Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization

Journal Article · Sat Oct 10 00:00:00 EDT 2009 · Virology

DOI:https://doi.org/10.1016/j.virol.2009.07.014· OSTI ID:21357545

Knejzlik, Zdenek; Ulbrich, Pavel ^[1]; Strohalm, Martin ^[1]; Lastuvkova, Hana; Kodicek, Milan ^[1]; Sakalian, Michael ^[2]; Ruml, Tomas ^[1]

---

1. Department of Biochemistry and Microbiology, Institute of Chemical Technology, Technicka 5, 166 28 Prague 6 (Czech Republic)
2. Institute of Microbiology, Academy of Sciences of the Czech Republic, Videnska 1083, 142 20 Prague 4 (Czech Republic)

The Mason-Pfizer monkey virus is a prototype Betaretrovirus with the defining characteristic that it assembles spherical immature particles from Gag-related polyprotein precursors within the cytoplasm of the infected cell. It was shown previously that the N-terminal part of the Gag p12 domain (wt-Np12) is required for efficient assembly. However, the precise role for p12 in mediating Gag-Gag interaction is still poorly understood. In this study we employed detailed circular dichroism spectroscopy, electron microscopy and ultracentrifugation analyses of recombinant wt-Np12 prepared by in vitro transcription and translation. The wt-Np12 domain fragment forms fibrillar structures in a concentration-dependent manner. Assembly into fibers is linked to a conformational transition from unfolded or another non-periodical state to alpha-helix during multimerization.

• OSTI ID: 21357545
• Journal Information: Virology, Journal Name: Virology Journal Issue: 1 Vol. 393; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
ANIMALS
CELL CONSTITUENTS
CENTRIFUGATION
CONFORMATIONAL CHANGES
CYTOPLASM
DICHROISM
ELECTRON MICROSCOPY
MAMMALS
MICROORGANISMS
MICROSCOPY
MONKEYS
ORGANIC COMPOUNDS
PARASITES
PRIMATES
PROTEINS
SEPARATION PROCESSES
SPECTROSCOPY
TRANSCRIPTION
ULTRACENTRIFUGATION
VERTEBRATES
VIRUSES