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Title: Atomic force microscopy investigation of Mason-Pfizer monkey virus and human immunodeficiency virus type 1 reassembled particles

Abstract

Particles of {delta}ProCANC, a fusion of capsid (Canada) and nucleocapsid (NC) protein of Mason-Pfizer monkey virus (M-PMV), which lacks the amino terminal proline, were reassembled in vitro and visualized by atomic force microscopy (AFM). The particles, of 83-84 nm diameter, exhibited ordered domains based on trigonal arrays of prominent rings with center to center distances of 8.7 nm. Imperfect closure of the lattice on the spherical surface was affected by formation of discontinuities. The lattice is consistent only with plane group p3 where one molecule is shared between contiguous rings. There are no pentameric clusters nor evidence that the particles are icosahedral. Tubular structures were also reassembled, in vitro, from two HIV fusion proteins, {delta}ProCANC and CANC. The tubes were uniform in diameter, 40 nm, but varied in length to a maximum of 600 nm. They exhibited left handed helical symmetry based on a p6 hexagonal net. The organization of HIV fusion proteins in the tubes is significantly different than for the protein units in the particles of M-PMV {delta}ProCANC.

Authors:
 [1];  [2];  [3];  [2];  [2];  [3];  [4]
  1. Department of Molecular Biology and Biochemistry, University of California, Irvine, 560 SH, Irvine, CA 92697-3900 (United States)
  2. Institute of Chemical Technology, Technicka 5, 166 28 Prague 6 (Czech Republic)
  3. (Czech Republic)
  4. Department of Molecular Biology and Biochemistry, University of California, Irvine, 560 SH, Irvine, CA 92697-3900 (United States). E-mail: amcphers@uci.edu
Publication Date:
OSTI Identifier:
20977013
Resource Type:
Journal Article
Resource Relation:
Journal Name: Virology; Journal Volume: 360; Journal Issue: 2; Other Information: DOI: 10.1016/j.virol.2006.10.015; PII: S0042-6822(06)00752-5; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AIDS VIRUS; ATOMIC FORCE MICROSCOPY; IN VITRO; MONKEYS; PROLINE; PROTEINS

Citation Formats

Kuznetsov, Yu. G., Ulbrich, P., Institute of Molecular Genetics, Czech Academy of Sciences, 166 10 Prague, Haubova, S., Ruml, T., Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 166 10 Prague, and McPherson, A. Atomic force microscopy investigation of Mason-Pfizer monkey virus and human immunodeficiency virus type 1 reassembled particles. United States: N. p., 2007. Web. doi:10.1016/j.virol.2006.10.015.
Kuznetsov, Yu. G., Ulbrich, P., Institute of Molecular Genetics, Czech Academy of Sciences, 166 10 Prague, Haubova, S., Ruml, T., Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 166 10 Prague, & McPherson, A. Atomic force microscopy investigation of Mason-Pfizer monkey virus and human immunodeficiency virus type 1 reassembled particles. United States. doi:10.1016/j.virol.2006.10.015.
Kuznetsov, Yu. G., Ulbrich, P., Institute of Molecular Genetics, Czech Academy of Sciences, 166 10 Prague, Haubova, S., Ruml, T., Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 166 10 Prague, and McPherson, A. Tue . "Atomic force microscopy investigation of Mason-Pfizer monkey virus and human immunodeficiency virus type 1 reassembled particles". United States. doi:10.1016/j.virol.2006.10.015.
@article{osti_20977013,
title = {Atomic force microscopy investigation of Mason-Pfizer monkey virus and human immunodeficiency virus type 1 reassembled particles},
author = {Kuznetsov, Yu. G. and Ulbrich, P. and Institute of Molecular Genetics, Czech Academy of Sciences, 166 10 Prague and Haubova, S. and Ruml, T. and Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, 166 10 Prague and McPherson, A.},
abstractNote = {Particles of {delta}ProCANC, a fusion of capsid (Canada) and nucleocapsid (NC) protein of Mason-Pfizer monkey virus (M-PMV), which lacks the amino terminal proline, were reassembled in vitro and visualized by atomic force microscopy (AFM). The particles, of 83-84 nm diameter, exhibited ordered domains based on trigonal arrays of prominent rings with center to center distances of 8.7 nm. Imperfect closure of the lattice on the spherical surface was affected by formation of discontinuities. The lattice is consistent only with plane group p3 where one molecule is shared between contiguous rings. There are no pentameric clusters nor evidence that the particles are icosahedral. Tubular structures were also reassembled, in vitro, from two HIV fusion proteins, {delta}ProCANC and CANC. The tubes were uniform in diameter, 40 nm, but varied in length to a maximum of 600 nm. They exhibited left handed helical symmetry based on a p6 hexagonal net. The organization of HIV fusion proteins in the tubes is significantly different than for the protein units in the particles of M-PMV {delta}ProCANC.},
doi = {10.1016/j.virol.2006.10.015},
journal = {Virology},
number = 2,
volume = 360,
place = {United States},
year = {Tue Apr 10 00:00:00 EDT 2007},
month = {Tue Apr 10 00:00:00 EDT 2007}
}