This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mitra, T.
Right arrow Articles by Green, K. Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mitra, T.
Right arrow Articles by Green, K. Y.

 Previous Article  |  Next Article 

Journal of Virology, May 2004, p. 4931-4935, Vol. 78, No. 9
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.9.4931-4935.2004

Mutagenesis of Tyrosine 24 in the VPg Protein Is Lethal for Feline Calicivirus

Tanaji Mitra, Stanislav V. Sosnovtsev, and Kim Y. Green*

Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Department of Health and Human Services, Bethesda, Maryland 20892

Received 3 July 2003/ Accepted 16 January 2004

The genome of feline calicivirus (FCV) is an ~7.7-kb single-stranded positive-sense RNA molecule that is polyadenylated at its 3' end and covalently linked to a VPg protein (calculated mass, 12.6 kDa) at its 5' end. We performed a mutational analysis of the VPg protein in order to identify amino acids potentially involved in linkage to the genome and replication. The tyrosine residues at positions 12, 24, 76, and 104 were changed to alanines by mutagenesis of an infectious FCV cDNA clone. Viruses were recovered when Tyr-12, Tyr-76, or Tyr-104 of the VPg protein was changed to alanine, but virus was not recovered when Tyr-24 was changed to alanine. Growth properties of the recovered viruses were similar to those of the parental virus. We examined whether the amino acids serine, threonine, and phenylalanine could substitute for the tyrosine at position 24, but these mutations were lethal as well. A tyrosine at this relative position is conserved among all calicivirus VPg proteins examined thus far, suggesting that the VPg protein of caliciviruses, like those of picornaviruses and potyviruses, utilizes tyrosine in the formation of a covalent bond with RNA.


* Corresponding author. Mailing address: Department of Health and Human Services, National Institutes of Health, NIAID/LID, Building 50, Room 6318, 9000 Rockville Pike, Bethesda, MD 20892-8026. Phone: (301) 594-1665. Fax: (301) 480-5031. E-mail: kgreen{at}niaid.nih.gov.


Journal of Virology, May 2004, p. 4931-4935, Vol. 78, No. 9
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.9.4931-4935.2004




This article has been cited by other articles:

  • Grzela, R., Szolajska, E., Ebel, C., Madern, D., Favier, A., Wojtal, I., Zagorski, W., Chroboczek, J. (2008). Virulence Factor of Potato Virus Y, Genome-attached Terminal Protein VPg, Is a Highly Disordered Protein. J. Biol. Chem. 283: 213-221 [Abstract] [Full Text]  
  • Kaiser, W. J., Chaudhry, Y., Sosnovtsev, S. V., Goodfellow, I. G. (2006). Analysis of protein-protein interactions in the feline calicivirus replication complex. J. Gen. Virol. 87: 363-368 [Abstract] [Full Text]