Title

More than one way to TRIM a capsid

UMMS Affiliation

Program in Molecular Medicine

Publication Date

11-27-2012

Document Type

Response or Comment

Disciplines

Biochemistry | Immunology of Infectious Disease | Molecular Biology | Virology | Viruses

Abstract

Antibodies protect against lethal infection by bacteria or nonenveloped viruses such as adenovirus (1). They are secreted by plasma cells at the rate of thousands of molecules per second, and it has long been assumed that they function exclusively in the extracellular milieu. The recent discovery of a cytoplasmic process called antibody-dependent intracellular neutralization (ADIN) put an end to this dogma: virion-associated antibodies that fail to prevent virus entry into susceptible target cells have a second chance to block infection from within the target cell cytoplasm (2). In PNAS, Hauler et al. (3) generate a din of excitement by showing that the host AAA ATPase valosin-containing protein (VCP) cooperates with the E3 ubiquitin ligase tripartite motif-containing protein 21 (TRIM21) to dismantle the antibody-coated virion, thus permitting the proteasome access to the building block proteins of the virion capsid.

DOI of Published Version

10.1073/pnas.1217596109

Source

Proc Natl Acad Sci U S A. 2012 Nov 27;109(48):19517-8. doi: 10.1073/pnas.1217596109. Epub 2012 Nov 13. Link to article on publisher's site

Journal/Book/Conference Title

Proceedings of the National Academy of Sciences of the United States of America

Related Resources

Link to Article in PubMed

PubMed ID

23150592

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