Publication: The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5α
The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5α
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Morger, D., Zosel, F., Bühlmann, M., Züger, S., Mittelviefhaus, M., Schuler, B., Luban, J., & Grütter, M. G. (2018). The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5α. Journal of Virology, 92, e01541-17. https://doi.org/10.1128/JVI.01541-17
Abstract
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Rhesus TRIM5α (rhTRIM5α) potently restricts replication of human immunodeficiency virus type 1 (HIV-1). Restriction is mediated through direct binding of the C-terminal B30.2 domain of TRIM5α to the assembled HIV-1 capsid core. This host-pathogen interaction involves multiple capsid molecules within the hexagonal HIV-1 capsid lattice. However, the molecular details of this interaction and the precise site at which the B30.2 domain binds remain largely unknown. The human orthologue of TRIM5α (hsTRIM5α) fails to block infection by HIV-1
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- Morger, Damien
- Zosel, Franziska
- Bühlmann, Martin
- Züger, Sara
- Mittelviefhaus, Maximilian
- Schuler, Benjamin
- Luban, Jeremy
- Grütter, Markus G
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Morger, D., Zosel, F., Bühlmann, M., Züger, S., Mittelviefhaus, M., Schuler, B., Luban, J., & Grütter, M. G. (2018). The Three-Fold Axis of the HIV-1 Capsid Lattice Is the Species-Specific Binding Interface for TRIM5α. Journal of Virology, 92, e01541-17. https://doi.org/10.1128/JVI.01541-17
