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Journal of Virology, December 2009, p. 12631-12635, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01072-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Protonation of Individual Histidine Residues Is Not Required for the pH-Dependent Entry of West Nile Virus: Evaluation of the "Histidine Switch" Hypothesis{triangledown}

Steevenson Nelson,{dagger} Subhajit Poddar,{dagger} Tsai-Yu Lin, and Theodore C. Pierson*

Viral Pathogenesis Section, Laboratory of Viral Diseases, National Institutes of Health, Bethesda, Maryland

Received 26 May 2009/ Accepted 11 September 2009

Histidine residues have been hypothesized to function as sensors of environmental pH that can trigger the activity of viral fusion proteins. We investigated a requirement for histidine residues in the envelope (E) protein of West Nile virus during pH-dependent entry into cells. Each histidine was individually replaced with a nonionizable amino acid and tested functionally. In each instance, mutants capable of orchestrating pH-dependent infection were identified. These results do not support a requirement for any single histidine as a pH-sensing "switch," and they suggest that additional features of the E protein are involved in triggering pH-dependent steps in the flavivirus life cycle.

* Corresponding author. Mailing address: Viral Pathogenesis Section, Laboratory of Viral Diseases, National Institutes of Health, 33 North Drive, Building 33, Room 1E19A.2, Bethesda, MD 20892. Phone: (301) 451-7977. Fax: (301) 451-7978. E-mail: piersontc{at}mail.nih.gov

{triangledown} Published ahead of print on 23 September 2009.

{dagger} These authors contributed equally.

Journal of Virology, December 2009, p. 12631-12635, Vol. 83, No. 23
0022-538X/09/$08.00+0     doi:10.1128/JVI.01072-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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