Abstract
Emerging evidence suggests that the tripartite motif containing 62 (TRIM62), a member of the TRIM family, plays an important role in antiviral processes. The objective of the study was to explore the role of TRIM62 in reticuloendotheliosis virus (REV) infection and its potential molecular mechanism. We first demonstrated that the REV infection affected the TRIM62 expression first upregulated and then downregulated in CEF cells. Next, we evaluated the effect of TRIM62 on viral replication. Overexpression of TRIM62 decreased REV replication. On the contrary, silencing of endogenously expressed TRIM62 increased viral replication. Then, to explore the necessity of domains in TRIM62's negative regulation on viral replication, we transfected CEF cells with TRIM62 domain deletion mutants. Deletion domain partially abolished TRIM62's antiviral activity. The effect of SPRY domain deletion was the highest and that of coiled-coil was the lowest. Further, we identified 18 proteins that coimmunoprecipitated and interacted with TRIM62 by immunocoprecipitation and mass spectrometry analysis. Strikingly, among which, both Ras-related protein Rab-5b (RAB5B) and Arp2/3 complex 34-kDa subunit (ARPC2) were involved in actin cytoskeletal pathway. Altogether, these results strongly suggest that chicken TRIM62 provides host defense against viral infection, and all domains are required for its action. RAB5B and ARPC2 may play important roles in its negative regulation processes.
Highlights
tripartite motif containing 62 (TRIM62) is a member of the TRIM family proteins and is known as DEAR1 [1]
Time course infection of reticuloendotheliosis virus (REV) in CEF cells showed that the REV mRNA levels were significantly increased (p < 0.001) from 48 to 96 h post-infection (Figure 1A), and the TRIM62 mRNA levels were significantly upregulated at 48 h (p < 0.1) and 72 h (p < 0.1) as compared to that in uninfected CEF cells
The protein levels of REV and TRIM62 were detected by WB, which were consistent with the dynamic changes of mRNA levels
Summary
TRIM62 (tripartite motif containing 62) is a member of the TRIM family proteins and is known as DEAR1 (ductal epithelium-associated RING chromosome) [1]. TRIM family proteins, known as RBCC proteins, contain conserved RING finger, B-box, coiled-coil domains, and a variable C terminus [2]. Despite their common domain structure, TRIM proteins play critical roles in distinct cellular processes such as intercellular signaling, innate immunity, transcription, autophagy, and carcinogenesis [3, 4]. Members of the TRIM family of E3 ligases exhibit antiviral activities [5, 6]. Expression of low amounts of TRIM62 enhanced HIV gene expression and release, and the E3 mutant of TRIM62 inhibited HIV release more potently than the wild-type
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