Key result
TRIM22 is an evolutionarily ancient protein that restricts the replication of several viruses, including EMCV, HBV, and HIV-1, and may play a role in cellular differentiation, cancers, and autoimmune diseases.
This review summarizes the structure and function of TRIM22, highlighting its role in viral restriction, cellular differentiation, and potential implications in cancer and autoimmune diseases.
TRIM22's antiviral roles merit targeted research; leaves open clinical translation in infection, cancer, and autoimmunity.
The tripartite motif (TRIM) family of proteins is an evolutionarily ancient group of proteins with homologues identified in both invertebrate and vertebrate species. Human TRIM22 is one such protein that has a dynamic evolutionary history that includes gene expansion, gene loss, and strong signatures of positive selection. To date, TRIM22 has been shown to restrict the replication of a number of viruses, including encephalomyocarditis virus (EMCV), hepatitis B virus (HBV), and human immunodeficiency virus type 1 (HIV-1). In addition, TRIM22 has also been implicated in cellular differentiation and proliferation and may play a role in certain cancers and autoimmune diseases. This comprehensive paper summarizes our current understanding of TRIM22 structure and function.
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Hattlmann et al. (2012) conducted a review in Viral infections. TRIM22 was evaluated. TRIM22 is an evolutionarily ancient protein that restricts the replication of several viruses, including EMCV, HBV, and HIV-1, and may play a role in cellular differentiation, cancers, and autoimmune diseases.
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