What is it about?

Understanding how viruses overcome the host's innate defenses to efficiently spread is crucial in the fight against infections. Here, we deciphered a non-canonical autophagy pathway that is exploited by HIV-1 (human immunodeficiency virus type 1) to overcome a viral restriction factor called BST2/Tetherin. Through advanced microscopy and biochemical approaches, we discovered that an autophagic protein called ATG5 selectively engages BST2 trapping viruses at the cell surface, directing them towards this non-canonical autophagy pathway for degradation. We also found that this non-canonical autophagy pathway is used by HIV-1 to attenuate the inflammatory responses mediated by BST2 virion retention.

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Why is it important?

BST2/Tetherin has a broad restriction activity against various enveloped viruses. These discoveries are likely to have implications for research on many enveloped viruses, or on extracellular elements trapped by BST2 at the surface of cells (such as exosomes or midbodies).


In this study, we made a novel finding regarding the protein ATG5. We identified an additional function of ATG5 beyond its known role in the canonical autophagy pathway, wherein it acts as an adaptor for membrane receptors. This discovery presents exciting opportunities for further investigation into the involvement of ATG5 in engaging surface receptors in the non-canonical autophagy pathway.

Clarisse Berlioz-Torrent

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This page is a summary of: ATG5 selectively engages virus-tethered BST2/tetherin in an LC3C-associated pathway, Proceedings of the National Academy of Sciences, May 2023, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2217451120.
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