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J Virol, February 1998, p. 1210-1218, Vol. 72, No. 2
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

WIN 52035-Dependent Human Rhinovirus 16: Assembly Deficiency Caused by Mutations near the Canyon Surface

Wensheng Wang,dagger Wai-Ming Lee, Anne G. Mosser, and Roland R. Rueckert*

Institute for Molecular Virology, University of Wisconsin, Madison, Wisconsin 53706-1596

Received 2 July 1997/Accepted 16 October 1997

Three drug-dependent mutants of human rhinovirus 16 (HRV16) were characterized by sequence analyses of spontaneous mutant isolates and were genetically reconstructed from a parental cDNA plasmid. These mutants formed plaques in the presence but not in the absence of the selecting antiviral drug, WIN 52035, which binds to the capsid of wild-type virus and inhibits its attachment to the host cell. The drug-dependent phenotype of each mutant was caused by a single amino acid substitution in the VP1 coat protein. The three independent mutations conferring drug dependence are M1103T, T1208A, and V1210A. Single-step growth experiments involving rescue of one of the three mutants (V1210A) by delayed drug addition suggested (i) that the drug dependence lesion is at the stage of virus assembly and (ii) that one or more components of the viral assembly pool decay in the absence of drug. RNA accumulation and infectivity were unaffected by the absence of drug in all three mutants, suggesting that the labile assembly component is coat protein.

* Corresponding author. Mailing address: Institute for Molecular Virology, University of Wisconsin, 1525 Linden Dr., Madison, WI 53706-1596. Phone: (608) 262-6949. Fax: (608) 262-7414. E-mail: agmosser{at}facstaff.wisc.edu.

dagger Present address: Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392.




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