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Journal of Virology, April 2001, p. 4002-4007, Vol. 75, No. 8
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.8.4002-4007.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Biophysical Characterization and Vector-Specific Antagonist Activity of Domain III of the Tick-Borne Flavivirus Envelope Protein

S. Bhardwaj,1 M. Holbrook,2 R. E. Shope,2 A. D. T. Barrett,2 and S. J. Watowich1,*

Department of Human Biological Chemistry & Genetics and Sealy Center for Structural Biology1 and Department of Pathology and Center for Tropical Diseases,2 University of Texas Medical Branch, Galveston, Texas 77555

Received 30 October 2000/Accepted 23 January 2001

The molecular determinants responsible for flavivirus host cell binding and tissue tropism are largely unknown, although domain III of the envelope protein has been implicated in these functions. We examined the solution properties and antagonist activity of Langat virus domain III. Our results suggest that domain III adopts a stably folded structure that can mediate binding of tick-borne flaviviruses but not mosquito-borne flaviviruses to their target cells. Three clusters of phylogenetically conserved residues are identified that may be responsible for the vector-specific antagonist activity of domain III.

* Corresponding author. Mailing address: Dept. of Human Biological Chemistry & Genetics, University of Texas Medical Branch, Galveston, TX 77555-0645. Phone: (409) 747-4749. Fax: (409) 747-4745. E-mail: watowich{at}bloch.utmb.edu.

Journal of Virology, April 2001, p. 4002-4007, Vol. 75, No. 8
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.8.4002-4007.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.