Abstract
The ubiquitin-proteasome system (UPS) has been recognized for regulating fundamental cellular processes, followed by induction of proteasomal degradation of target proteins, and triggers multiple signaling pathways that are crucial for numerous aspects of cellular physiology. Especially tripartite motif (TRIM) proteins, well-known E3 ubiquitin ligases, emerge as having critical roles in several antiviral signaling pathways against varying viral infections. Here we highlight recent advances in the study of antiviral roles of TRIM proteins toward influenza virus infection in terms of the modulation of pathogen recognition receptor (PRR)-mediated innate immune sensing, direct obstruction of influenza viral propagation, and participation in virus-induced autophagy.
Highlights
Influenza virus is an enveloped RNA virus that harbors a genome comprising eight segments of negative-sense, single-stranded RNA encoding at least ten distinct proteins [1]
Given that the machinery by which ubiquitin is transferred from E2 to a substrate by E3 ligases, their superfamily is divided into three major groups: Really Interesting New Gene (RING), Homologous to E6-associated protein C Terminus (HECT) domains, and RING-in-between-RING (RBR) [27,28,29,30]
The tripartite motif (TRIM) proteins play a crucial role in regulating viral infection and the antiviral strategies which are classified by three broad categories: (1) modulation of pathogen recognition receptor (PRR)-mediated innate immune sensing, (2) direct obstruction of viral propagation, and (3) virus-induced autophagy
Summary
Influenza virus is an enveloped RNA virus that harbors a genome comprising eight segments of negative-sense, single-stranded RNA encoding at least ten distinct proteins [1]. When a virus enters the cells through recognition of the sialic acid-terminating glycan receptors by the viral hemagglutinin (HA) glycoprotein, vRNP complexes are released into the cytoplasm through the endocytic pathway, subsequently delivered into the nucleus for their replication [3,4]. At this initiation step, low endosomal pH stimulates membrane fusion mediated by the hemagglutinin 2 protein (HA2), and activates the M2 proton channel, driving cytoplasmic release of vRNPs from the inner shell of the viral matrix protein 1 (M1) [5,6]. This review will focus on how the influenza virus utilizes the TRIM proteins to escape TRIM-mediated antiviral action for propagation
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