Journal
MEDCOMM
Volume 2, Issue 4, Pages 798-809Publisher
WILEY
DOI: 10.1002/mco2.92
Keywords
endocytic trafficking; endosome; host-pathogen interaction; S protein; SARS-CoV-2
Categories
Funding
- Natural Science Foundation of China [91854121, 31871429, 82073404]
- National Science Fund for Distinguished Young Scholars [32125012]
- National Key R&D Program of China [2018YFC1005004]
- Sichuan Science and Technology Program [2018RZ0128]
- COVID-19 of West China Hospital [HX-2019-nCoV-064]
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Research has shown that SARS-CoV-2 utilizes the interaction between SNX27 and the S protein to facilitate the expression of viral surface proteins, with the S protein binding to the PDZ domain of SNX27 for this process.
SARS-CoV-2 is an enveloped positive-sense RNA virus that depends on host factors for all stages of its life. Membrane receptor ACE2 is a well-established factor for SARS-CoV-2 docking. In addition to ACE2, whole-genome genetic screens have identified additional proteins, such as endosomal trafficking regulators SNX27 and retromer, as key host factors required for SARS-CoV-2 infection. However, it is poorly understood how SARS-CoV-2 utilize host endocytic transport pathways to produce productive infection. Here, we report that SNX27 interacts with the SARS-CoV-2 spike (S) protein to facilitate S protein surface expression. Interestingly, S protein binds to the PDZ domain of SNX27, although it does not contain a PDZ-binding motif (PDZbm). Either abrogation of the SNX27 PDZ domain or S protein MTSC motif, which is critical for SNX27 binding, decreases surface expression of S protein and viral production. Collectively, our study highlights a novel approach utilized by SARS-CoV-2 to facilitate virion trafficking to establish virus infection.
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