HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Kukkonen, S. K. J. Articles by Plyusnin, A. Search for Related Content PubMed PubMed Citation Articles by Kukkonen, S. K. J. Articles by Plyusnin, A. Agricola Articles by Kukkonen, S. K. J. Articles by Plyusnin, A.

Tula hantavirus L protein is a 250 kDa perinuclear membrane-associated protein

Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland

Correspondence
Sami K. J. Kukkonen
sami.kukkonen{at}iki.fi

The complete open reading frame of Tula hantavirus (TULV) L RNA was cloned in three parts. The middle third (nt 2191–4344) could be expressed in E. coli and was used to immunize rabbits. The resultant antiserum was then used to immunoblot concentrated TULV and infected Vero E6 cells. The L protein of a hantavirus was detected, for the first time, in infected cells and was found to be expressed as a single protein with an apparent molecular mass of 250 kDa in both virions and infected cells. Using the antiserum, the expression level of the L protein was followed and image analysis of immunoblots indicated that there were 10⁴ copies per cell at the peak level of expression. The antiserum was also used to detect the L protein in cell fractionation studies. In cells infected with TULV and cells expressing recombinant L, the protein pelleted with the microsomal membrane fraction. The membrane association was confirmed with membrane flotation assays. To visualize L protein localization in cells, a fusion protein of L and enhanced green fluorescent protein, L–EGFP, was expressed in Vero E6 cells with a plasmid-driven T7 expression system. L–EGFP localized in the perinuclear region where it had partial co-localization with the Golgi matrix protein GM130 and the TULV nucleocapsid protein.

This article has been cited by other articles:

				A. Alminaite, V. Backstrom, A. Vaheri, and A. Plyusnin Oligomerization of hantaviral nucleocapsid protein: charged residues in the N-terminal coiled-coil domain contribute to intermolecular interactions J. Gen. Virol., September 1, 2008; 89(9): 2167 - 2174. [Abstract] [Full Text] [PDF]

				H. N. Ramanathan, D.-H. Chung, S. J. Plane, E. Sztul, Y.-k. Chu, M. C. Guttieri, M. McDowell, G. Ali, and C. B. Jonsson Dynein-Dependent Transport of the Hantaan Virus Nucleocapsid Protein to the Endoplasmic Reticulum-Golgi Intermediate Compartment J. Virol., August 15, 2007; 81(16): 8634 - 8647. [Abstract] [Full Text] [PDF]

				A. Alminaite, V. Halttunen, V. Kumar, A. Vaheri, L. Holm, and A. Plyusnin Oligomerization of hantavirus nucleocapsid protein: analysis of the N-terminal coiled-coil domain. J. Virol., September 1, 2006; 80(18): 9073 - 9081. [Abstract] [Full Text] [PDF]