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Vol. 12, Issue 4, 809-820, April 2001
1
Integrin-associated Proteins CD9, CD81, and CD98
and
*Department of Cell Biology, University of Virginia Health
System, School of Medicine, Charlottesville, Virginia 22908; and
ADAM 3 is a sperm surface glycoprotein that has been implicated in
sperm-egg adhesion. Because little is known about the adhesive activity of ADAMs, we investigated the interaction of ADAM 3 disintegrin domains, made in bacteria and in insect cells, with
murine eggs. Both recombinant proteins inhibited sperm-egg binding and
fusion with potencies similar to that which we recently reported for the ADAM 2 disintegrin domain. Alanine scanning mutagenesis
revealed a critical importance for the glutamine at position 7 of the
disintegrin loop. Fluorescent beads coated with the ADAM 3 disintegrin domain bound to the egg surface. Bead binding was
inhibited by an authentic, but not by a scrambled, peptide analog of
the disintegrin loop. Bead binding was also inhibited by the
function-blocking anti-Department of Microbiology, University of Mie, Mie,
Japan, 514-8507
6 monoclonal antibody (mAb) GoH3, but not by
a nonfunction blocking anti-6 mAb, or by mAbs against either the
v or 
3 integrin subunits. We also present evidence that
in addition to the tetraspanin CD9, two other
1-integrin-associated proteins, the tetraspanin CD81 as well
as the single pass transmembrane protein CD98 are expressed on murine
eggs. Antibodies to CD9 and CD98 inhibited in vitro fertilization and
binding of the ADAM 3 disintegrin domain. Our findings are
discussed in terms of the involvement of multiple sperm ADAMs and
multiple egg 1 integrin-associated proteins in sperm-egg
binding and fusion. We propose that an egg surface "tetraspan web"
facilitates fertilization and that it may do so by fostering ADAM-integrin interactions.
Corresponding author: E-mail address:
jw7g{at}virginia.edu.
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