Recombinant soluble low density lipoprotein receptor fragment inhibits minor group rhinovirus infection in vitro.
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 beta 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
TC
Institute of Biochemistry, University of Vienna, Austria.
Zechmeister
T
T
Gruenberger
M
M
Ronacher
B
B
Schwihla
H
H
Blaas
D
D
D000818:Animals; D016367:Baculoviridae / Q000235:genetics; D003001:Cloning, Molecular; D006801:Humans; D008024:Ligands; D010446:Peptide Fragments / Q000235:genetics / Q000494:pharmacology*; D011973:Receptors, LDL / Q000235:genetics; D011993:Recombinant Fusion Proteins / Q000494:pharmacology; D012229:Rhinovirus / Q000187:drug effects*; D017421:Sequence Analysis; D012995:Solubility; D018411:Spodoptera / Q000166:cytology
D008024:Ligands; D010446:Peptide Fragments; D011973:Receptors, LDL; D011993:Recombinant Fusion Proteins