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:
- Department of Molecular Biology and Biochemistry, University of California, Irvine, 560 SH, Irvine, CA 92697-3900 (United States)
- Institute of Chemical Technology, Technicka 5, 166 28 Prague 6 (Czech Republic)
- (Czech Republic)
- 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}
}
-
The characteristics and requirements of multinucleate cell (syncytium) induction by Mason--Pfizer monkey virus (M-PMV) on human and non-human primate cells have been investigated. Multinucleate cell induction by this D-type retrovirus shows single-hit kinetics on human foreskin and rhesus monkey fetal lung cells. The peak of syncytium-forming activity in an isopycnic sucrose gradient coincides with the peak of M-PMV virions as assessed by electron microscopy and analysis of viral polypeptides. Unlike the paramyxoviruses, M-PMV does not induce early cell fusion when added in high concentrations to the target cells. Furthermore, multinucleate cell formation is maximal 48 hr postinfection and the sizemore »
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