Conformational changes of the N-terminal part of Mason-Pfizer monkey virus p12 protein during multimerization
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- 作者：Zdeně ; k Knejzlí ; k ; Pavel Ulbrich ; Martin Strohalm ; Hana Laš ; tů ; vková ; Milan Kodí ; č ; ek ; Michael Sakalian ; Tomá ; š ; Ruml
- 关键词：M-PMV ; α ; -Helix ; Multimerization ; CD spectroscopy ; Virus assembly ; p12 protein
- 刊名：Virology
- 出版年：2009
- 出版时间：10 October 2009
- 年：2009
- 卷：393
- 期：1
- 页码：168-176
- 全文大小：1313 K
文摘
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 α-helix during multimerization.