Supramolecular organization of immature and mature murine leukemia virus revealed by electron cryo-microscopy: Implications for retroviral assembly mechanisms

被引:151
作者
Yeager, M
Wilson-Kubalek, EM
Weiner, SG
Brown, PO
Rein, A
机构
[1] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA
[2] NCI, Lab Mol Virol & Carcinogenesis, Adv Biosci Labs, Basic Res Program,Frederick Canc Res Facil, Frederick, MD 21702 USA
[3] Stanford Univ, Med Ctr, Howard Hughes Med Inst, Dept Biochem, Stanford, CA 94305 USA
关键词
image processing; retroviruses; virus assembly;
D O I
10.1073/pnas.95.13.7299
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
We have used electron cryo-microscopy and image analysis to examine the native structure of immature, protease-deficient (PR-) and mature, wild-type (WT) Moloney murine leukemia virus (MuLV). Maturational cleavage of the Gag polyprotein by the viral protease is associated with striking morphological changes. The PR- MuLV particles exhibit a rounded central core, which has a characteristic track-like shell on its surface, whereas the WT MuLV cores display a polygonal surface with loss of the track-like feature. The pleomorphic shape and inability to refine unique orientation angles suggest that neither the PR- nor the WT MuLV adheres to strict icosahedral symmetry. Nevertheless, the PR- MuLV particles do exhibit paracrystalline order with a spacing between Gag molecules of approximate to 45 Angstrom and a length of approximate to 200 Angstrom. Because of the pleomorphic shape and paracrystalline packing of the Gag-RNA complexes, we raise the possibility that assembly of MuLV is driven by protein-RNA, as well as protein-protein, interactions. The maturation process involves a dramatic reorganization of the packing arrangements within the ribonucleoprotein core with disordering and loosening of the individual protein components.
引用
收藏
页码:7299 / 7304
页数:6
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