Atomic force microscopy investigation of Mason-Pfizer monkey virus and human immunodeficiency virus type 1 reassembled particles
- 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)
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.
- OSTI ID:
- 20977013
- Journal Information:
- Virology, Journal Name: Virology Journal Issue: 2 Vol. 360; ISSN VIRLAX; ISSN 0042-6822
- Country of Publication:
- United States
- Language:
- English
Similar Records
Characterization of Mason--Pfizer monkey virus-induced cell fusion. [uv radiation]
Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization