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The TRIpartite Motif (TRIM) proteins play key roles in cell differentiation, apoptosis, development, autophagy, and innate immunity in vertebrates. In the present study, a novel TRIM9 homolog (designated as  LvTRIM9-1 ) specifically expressed in the lymphoid organ of shrimp was identified from the Pacific whiteleg shrimp  Litopenaeus vannamei . Its deduced amino acid sequence possesses the typical features of TRIM proteins, including a RING domain, two B-boxes, a coiled-coil domain, a FN3 domain, and a SPRY domain. The transcripts of  LvTRIM9-1  were mainly located in the lymphoid tubules of the lymphoid organ. Knockdown of  LvTRIM9-1  could apparently inhibit the transcriptions of some genes from white spot syndrome virus (WSSV) and reduce the viral propagation in the lymphoid organ. Overexpression of  LvTRIM9-1  in mammalian cells could activate the promoter activity  of NF-κB, and an  in vivo  experiment in shrimp showed that knockdown of  LvTRIM9-1  reduced the expression of  LvRelish  in the lymphoid organ. Yeast two-hybridization and co-immunoprecipitation (Co-IP) assays confirmed that LvTRIM9-1 could directly interact with LvIMD, a key component of the IMD pathway, through its SPRY domain. These data suggest that LvTRIM9-1 could activate the IMD pathway in shrimp  via  interaction with LvIMD. This is the first evidence to show the regulation of a TRIM9 protein on the IMD pathway through its direct interaction with IMD, which will enrich our knowledge on the role of TRIM proteins in innate immunity of invertebrates.

A Novel TRIM9 Protein Promotes NF-κB Activation Through Interacting With LvIMD in Shrimp During WSSV Infection