Key result
Coxsackievirus B3 3C protease cleaves the host antiviral protein TRIM7 at glutamine 24, dampening its E3 ubiquitin ligase activity and impairing its ability to restrict viral infection.
Why the study?
Understanding how the host controls enteroviruses and how these viruses evade host restriction is important for informing potential therapeutic interventions against viral myocarditis and other conditions.
Coxsackievirus B3 uses its 3C protease to cleave the host antiviral protein TRIM7, dampening host immunity and revealing a mechanism of viral immune evasion relevant to viral myocarditis.
Suggests immune evasion mechanism in viral myocarditis models; hypothesis-generating for TRIM7-targeted interventions pending human data.
Enteroviruses are significant human pathogens that cause viral myocarditis, pancreatitis, and meningitis. Knowing how the host controls these viruses and how the viruses may evade host restriction is important for understanding fundamental concepts in antiviral immunity and for informing potential therapeutic interventions. In this study, we demonstrate that coxsackievirus B3 uses its virally encoded protease to target the host antiviral protein TRIM7 for cleavage, suggesting a potential mechanism of viral immune evasion. We additionally show that TRIM7 has evolved in certain mammalian lineages to express protein variants with distinct antiviral activities and susceptibilities to viral protease-mediated cleavage.
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Fan et al. (2022) studied Enterovirus infection. Enterovirus 3C protease was evaluated on TRIM7 cleavage and antiviral activity. Coxsackievirus B3 3C protease cleaves the host antiviral protein TRIM7 at glutamine 24, dampening its E3 ubiquitin ligase activity and impairing its ability to restrict viral infection.
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