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Journal of Virology, April 2001, p. 3999-4001, Vol. 75, No. 8
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.8.3999-4001.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Langat Virus M Protein Is Structurally Homologous to prM

Michael R. Holbrook, Heiman Wang, and Alan D. T. Barrett*

Center for Tropical Diseases and Department of Pathology, University of Texas Medical Branch, Galveston, Texas 77555-0609

Received 9 November 2000/Accepted 23 January 2001

Langat (LGT) virus M protein has been generated in a recombinant system. Antiserum raised against the LGT virus M protein neutralizes tick-borne encephalitis serocomplex flaviviruses but not mosquito-borne flaviviruses, indicating that the M protein is exposed on the surface of virions. The antiserum recognizes intracellular LGT virus prM/M and binds to prM and M in Western blots of whole-cell lysates and purified virus, respectively. These data suggest that the prM and M proteins are structurally similar under native conditions and support the hypothesis that the "pr" portion of prM facilitates proper folding of the M protein for expression on the virion surface.

* Corresponding author. Mailing address: Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555-0609. Phone: (409) 772-6662. Fax: (409) 747-2415. E-mail: abarrett{at}utmb.edu.

Journal of Virology, April 2001, p. 3999-4001, Vol. 75, No. 8
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.8.3999-4001.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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