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A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusion

A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusion THE union of sperm and egg is a special membrane fusion event that gives a signal1 to begin development. We have hypothesized2 that proteins mediating cell–cell fusion events resemble viral fusion proteins3,4and have shown that PH-30, a sperm surface protein involved in sperm–egg fusion5, shares biochemical characteristics with viral fusion proteins6. We report here the complementary DNA and deduced amino-acid sequences of the mature αand β subunits of PH-30. Both are type-I integral membrane glyco-proteins. The α subunit contains a putative fusion peptide typical of viral fusion proteins and the β subunit contains a domain related to a family of soluble integrin ligands found in snake venoms. Thus, the PH-30α/ βcomplex resembles many viral fusion proteins in both its membrane topology and its predicted binding and fusion functions. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusion

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References (36)

Publisher
Springer Journals
Copyright
Copyright © 1992 by Nature Publishing Group
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/356248a0
Publisher site
See Article on Publisher Site

Abstract

THE union of sperm and egg is a special membrane fusion event that gives a signal1 to begin development. We have hypothesized2 that proteins mediating cell–cell fusion events resemble viral fusion proteins3,4and have shown that PH-30, a sperm surface protein involved in sperm–egg fusion5, shares biochemical characteristics with viral fusion proteins6. We report here the complementary DNA and deduced amino-acid sequences of the mature αand β subunits of PH-30. Both are type-I integral membrane glyco-proteins. The α subunit contains a putative fusion peptide typical of viral fusion proteins and the β subunit contains a domain related to a family of soluble integrin ligands found in snake venoms. Thus, the PH-30α/ βcomplex resembles many viral fusion proteins in both its membrane topology and its predicted binding and fusion functions.

Journal

Nature – Springer Journals

Published: Mar 19, 1992

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