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Journal of Virology, January 2004, p. 683-691, Vol. 78, No. 2
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.2.683-691.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Spacing between Cysteines Two and Three of the LDL-A Module of Tva Is Important for Subgroup A Avian Sarcoma and Leukosis Virus Entry

Tia Rai, Deborah Marble, Kayla Rihani, and Lijun Rong*

Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612

Received 17 July 2003/ Accepted 3 October 2003

Rong et al. have demonstrated previously that with a few substitutions, the fourth repeat of human low-density lipoprotein (hLDL-A4) receptor can functionally replace the LDL-A module of Tva, the cellular receptor for subgroup A avian sarcoma and leukosis virus (ASLV-A), in viral entry (L. Rong, K. Gendron, and P. Bates, Proc. Natl. Acad. Sci. USA 95:8467-8472, 1998). Here we have shown that swapping the amino terminus of hLDL repeat 5 (hLDL-A5) with that of Tva, in addition to the corresponding substitutions made in human LDL-A4, was required to convert hLDL-A5 into an efficient ASLV-A receptor. These results substantiated our previous findings regarding the role of the specific residues in the viral interaction domain of Tva and demonstrated the critical role of the amino terminus of the Tva LDL-A module in ASLV-A infection. Furthermore, we have shown that the residues between cysteines 2 and 3 of the Tva LDL-A module in a Tva/LDL-A5 chimeric protein can be functionally replaced by the corresponding region of another LDL-A module, human LDL receptor-related protein repeat 22 (LDL-A22), to mediate efficient ASLV-A entry. Since the only conserved feature between the C2-C3 region of LDL-A22 and the Tva LDL-A module is that both contain nine amino acids of which none are conserved, we conclude that the spacing between C2 and C3 of the LDL-A module of Tva is an important determinant for ASLV-A entry. Thus, the present study provides strong evidence to support our hypothesis that one role of the N terminus of the LDL-A module of Tva is to allow proper folding and conformation of the protein for optimal interaction with the viral glycoprotein EnvA in ASLV-A entry.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, E829 MSB, 835 S. Wolcott Ave., Chicago, IL 60612. Phone: (312) 355-0203. Fax: (312) 996-6415. E-mail: lijun{at}uic.edu.

Journal of Virology, January 2004, p. 683-691, Vol. 78, No. 2
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.2.683-691.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Contreras-Alcantara, S., Godby, J. A., Delos, S. E. (2006). The Single Ligand-binding Repeat of Tva, a Low Density Lipoprotein Receptor-related Protein, Contains Two Ligand-binding Surfaces. J. Biol. Chem. 281: 22827-22838 [Abstract] [Full Text]  
  • Rai, T., Caffrey, M., Rong, L. (2005). Identification of Two Residues within the LDL-A Module of Tva That Dictate the Altered Receptor Specificity of Mutant Subgroup A Avian Sarcoma and Leukosis Viruses. J. Virol. 79: 14962-14966 [Abstract] [Full Text]  
  • Guo, Y., Yu, X., Rihani, K., Wang, Q.-Y., Rong, L. (2004). The Role of a Conserved Acidic Residue in Calcium-dependent Protein Folding for a Low Density Lipoprotein (LDL)-A Module: IMPLICATIONS IN STRUCTURE AND FUNCTION FOR THE LDL RECEPTOR SUPERFAMILY. J. Biol. Chem. 279: 16629-16637 [Abstract] [Full Text]  


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