Retrovirus envelope protein complex structure in situ studied by cryo-electron tomography.

Abstract:

:We used cryo-electron tomography in conjunction with single-particle averaging techniques to study the structures of frozen-hydrated envelope glycoprotein (Env) complexes on intact Moloney murine leukemia retrovirus particles. Cryo-electron tomography allows 3D imaging of viruses in toto at a resolution sufficient to locate individual macromolecules, and local averaging of abundant complexes substantially improves the resolution. The averaging of repetitive features in electron tomograms is hampered by a low signal-to-noise ratio and anisotropic resolution, which results from the "missing-wedge" effect. We developed an iterative 3D averaging algorithm that compensates for this effect and used it to determine the trimeric structure of Env to a resolution of 2.7 nm, at which individual domains can be resolved. Strikingly, the 3D reconstruction is shaped like a tripod in which the trimer penetrates the membrane at three distinct locations approximately 4.5 nm apart from one another. The Env reconstruction allows tentative docking of the x-ray crystal structure of the receptor-binding domain. This study thus provides 3D structural information regarding the prefusion conformation of an intact unstained retrovirus surface protein.

authors

Förster F,Medalia O,Zauberman N,Baumeister W,Fass D

doi

10.1073/pnas.0409178102

keywords:

subject

Has Abstract

pub_date

2005-03-29 00:00:00

pages

4729-34

issue

13

eissn

0027-8424

issn

1091-6490

pii

0409178102

journal_volume

102

pub_type

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