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Structural Basis of Egg Coat-Sperm Recognition at Fertilization (Jun 2017)

cell
Title:
Structural Basis of Egg Coat-Sperm Recognition at Fertilization
Journal:
Cell. 2017 Jun 15;169(7):1315-1326.e17
Author(s):
Raj I1, Sadat Al Hosseini H1, Dioguardi E1, Nishimura K1, Han L1, Villa A1, de Sanctis D2, Jovine L3.
Author(s) affiliation:
1Department of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge, SE-141 83, Sweden.
2 ESRF - The European Synchrotron Radiation Facility, Grenoble 38000, France.
3Department of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge, SE-141 83, Sweden
 

 

Short description:
Sperm-binding repeats of mollusk VERL and mouse ZP2 egg coat proteins fold similarly
Structures of VERL/lysin complexes reveal the atomic basis of egg coat-sperm recognition
A medium-affinity VERL repeat selectively binds lysin from the same species
VERL/lysin recognition suggests a mechanism for sperm penetration through the egg coat
Link to the journal
 

 

Abstract taken from PubMed

Abstract:
Recognition between sperm and the egg surface marks the beginning of life in all sexually reproducing organisms. This fundamental biological event depends on the species-specific interaction between rapidly evolving counterpart molecules on the gametes. We report biochemical, crystallographic, and mutational studies of domain repeats 1-3 of invertebrate egg coat protein VERL and their interaction with cognate sperm protein lysin. VERL repeats fold like the functionally essential N-terminal repeat of mammalian sperm receptor ZP2, whose structure is also described here. Whereas sequence-divergent repeat 1 does not bind lysin, repeat 3 binds it non-species specifically via a high-affinity, largely hydrophobic interface. Due to its intermediate binding affinity, repeat 2 selectively interacts with lysin from the same species. Exposure of a highly positively charged surface of VERL-bound lysin suggests that complex formation both disrupts the organization of egg coat filaments and triggers their electrostatic repulsion, thereby opening a hole for sperm penetration and fusion.

Copyright © 2017 The Author(s). Published by Elsevier Inc. All rights reserved.
Link to the paper on PubMed
 




 

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