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Journal of Virology, November 1999, p. 9072-9079, Vol. 73, No. 11
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Poliovirus Mutants at Histidine 195 of VP2 Do Not Cleave VP0 into VP2 and VP4

Musa Hindiyeh,1,dagger Qi-Han Li,1,Dagger Ravi Basavappa,2,§ James M. Hogle,2 and Marie Chow1,*

Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205,1 and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 021152

Received 12 May 1999/Accepted 4 August 1999

The final stage of poliovirus assembly is characterized by a cleavage of the capsid precursor protein VP0 into VP2 and VP4. This cleavage is thought to be autocatalytic and dependent on RNA encapsidation. Analysis of the poliovirus empty capsid structure has led to a mechanistic model for VP0 cleavage involving a conserved histidine residue that is present in the surrounding environment of the VP0 cleavage site. Histidine 195 of VP2 (2195H) is hypothesized to activate local water molecules, thus initiating a nucleophilic attack at the scissile bond. To test this hypothesis, 2195H mutants were constructed and their phenotypes were characterized. Consistent with the requirement of VP0 cleavage for poliovirus infectivity, all 2195H mutants were nonviable upon introduction of the mutant genomes into HeLa cells. Replacement of 2195H with threonine or arginine resulted in the assembly of a highly unstable 150S virus particle. Further analyses showed that these particles contain genomic RNA and uncleaved VP0, criteria associated with the provirion assembly intermediate. These data support the involvement of 2195H in mediating VP0 cleavage during the final stages of virus assembly.

* Corresponding author. Mailing address: University of Arkansas for Medical Sciences, 4301 W. Markham, Slot 511, Little Rock, AR 72205. Phone: (501) 686-5155. Fax: (501) 686-5362.

dagger Present address: University of Utah/ARUP, Salt Lake City, UT 84108.

Dagger Present address: Institute of Medical Biology, Kunming, People's Republic of China.

§ Present address: Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642.

Journal of Virology, November 1999, p. 9072-9079, Vol. 73, No. 11
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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