The abalone egg vitelline envelope receptor for sperm lysin is a giant multivalent molecule

Swanson, Willie J.; Vacquier, Victor D.

doi:10.1073/pnas.94.13.6724

Cited by 114 publications

(153 citation statements)

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“…The VE of abalone eggs contains several proteins in addition to the large glycoprotein VERL (9). The majority of these are of significantly smaller size than VERL, migrating as a number of discrete peptides in the size range of 14.2 -24 kDa (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…VEs were solubilized following the protocol of ref. 9, aliquots of solubilized protein were reserved for SDS͞PAGE, and the remainder of VE proteins were reserved for MS͞MS. For SDS͞PAGE, 5 g of total pink and green VE proteins were loaded, run, and silver stained on 2.5-15% acrylamide gels as in ref.…”

Section: Methodsmentioning

confidence: 99%

“…Because ZP3 is thought to be responsible for the heterospecific barrier to fertilization presented by the mammalian egg coat through its sperm receptor activity (1), this result suggests adaptive divergence of ZP3 might contribute to reproductive isolation. The strongest evidence for the role of egg coat proteins in reproductive isolation come from abalone, where the sperm protein lysin facilitates sperm access to the egg membrane surface by dissolving a hole through the elevated egg VE (16) through binding to VERL (9). Lysin domains under positive selection are responsible for species-specific dissolution of the vitelline envelope (36), and are believed to coevolve with a subset of repetitive VERL elements similarly found to be under positive selection among abalone species (10).…”

Section: Positive Selection Drives the Evolution Of Most Abalone Egg mentioning

confidence: 99%

“…However, a large glycoprotein from the egg coat [vitelline envelope (VE)] of the marine gastropod abalone (Haliotis spp.) has been identified (9) and is known to contain a ZP domain (10), raising the possibility of a common molecular basis of animal egg coat structures.…”

mentioning

confidence: 99%

“…For example, sites within ZP3 under selection among mammals (13) correspond to the putative sperm binding domain in mouse (14,15). Similarly, the abalone sperm protein lysin binds to the ZP glycoprotein vitelline envelope receptor of lysin (VERL) (9) to facilitate sperm access to the egg membrane surface during fertilization (16), and both proteins show signs of adaptive divergence among abalone taxa (10,17,18). Coevolution between gamete recognition molecules is of significant interest because of their potential contribution to rapid reproductive isolation (19), which theoretical models show can occur even in sympatry if sexual conflict develops between components of male and female fitness (20).…”

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confidence: 99%

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Rapidly evolving zona pellucida domain proteins are a major component of the vitelline envelope of abalone eggs

Aagaard

MacCoss

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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116

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Proteins harboring a zona pellucida (ZP) domain are prominent components of vertebrate egg coats. Although less well characterized, the egg coat of the non-vertebrate marine gastropod abalone (Haliotis spp.) is also known to contain a ZP domain protein, raising the possibility of a common molecular basis of metazoan egg coat structures. Egg coat proteins from vertebrate as well as non-vertebrate taxa have been shown to evolve under positive selection. Studied most extensively in the abalone system, coevolution between adaptively diverging egg coat and sperm proteins may contribute to the rapid development of reproductive isolation. Thus, identifying the pattern of evolution among egg coat proteins is important in understanding the role these genes may play in the speciation process. The purpose of the present study is to characterize the constituent proteins of the egg coat [vitelline envelope (VE)] of abalone eggs and to provide preliminary evidence regarding how selection has acted on VE proteins during abalone evolution. A proteomic approach is used to match tandem mass spectra of peptides from purified VE proteins with abalone ovary EST sequences, identifying 9 of 10 ZP domain proteins as components of the VE. Maximum likelihood models of codon evolution suggest positive selection has acted among a subset of amino acids for 6 of these genes. This work provides further evidence of the prominence of ZP proteins as constituents of the egg coat, as well as the prominent role of positive selection in diversification of these reproductive proteins.adaptive evolution ͉ egg coat proteins ͉ gamete recognition M etazoan eggs are surrounded by a fibrous coat referred to as the zona pellucida, as the vitelline or perivitelline envelope, or as the chorion. The constituent proteins of these structures, which we collectively refer to as egg coats, have been well characterized among vertebrate taxa, including species of mammals (1), teleost fish (2), amphibians (3), and birds (4). These studies show the principle constituents of vertebrate egg coats to be glycosylated proteins sharing a common structural motif of Ϸ260 aa known as the zona pellucida (ZP) domain. ZP domain proteins are found among diverse eukaryotic structures, facilitating protein polymerization through intramolecular disulfide bonds among conserved cysteine resides within the ZP domain (5). For example, the predominant model of mouse egg coat (zona pellucida) formation posits filaments of arrays of two ZP proteins (ZP2 and ZP3) crosslinked via a third (ZP1), resulting in a fibrous matrix completely enclosing the egg (1). Although orthologs of these mammalian proteins are known from egg coat structures across vertebrate lineages (6, 7), non-vertebrate taxa are less well studied and it is not yet clear whether ZP proteins are similarly prominent features of egg coats across metazoans. For example, all known proteins comprising Drosophila egg coat structures lack ZP domains (8). However, a large glycoprotein from the egg coat [vitelline envelope (VE)] of the m...

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Positive Selection Drives the Evolution Of Most Abalone Egg mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Rapidly evolving zona pellucida domain proteins are a major component of the vitelline envelope of abalone eggs

Aagaard

MacCoss

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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116

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Abalone lysin: the dissolving and evolving sperm protein

2000

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Abalone sperm lysin is a non-enzymatic protein that creates a hole for sperm passage in the envelope surrounding the egg. Lysin exhibits species-specificity in making the hole and it evolves rapidly by positive selection. Our studies have focused on combining structural, biochemical, and evolutionary data to understand the mechanism of action and evolution of this remarkable protein. Currently, more is known about lysin than about any other protein involved in animal fertilization. We present an hypothesis to explain lysin's rapid evolution and the evolution of species-specific fertilization in this order of mollusks. We also propose a two-step model for lysin's action in which a dimer of lysin binds species-specifically to its glycoprotein receptor, and then monomerizes and binds the receptor in a non-speciesspecific manner. This experimental system yields data relevant to the general problem of molecular recognition between cell surfaces, and is also important to our thinking about how new species arise in the sea. BioEssays 23:95±103,

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Abalone lysin: the dissolving and evolving sperm protein

Kresge¹,

Vacquier²,

Stout³

2001

Bioessays

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Abalone sperm lysin is a non-enzymatic protein that creates a hole for sperm passage in the envelope surrounding the egg. Lysin exhibits species-specificity in making the hole and it evolves rapidly by positive selection. Our studies have focused on combining structural, biochemical, and evolutionary data to understand the mechanism of action and evolution of this remarkable protein. Currently, more is known about lysin than about any other protein involved in animal fertilization. We present an hypothesis to explain lysin's rapid evolution and the evolution of species-specific fertilization in this order of mollusks. We also propose a two-step model for lysin's action in which a dimer of lysin binds species-specifically to its glycoprotein receptor, and then monomerizes and binds the receptor in a non-species-specific manner. This experimental system yields data relevant to the general problem of molecular recognition between cell surfaces, and is also important to our thinking about how new species arise in the sea. BioEssays 23:95-103, 2001.

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The abalone egg vitelline envelope receptor for sperm lysin is a giant multivalent molecule

Cited by 114 publications

References 37 publications

Rapidly evolving zona pellucida domain proteins are a major component of the vitelline envelope of abalone eggs

Rapidly evolving zona pellucida domain proteins are a major component of the vitelline envelope of abalone eggs

Abalone lysin: the dissolving and evolving sperm protein

Abalone lysin: the dissolving and evolving sperm protein

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