by 23 publications

(14 citation statements)

References 73 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Egg layers are indicated to the right: CL, cumulus layer; ZP, zona pellucida; PVS, perivitelline space; EC, egg cytoplasm. (b) ZP3 protein structure with predicted functional domains drawn to scale, based on alignment with Mus (Akatsuka et al . 1998; Jovine et al .…”

Section: Discussionmentioning

confidence: 99%

Reproductive protein evolution within and between species: maintenance of divergent ZP3 alleles in Peromyscus

Turner

Hoekstra

2008

Molecular Ecology

View full text Add to dashboard Cite

In a variety of animal taxa, proteins involved in reproduction evolve more rapidly than nonreproductive proteins. Most studies of reproductive protein evolution, however, focus on divergence between species, and little is known about differentiation among populations within a species. Here we investigate the molecular population genetics of the protein ZP3 within two Peromyscus species. ZP3 is an egg coat protein involved in primary binding of egg and sperm and is essential for fertilization. We find that amino acid polymorphism in the sperm-combining region of ZP3 is high relative to silent polymorphism in both species of Peromyscus. In addition, while there is geographical structure at a mitochondrial gene (Cytb), a nuclear gene (Lcat) and eight microsatellite loci, we find no evidence for geographical structure at Zp3 in Peromyscus truei. These patterns are consistent with the maintenance of ZP3 alleles by balancing selection, possibly due to sexual conflict or pathogen resistance. However, we do not find evidence that reinforcement promotes ZP3 diversification; allelic variation in P. truei is similar among populations, including populations allopatric and sympatric with sibling species. In fact, most alleles are present in all populations sampled across P. truei's range. While additional data are needed to identify the precise evolutionary forces responsible for sequence variation in ZP3, our results suggest that in Peromyscus, selection to maintain divergent alleles within species contributes to the pattern of rapid amino acid substitution observed among species.

show abstract

Section: Discussionmentioning

confidence: 99%

Reproductive protein evolution within and between species: maintenance of divergent ZP3 alleles in Peromyscus

Turner

Hoekstra

2008

Molecular Ecology

View full text Add to dashboard Cite

show abstract

“…Therefore, other mammalian species containing four zona proteins were sought. In rat, the three transcripts encoding ZP1, ZP2, and ZP3 initially reported (37) have been augmented by a fourth that encodes a hypothetical protein of 540 amino acids that is 68% identical to human ZP4/ZPB with 20 conserved cysteine residues and both a trefoil and zona domain (Fig. 5).…”

Section: Table I Lc-ms and Ms/ms Analysis Of Rat Zp4mentioning

confidence: 99%

“…Despite close examination, no additional zona proteins were detected in native mouse zonae pellucidae by mass spectrometry (12). Mouse and rat evolutionarily diverged only 12-24 million years ago (36), and the primary protein structures of rat ZP1, ZP2, and ZP3 are 88 -92% identical to their murine homologues (37). However, the existence of an additional zona transcript deduced from cDNA (GenBank TM accession number NM_172330) raised the possibility of a fourth protein in the rat zona pellucida.…”

mentioning

confidence: 99%

Human Sperm Do Not Bind to Rat Zonae Pellucidae Despite the Presence of Four Homologous Glycoproteins

Hoodbhoy

Joshi

Boja

et al. 2005

Journal of Biological Chemistry

View full text Add to dashboard Cite

The specificity of sperm-egg recognition in mammals is mediated primarily by the zona pellucida surrounding ovulated eggs. Mouse sperm are quite promiscuous and bind to human eggs, but human spermatozoa will not bind to mouse eggs. The mouse zona pellucida contains three glycoproteins, ZP1, ZP2, and ZP3, which are conserved in rat and human. The recent observation that human zonae pellucidae contain a fourth protein raises the possibility that the presence of four zona proteins will support human sperm binding. Using mass spectrometry, four proteins that are similar in size and share 62-70% amino acid identity with human ZP1, ZP2, ZP3, and ZP4/ZPB were detected in rat zonae pellucidae. However, although mouse and rat spermatozoa bind to eggs from each rodent, human sperm bind to neither, and the presence of human follicular fluid did not alter the specificity of sperm binding. In addition, mutant mouse eggs lacking hybrid/complex N-glycans or deficient in Core 2 O-glycans were no more able to support human sperm binding than normal mouse eggs. These data suggest that the presence of four zona proteins are not sufficient to support human sperm binding to rodent eggs and that additional determinants must be responsible for taxon-specific fertilization among mammals.After passage through the lower female reproductive tract, mammalian spermatozoa fertilize ovulated eggs in the ampulla of the oviduct. A key event in successful fertilization is sperm binding to the surface of the extracellular zona pellucida that surrounds the egg. Following zona penetration and fusion with the egg plasma membrane, peripherally located cortical granules within the egg exocytose their contents, which modify the zona matrix such that sperm no longer bind. These events are carefully orchestrated to ensure that a single sperm fertilizes a single egg (1).Despite decades of investigation, the molecular basis of mammalian sperm-egg recognition remains controversial. Human sperm are particularly fastidious and bind to old world primate eggs but not to eggs of other species. In contrast, mouse sperm are quite promiscuous, binding with near universality to eggs from other mammalian orders (2). The mouse zona pellucida is composed of three major glycoproteins, ZP1, ZP2, and ZP3, one of which, ZP2, is proteolytically cleaved following fertilization (3). Mouse lines have been established that lack each of the zona proteins as well as lines in which human ZP2 and/or human ZP3 replace endogenous mouse proteins (4). Mice without ZP1 form a zona pellucida matrix to which mouse sperm bind and Zp1 null females are fertile, albeit with decreased fecundity (5). Mice in which endogenous proteins are replaced with human ZP2, human ZP3, or both are also fertile but do not support human sperm binding (6, 7). Thus, mouse ZP1 is not required for sperm-egg recognition, and human ZP2 and ZP3 are not sufficient to support human sperm binding.These results suggest that "humanized" zona matrices either lack a factor or contain a factor that prevents the binding of h...

show abstract

“…Even though rat ZP3 shares more than 90% amino acid sequence homology with mouse ZP3, variations in glycosylation patterns and glycan chain composition appear to provide an additional level of species-specificity (Akatsuka et al 1998;Smith et al 2005). The lack of effects on mouse and chicken fertility after immunisation with possum rZP3 or pZP3e, previously shown to reduce female possum fertility, is an encouraging start in demonstrating that species specificity of fertility-control vaccines may be possible.…”

Section: Discussionmentioning

confidence: 94%

Development of a contraceptive vaccine for the marsupial brushtail possum (Trichosurus vulpecula): lack of effects in mice and chickens immunised with recombinant possum ZP3 protein and a possum ZP3 antifertility epitope

et al. 2008

View full text Add to dashboard Cite

Zona pellucida fertility-control vaccines are being developed in New Zealand to control an introduced marsupial pest, the brushtail possum (Trichosurus vulpecula). In this study recombinant possum ZP3 protein (rZP3) and a possum ZP3 peptide (amino acids 334-361) (both known to block fertility in possums) were examined for their potential to induce speciesspecific, or at least marsupial-specific, infertility. Laboratory mice (a 'model' eutherian mammal species) and domestic chickens (a 'model' bird species) immunised with possum rZP3 or possum-infertility ZP3 peptide in Freund's adjuvants showed no reduction in a range of parameters indicative of reproductive performance. The lack of contraceptive effects on mouse and chicken fertility is an encouraging result in terms of rZP3 and ZP3 peptide specificity, and these promising antigens are to be expressed in a bacterial ghost vaccine system for mucosal delivery to possums and the effects on possum fertility evaluated. Ultimately, a much wider range of non-target species will need to be screened and tested once the antigens have been successfully formulated in their final delivery vehicle.

show abstract

Rat zona pellucida glycoproteins: Molecular cloning and characterization of the three major components

Cited by 23 publications

References 73 publications

Reproductive protein evolution within and between species: maintenance of divergent ZP3 alleles in Peromyscus

Reproductive protein evolution within and between species: maintenance of divergent ZP3 alleles in Peromyscus

Human Sperm Do Not Bind to Rat Zonae Pellucidae Despite the Presence of Four Homologous Glycoproteins

Development of a contraceptive vaccine for the marsupial brushtail possum (Trichosurus vulpecula): lack of effects in mice and chickens immunised with recombinant possum ZP3 protein and a possum ZP3 antifertility epitope

Contact Info

Product

Resources

About