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    Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ

    Zanetti, Giulia and Briggs, J.A. and Grunewald, K. and Sattentau, Q.J. and Fuller, S.D. (2006) Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ. PLoS Pathogens 2 , ISSN 1553-7374.

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    Abstract

    The envelope glycoprotein (Env) complexes of the human and simian immunodeficiency viruses (HIV and SIV, respectively) mediate viral entry and are a target for neutralizing antibodies. The receptor binding surfaces of Env are in large part sterically occluded or conformationally masked prior to receptor binding. Knowledge of the unliganded, trimeric Env structure is key for an understanding of viral entry and immune escape, and for the design of vaccines to elicit neutralizing antibodies. We have used cryo-electron tomography and averaging to obtain the structure of the SIV Env complex prior to fusion. Our result reveals novel details of Env organisation, including tight interaction between monomers in the gp41 trimer, associated with a three-lobed, membrane-distal gp120 trimer. A cavity exists at the gp41–gp120 trimer interface. Our model for the spike structure agrees with previously predicted interactions between gp41 monomers, and furthers our understanding of gp120 interactions within an intact spike.

    Metadata

    Item Type: Article
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Depositing User: Sarah Hall
    Date Deposited: 20 May 2019 10:45
    Last Modified: 02 Aug 2023 17:51
    URI: https://eprints.bbk.ac.uk/id/eprint/27571

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