Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2015;129:167-87.
doi: 10.1016/bs.pmbts.2014.10.006. Epub 2014 Dec 12.

TRIM21-dependent Intracellular Antibody Neutralization of Virus Infection

Affiliations
Review

TRIM21-dependent Intracellular Antibody Neutralization of Virus Infection

William A McEwan et al. Prog Mol Biol Transl Sci. .

Abstract

The ability of antibodies to prevent viral infection has long been recognized. In vitro neutralization assays, which take place in the absence of professional immune effector mechanisms, have demonstrated that the process of neutralization can occur by a variety of molecular mechanisms. Most known mechanisms involve the blocking of an event essential for infection, for instance, the steric inhibition of attachment to entry receptors. As such, neutralization is often thought of as a passive process that can occur without the need for host effector machinery. In contrast to this view, it has recently been demonstrated that neutralization can depend on the widely expressed cytosolic Fc binding protein TRIM21. This unique and novel Ig receptor directs the ubiquitin and proteasome-dependent degradation of intracellular antibody-bound viral particles and prevents infection. It has been further demonstrated that detection of cytosolic antibody by TRIM21 activates inflammatory signaling pathways and promotes the production of cytokines and chemokines. Studies in a TRIM21-null mouse demonstrate the importance of these activities: homozygous knockouts suffer fatal viral infection where wild-type mice survive. Though there is much to be learned about the role of TRIM21 in immunity, it is clear that there is a hitherto unappreciated role for antibodies in the intracellular environment.

Keywords: ADIN; Antibody; Neutralization; TRIM21.

Similar articles

See all similar articles

Cited by 7 articles

See all "Cited by" articles

Publication types

LinkOut - more resources

Feedback