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RESEARCH COMMUNICATION |
a Institute of Biochemistry, University of Vienna, A-1030 Vienna, Austria;
b Institute of Applied Genetics, University of Agriculture, Forestry, and Renewable Natural Resources in Vienna, Muthgasse, A-1190 Wien, Austria.
A fragment of the low density lipoprotein receptor encompassing the seven ligand binding repeats was expressed in Sf9 insect cells as a fusion protein with a carboxyl-terminally linked hexa-his tag by using a baculovirus vector. Up to 10 mg/l of the fusion protein was secreted into the medium. The material was soluble in the absence of detergent and active in binding ß very low density lipoprotein and a member of the minor group of human rhinoviruses (HRV2) in ligand blots from sodium dodecyl sulfate-polyacrylamide gels run under nonreducing conditions. The receptor fragment specifically inhibits viral infection of HeLa cells by minor group HRVs in a concentration-dependent manner. Viral infectivity is neutralized by aggregation.—Marlovits, T. C., Zechmeister, T., Gruenberger, M., Ronacher, B., Schwihla, H., Blaas, D. Recombinant soluble low density lipoprotein receptor fragment inhibits minor group rhinovirus infection in vitro. FASEB J. 12, 695–703 (1998)
Key Words: human rhinovirus • LDLR • viral inhibition • baculovirus expression
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