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Journal of Virology, March 2008, p. 2752-2764, Vol. 82, No. 6
0022-538X/08/$08.00+0     doi:10.1128/JVI.02492-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Molecular Characterization of a Subgroup Specificity Associated with the Rotavirus Inner Capsid Protein VP2{triangledown}

Sarah M. McDonald and John T. Patton*

Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 50 South Drive MSC 8026, Room 6314, Bethesda, Maryland 20892-8026

Received 20 November 2007/ Accepted 21 December 2007

Group A rotaviruses are classified into serotypes, based on the reactivity pattern of neutralizing antibodies to VP4 and VP7, as well as into subgroups (SGs), based on non-neutralizing antibodies directed against VP6. The inner capsid protein (VP2) has also been described as a SG antigen; however, little is known regarding the molecular determinants of VP2 SG specificity. In this study, we characterize VP2 SGs by correlating genetic markers with the immunoreactivity of the SG-specific monoclonal antibody (YO-60). Our results show that VP2 proteins similar in sequence to that of the prototypic human strain Wa are recognized by YO-60, classifying them as VP2 SG-II. In contrast, proteins not bound by YO-60 are similar to those of human strains DS-1 or AU-1 and represent VP2 SG-I. Using a mutagenesis approach, we identified residues that determine recognition by either YO-60 or the group A-specific VP2 monoclonal antibody (6E8). We found that YO-60 binds to a conformationally dependent epitope that includes Wa VP2 residue M328. The epitope for 6E8 is also contingent upon VP2 conformation and resides within a single region of the protein (Wa VP2 residues A440 to T530). Using a high-resolution structure of bovine rotavirus double-layered particles, we predicted these epitopes to be spatially distinct from each other and located on opposite surfaces of VP2. This study reveals the extent of genetic variation among group A rotavirus VP2 proteins and illuminates the molecular basis for a previously described SG specificity associated with the rotavirus inner capsid protein.

* Corresponding author. Mailing address: Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, 50 South Dr. MSC 8026, Rm. 6314, Bethesda, MD 20892-8026. Phone: (301) 594-1615. Fax: (301) 496-8312. E-mail: jpatton{at}niaid.nih.gov

{triangledown} Published ahead of print on 23 January 2008.

Journal of Virology, March 2008, p. 2752-2764, Vol. 82, No. 6
0022-538X/08/$08.00+0     doi:10.1128/JVI.02492-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • McDonald, S. M., Aguayo, D., Gonzalez-Nilo, F. D., Patton, J. T. (2009). Shared and Group-Specific Features of the Rotavirus RNA Polymerase Reveal Potential Determinants of Gene Reassortment Restriction. J. Virol. 83: 6135-6148 [Abstract] [Full Text]  
  • Heiman, E. M., McDonald, S. M., Barro, M., Taraporewala, Z. F., Bar-Magen, T., Patton, J. T. (2008). Group A Human Rotavirus Genomics: Evidence that Gene Constellations Are Influenced by Viral Protein Interactions. J. Virol. 82: 11106-11116 [Abstract] [Full Text]  


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