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Regulation of Virus Neutralization and the Persistent Fraction by TRIM21

McEwan, W. A.; Hauler, F.; Williams, C. R.; Bidgood, S. R.; Mallery, D. L.; Crowther, R. A.; James, L. C.. 2012 Regulation of Virus Neutralization and the Persistent Fraction by TRIM21. Journal of Virology, 86 (16). 8482-8491. 10.1128/JVI.00728-12

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Abstract/Summary

Despite a central role in immunity, antibody neutralization of virus infection is poorly understood. Here we show how the neutralization and persistence of adenovirus type 5, a prevalent nonenveloped human virus, are dependent upon the intracellular antibody receptor TRIM21. Cells with insufficient amounts of TRIM21 are readily infected, even at saturating concentrations of neutralizing antibody. Conversely, high TRIM21 expression levels decrease the persistent fraction of the infecting virus and allows neutralization by as few as 1.6 antibody molecules per virus. The direct interaction between TRIM21 and neutralizing antibody is essential, as single-point mutations within the TRIM21-binding site in the Fc region of a potently neutralizing antibody impair neutralization. However, infection at high multiplicity can saturate TRIM21 and overcome neutralization. These results provide insight into the mechanism and importance of a newly discovered, effector-driven process of antibody neutralization of nonenveloped viruses.

Item Type: Publication - Article
Digital Object Identifier (DOI): 10.1128/JVI.00728-12
Programmes: BAS Programmes > Polar Science for Planet Earth (2009 - ) > Ice Sheets
ISSN: 0022-538X
NORA Subject Terms: Biology and Microbiology
Date made live: 09 Jul 2014 11:50 +0 (UTC)
URI: http://nora.nerc.ac.uk/id/eprint/507782

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