Abstract
Tripartite motif-containing protein 32 (TRIM32) belongs to the tripartite motif (TRIM) family, which consists of a large number of proteins containing a RING (Really Interesting New Gene) domain, one or two B-box domains, and coiled coil motif followed by different C-terminal domains. The TRIM family is known to be implicated in multiple cellular functions, including antiviral activity. However, it is presently unknown whether TRIM32 of common carp (Cyprinus carpio) has the antiviral effect. In this study, the sequence, expression, and antiviral function of TRIM32 homolog from common carp were analyzed. The full-length coding sequence region of trim32 was cloned from common carp. The results showed that the expression of TRIM32 (mRNA) was highest in the brain, remained stably expressed during embryonic development, and significantly increased following spring viraemia of carp virus (SVCV) infection. Transient overexpression of TRIM32 in affected Epithelioma papulosum cyprinid cells led to significant decrease of SVCV production as compared to the control group. These results suggested a potentially important role of common carp TRIM32 in enhancing host immune response during SVCV infection both in vivo and in vitro.
Highlights
The tripartite motif (TRIM) family contains an N-terminal E3 ubiquitin ligase RING domain followed by one or two zinc-binding motifs named B-box; a predicted coiled coil (CC) region; and a variable C-terminus, such as a PRY/SPRY domain, known as the B30.2 domain, or the NHL (NCL-1/HT2A/Lin-41 repeat) domain [1]
The TRIMs have been implicated in various antiviral effect [1,8] and our results were in agreement with these previous findings and suggested that common carp Tripartite motif-containing protein 32 (TRIM32) played a role in carp fish defense against viral infection or in brain development
Fertilized carp eggs were used to determine TRIM32 expression at various developmental stages and our results showed that the expression of TRIM32 was detected in all the experimental stages; the expression was stable throughout the early development
Summary
The tripartite motif (TRIM) family contains an N-terminal E3 ubiquitin ligase RING domain followed by one or two zinc-binding motifs named B-box; a predicted coiled coil (CC) region; and a variable C-terminus, such as a PRY/SPRY domain, known as the B30.2 domain, or the NHL (NCL-1/HT2A/Lin-41 repeat) domain [1]. Van der Aa et al identified some multigene subsets of TRIM genes, a unique feature of fish [11] This group conducted a hierarchical clustering analysis and identified 16 finTRIM clusters, which were up- or downregulated following viral hemorrhagic septicemia virus (VHSV) infection [12]. A recent study has indicated that Epinephelus coioides TRIM39 (EcTRIM39) plays an important role in cell cycle progression, and possibly inhibits fish virus replication by acting as a regulator of innate immune response against fish viruses [13]. We describe the inhibitory role of TRIM32 in common carp against SVCV infection, and have defined such a role in downregulating viral replication These new findings suggest a possible important role of TRIM32 in host immune response against viral infection in fish
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