Amino acid requirements for MDA5 and LGP2 recognition by paramyxovirus V proteins: A single arginine distinguishes MDA5 from RIG-I

Kenny R. Rodriguez, Curt M. Horvath*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Paramyxovirus V proteins bind to MDA5 (melanoma differentiation-associated gene 5) and LGP2 (laboratory of genetics and physiology gene 2) but not RIG-I (retinoic acid-inducible gene I). The results demonstrate MDA5 R806 is essential for inhibition by diverse V proteins. Complementary substitution for the analogous RIG-I L714 confers V protein recognition. The analogous LGP2 R455 is required for recognition by measles V protein, but not other V proteins. These findings indicate that paramyxoviruses use a single amino acid to distinguish MDA5 from RIG-I and have evolved distinct contact sites for LGP2 interference.

Original languageEnglish (US)
Pages (from-to)2974-2978
Number of pages5
JournalJournal of virology
Volume87
Issue number5
DOIs
StatePublished - Mar 2013

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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