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Journal of Virology, December 1998, p. 10246-10250, Vol. 72, No. 12
Institute of Biochemistry, Medical Faculty,
A-1030 Vienna, Austria
Received 20 May 1998/Accepted 24 August 1998
The large family of human rhinoviruses, the main causative agents
of the common cold, is divided into the major and the minor group based
on receptor specificity. Major group viruses attach to intercellular
adhesion molecule 1 (ICAM-1), a member of the immunoglobulin
superfamily, whereas minor group viruses use low-density lipoprotein
receptors (LDLR) for cell entry. During early attempts aimed at
isolating the minor group receptor, we discovered that a protein with
virus binding activity was released from HeLa cells upon incubation
with buffer at 37°C (F. Hofer, B. Berger, M. Gruenberger, H. Machat,
R. Dernick, U. Tessmer, E. Kuechler, and D. Blaas, J. Gen. Virol.
73:627-632, 1992). In light of the recent discovery of several new
members of the LDLR family, we reinvestigated the nature of this
protein and present evidence for its being derived from the human
very-low density lipoprotein receptor (VLDLR). A soluble VLDLR fragment
encompassing the eight complement type repeats and representing the
N-terminal part of the receptor was then expressed in the baculovirus
system; both the shed protein and the recombinant soluble VLDLR bind
minor group viruses and inhibit viral infection of HeLa cells in a
concentration-dependent manner.
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Very-Low-Density Lipoprotein Receptor Fragment Shed
from HeLa Cells Inhibits Human Rhinovirus Infection
*
Corresponding author. Mailing address: Institute of
Biochemistry, Medical Faculty, Dr. Bohr Gasse 9/3, A-1030, Vienna,
Austria. Phone: 43 1 4277 61630. Fax: 43 1 4277 9616. E-mail:
dieter.blaas{at}univie.ac.at.
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