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Journal of Virology, October 2001, p. 9696-9702, Vol. 75, No. 20
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.20.9696-9702.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

In Situ Spatial Organization of Potato Virus A Coat Protein Subunits as Assessed by Tritium Bombardment

Ludmila A. Baratova,1 Aleksander V. Efimov,2 Eugenie N. Dobrov,1 Natalija V. Fedorova,1 Reet Hunt,3 Gennadii A. Badun,4 Aleksander L. Ksenofontov,1 Lesley Torrance,5 and Lilian Järvekülg3,*

N. Belozersky Institute of Physico-Chemical Biology1 and Department of Chemistry,4 Moscow State University, Moscow 119899, and Institute of Protein Research, Puschino, Moscow Region,2 Russia; National Institute of Chemical Physics and Biophysics, Tallinn 12618, Estonia3; and Scottish Crop Research Institute, Invergowrie, Dundee DD2 5DA, Scotland, United Kingdom5

Received 9 April 2001/Accepted 13 July 2001

Potato virus A (PVA) particles were bombarded with thermally activated tritium atoms, and the intramolecular distribution of the label in the amino acids of the coat protein was determined to assess their in situ steric accessibility. This method revealed that the N-terminal 15 amino acids of the PVA coat protein and a region comprising amino acids 27 to 50 are the most accessible at the particle surface to labeling with tritium atoms. A model of the spatial arrangement of the PVA coat protein polypeptide chain within the virus particle was derived from the experimental data obtained by tritium bombardment combined with predictions of secondary-structure elements and the principles of packing alpha -helices and beta -structures in proteins. The model predicts three regions of tertiary structure: (i) the surface-exposed N-terminal region, comprising an unstructured N terminus of 8 amino acids and two beta -strands, (ii) a C-terminal region including two alpha -helices, as well as three beta -strands that form a two-layer structure called an abCd unit, and (iii) a central region comprising a bundle of four alpha -helices in a fold similar to that found in tobacco mosaic virus coat protein. This is the first model of the three-dimensional structure of a potyvirus coat protein.

* Corresponding author. Mailing address: National Institute of Chemical Physics and Biophysics, Akadeemia tee 23, Tallinn 12618, Estonia. Phone: 372 6398 367. Fax: 372 6398 382. E-mail: lilian{at}kbfi.ee.

Journal of Virology, October 2001, p. 9696-9702, Vol. 75, No. 20
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.20.9696-9702.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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