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J. Biol. Chem., Vol. 277, Issue 42, 39112-39118, October 18, 2002
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From the We employed a quantitative cell fusion assay to
identify structural domains of CD46 required for its function as a
receptor for human herpesvirus 6 (HHV-6). We examined the activities of recombinant variants of CD46, including different isoforms as well as
engineered truncations and molecular chimeras with decay-accelerating factor, a related protein in the family of regulators of complement activation (RCA). We observed strong receptor activity for all four
CD46 isoforms, which differ in the membrane-proximal extracellular and
cytoplasmic domains, indicating that the critical determinants for
HHV-6 receptor activity reside outside the C-terminal portion of CD46.
Analysis of the short consensus repeat (SCR) regions that comprise most
of the extracellular portion of CD46 indicated a strong dependence on
SCRs 2 and 3 and no requirement for SCRs 1 or 4. Fusion-inhibition
studies with SCR-specific monoclonal antibodies supported the essential
role of SCRs 2 and 3 in HHV-6 receptor activity. These findings
contrast markedly with fusion mediated by measles virus glycoproteins
for which we observed a strict dependence on SCRs 1 and 2, consistent
with previous reports. These results expand the emerging notion that
CD46 and other members of the RCA family are co-opted in distinct
manners by different infectious pathogens.
Human Herpesvirus 6 and Measles Virus Employ Distinct CD46
Domains for Receptor Function*
,¶
Laboratory of Viral Diseases, NIAID,
National Institutes of Health, Bethesda, Maryland 20892 and the
§ Unit of Human Virology, Department of Biological and
Technological Research, San Raffaele Scientific Institute,
20132 Milano, Italy
*
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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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