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Structure and stoichiometry of template-directed recombinant HIV-1 Gag particles.


ABSTRACT: Size polydispersity of immature human immunodeficiency virus type 1 (HIV-1) particles represents a challenge for traditional methods of biological ultrastructural analysis. An in vitro model for immature HIV-1 particles constructed from recombinant Gag proteins lacking residues 16-99 and the p6 domain assembled around spherical nanoparticles functionalized with DNA. This template-directed assembly approach led to a significant reduction in size polydispersity and revealed previously unknown structural features of immature-like HIV-1 particles. Electron microscopy and image reconstruction of these particles suggest that the Gag shell formed from different protein regions that are connected by a "scar"-an extended defect connecting the edges of two continuous, regularly packed protein layers. Thus, instead of a holey protein array, the experimental model presented here appears to consist of a continuous array of ?5000 proteins enveloping the core, in which regular regions are separated by extended areas of disorder.

SUBMITTER: Goicochea NL 

PROVIDER: S-EPMC3140650 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Structure and stoichiometry of template-directed recombinant HIV-1 Gag particles.

Goicochea Nancy L NL   Datta Siddhartha A K SA   Ayaluru Murali M   Kao Cheng C   Rein Alan A   Dragnea Bogdan B  

Journal of molecular biology 20110701 4


Size polydispersity of immature human immunodeficiency virus type 1 (HIV-1) particles represents a challenge for traditional methods of biological ultrastructural analysis. An in vitro model for immature HIV-1 particles constructed from recombinant Gag proteins lacking residues 16-99 and the p6 domain assembled around spherical nanoparticles functionalized with DNA. This template-directed assembly approach led to a significant reduction in size polydispersity and revealed previously unknown stru  ...[more]

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