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TRIM5α Restricts Flavivirus Replication by Targeting the Viral Protease for Proteasomal Degradation. 2019
Abhilash I Chiramel, and
Nicholas R Meyerson, and
Kristin L McNally, and
Rebecca M Broeckel, and
Vanessa R Montoya, and
Omayra Méndez-Solís, and
Shelly J Robertson, and
Gail L Sturdevant, and
Kirk J Lubick, and
Vinod Nair, and
Brian H Youseff, and
Robin M Ireland, and
Catharine M Bosio, and
Kyusik Kim, and
Jeremy Luban, and
Vanessa M Hirsch, and
R Travis Taylor, and
Fadila Bouamr, and
Sara L Sawyer, and
Sonja M Best
Innate Immunity and Pathogenesis Section, Laboratory of Virology, Rocky Mountain Laboratories (RML), National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health (NIH), Hamilton, MT 59840, USA.
Tripartite motif-containing protein 5α (TRIM5α) is a cellular antiviral restriction factor that prevents early events in retrovirus replication. The activity of TRIM5α is thought to be limited to retroviruses as a result of highly specific interactions with capsid lattices. In contrast to this current understanding, we show that both human and rhesus macaque TRIM5α suppress replication of specific flaviviruses. Multiple viruses in the tick-borne encephalitis complex are sensitive to TRIM5α-dependent restriction, but mosquito-borne flaviviruses, including yellow fever, dengue, and Zika viruses, are resistant. TRIM5α suppresses replication by binding to the viral protease NS2B/3 to promote its K48-linked ubiquitination and proteasomal degradation. Importantly, TRIM5α contributes to the antiviral function of IFN-I against sensitive flaviviruses in human cells. Thus, TRIM5α possesses remarkable plasticity in the recognition of diverse virus families, with the potential to influence human susceptibility to emerging flaviviruses of global concern.
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