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J. Virol., Nov 1996, 7510-7516, Vol 70, No. 11
Copyright © 1996, American Society for Microbiology

Residue Trp-48 of Tva is critical for viral entry but not for high- affinity binding to the SU glycoprotein of subgroup A avian leukosis and sarcoma viruses

K Zingler and JA Young
Department of Microbiology and Immunology, University of California School of Medicine, San Francisco 94143, USA.

Previously, mutant Tva receptors were classified as either partially or completely defective in mediating subgroup A avian leukosis and sarcoma virus (ALSV-A) entry (C. Belanger, K. Zingler, and J. A. T. Young, J. Virol. 69:1019-1024, 1995; K. Zingler, C. Belanger, R. Peters, D. Agard, and J. A. T. Young, J. Virol. 69:4261-4266, 1995). To specifically test the abilities of these mutant Tva proteins to bind ALSV-A surface (SU) protein, binding studies were performed with a subgroup A SU-immunoadhesin. This fusion protein is composed of the subgroup A Schmidt-Ruppin SU protein fused in frame to a rabbit immunoglobulin constant region. This reagent was conjugated to fluorescein isothiocyanate and used for flow cytometric analysis with transfected human 293 cells expressing different forms of Tva. The SU- immunoadhesin bound the wild-type Tva protein with a KD of approximately 1.5 nM. Amino acid substitutions that reduced viral entry at Asp-46 and at Cys-35 and Cys-50, which are predicted to form an intrachain disulfide bond in Tva, drastically reduced the binding affinity for the SU-immunoadhesin. Thus, the effects on viral entry of some mutations could be explained solely by changes in the binding affinity for ALSV-A SU. However, this was not true for other mutations tested, especially those with amino acid substitutions that replaced Trp-48. Compared with the wild-type receptor, these latter mutations led to approximately 43- to 200-fold reductions in viral infectivity but only to approximately 2.5- to 3.4-fold reductions in the binding affinity for the SU-immunoadhesin. These results support a role for Trp- 48 of Tva in mediating steps of viral entry subsequent to binding ALSV- A SU.

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