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Journal of Virology, July 2007, p. 7310-7315, Vol. 81, No. 13
0022-538X/07/$08.00+0     doi:10.1128/JVI.00034-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Vaccinia Virus F13L YPPL Motif Is Required for Efficient Release of Extracellular Enveloped Virus{triangledown}

Kady M. Honeychurch,1 Guang Yang,2 Robert Jordan,2 and Dennis E. Hruby1,2*

Department of Microbiology, Oregon State University, Corvallis, Oregon 97331,1 SIGA Technologies, Inc., Corvallis, Oregon 973332

Received 5 January 2007/ Accepted 20 April 2007

The Tyr-X-X-Leu (YxxL) motif of the vaccinia virus F13L protein was examined for late (L) domain activity. The ability of an F13L deletion virus to form plaques was restored by PCR products containing single alanine substitutions within the motif and a YAAL construct but not by constructs lacking both the Y and L residues. Recombinant viruses possessing alanine substitutions in place of the tyrosine or the leucine residue in the YxxL motif demonstrated small, asymmetrical plaques. RNA interference-dependent depletion of Alix and TSG101 (host proteins involved in L domain-dependent protein trafficking) diminished extracellular enveloped virion production to various degrees, suggesting that the YxxL motif is a genuine L domain.

* Corresponding author. Mailing address: Oregon State University, 220 Nash Hall, Corvallis, OR 97331. Phone: (541) 737-1849. Fax: (541) 737-2440. E-mail: hrubyd{at}bcc.orst.edu

{triangledown} Published ahead of print on 2 May 2007.

Journal of Virology, July 2007, p. 7310-7315, Vol. 81, No. 13
0022-538X/07/$08.00+0     doi:10.1128/JVI.00034-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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