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J. Biol. Chem., Vol. 277, Issue 22, 19727-19734, May 31, 2002
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From the Department of Microbiology and Immunology, Loyola
University Medical Center, Maywood, Illinois 60153
Oligomeric spike (S) glycoproteins extend from
coronavirus membranes. These integral membrane proteins assemble within
the endoplasmic reticulum of infected cells and are subsequently
endoproteolyzed in the Golgi, generating noncovalently associated S1
and S2 fragments. Once on the surface of infected cells and virions,
peripheral S1 fragments bind carcinoembryonic antigen-related cell
adhesion molecule (CEACAM) receptors, and this triggers membrane fusion reactions mediated by integral membrane S2 fragments. We focused on the
quaternary structure of S and its interaction with CEACAMs. We
discovered that soluble S1 fragments were dimers and that CEACAM binding was entirely dependent on this quaternary structure. However, two differentially tagged CEACAMs could not co-precipitate with the S
dimers, suggesting that binding sites were closely juxtaposed in the
dimer (steric hindrance) or that a single CEACAM generated global
conformational changes that precluded additional interactions (negative
cooperativity). CEACAM binding did indeed alter S1 conformations, generating alternative disulfide linkages that were revealed on SDS gels. CEACAM binding also induced separation of S1 and S2. Differentially tagged S2 fragments that were free of S1 dimers were not
co-precipitated, suggesting that S1 harbored the primary oligomerization determinants. We discuss the distinctions between the
S·CEACAM interaction and other virus-receptor complexes involved in
receptor-triggered entry.
Quaternary Structure of Coronavirus Spikes in Complex with
Carcinoembryonic Antigen-related Cell Adhesion Molecule Cellular
Receptors*
*
This work was supported in part by National Institutes of
Health Grant R01 NS 31616 (to T. M. G.) and NIAID Grant 5 T32
AI07508-05 from the National Institutes of Health (to K. L. Knight).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Microbiology
and Immunology, Loyola University Medical Center, 2160 South First
Ave., Maywood, IL 60153. Tel.: 708-216-4850; Fax: 708-216-9574; E-mail:
tgallag@lumc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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