RNA- and Virus-Independent Inhibition of Antiviral Signaling by RNA Helicase LGP2

Komuro, Akihiko; Horvath, Curt M.

doi:10.1128/jvi.01325-06

Cited by 262 publications

(264 citation statements)

References 30 publications

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“…Both RIG-I and MDA5 utilize a common adaptor molecule termed MAVS 29 , IPS-1 30 , Cardif 31 , or VISA 32 , which was independently identified by multiple groups and localizes to the mitochondrial membrane 29 . The third member of the family, lgp2, displays sequence homology to the helicase domains of RIG-I and MDA5, however lacks a CARD, domain and therefore serves as a negative regulator of both sensors [33][34][35] . Interestingly, a recent report suggests that lgp2 may play both a positive and negative regulatory role in RIG-I and MDA5-mediated innate immunity 36 .…”

Section: Non-tlr-mediated Viral Recognitionmentioning

confidence: 99%

Toll-like receptors regulation of viral infection and disease☆

Thompson

Iwasaki

2008

Advanced Drug Delivery Reviews

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In recent years, it has become increasingly evident that mammalian Toll-like receptors (TLRs) play a critical role in determining the outcome of virus infection. TLRs have evolved to recognize viral nucleic acids, and promote the stimulation of innate and adaptive immune responses. Interestingly, the study of mice harboring deficiencies in various TLR proteins and their adaptors suggests that TLR activation promotes protective anti-viral immunity in some cases, while exacerbating virusinduced disease in others. In this report we describe the interactions of viruses with both the TLR system and the intracellular recognition system and highlight the role of TLRs in shaping the outcome of virus infection in both a positive and negative manner.

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Section: Non-tlr-mediated Viral Recognitionmentioning

confidence: 99%

Toll-like receptors regulation of viral infection and disease☆

Thompson

Iwasaki

2008

Advanced Drug Delivery Reviews

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“…RLRs including RIG-I, melanoma differentiation factor 5 (MDA5) and laboratory of genetics and physiology 2 (LGP2) reside in the cellular cytoplasm, whereas TLRs are located on the plasma membrane or at the endosomal surface [2,[6][7][8][9]. Structurally, all three RLRs contain a DExD-box RNA helicase domain for RNA binding and with the exception of LGP2, also possess a caspase recruitment domain (CARD) that mediates downstream protein-protein interactions.…”

Section: Introductionmentioning

confidence: 99%

A functional C-terminal TRAF3-binding site in MAVS participates in positive and negative regulation of the IFN antiviral response

et al. 2011

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“…To prevent autonomous production of type I IFNs or overproduction of these cytokines following viral infection, which causes a pathological immune response, the cell has evolved distinct strategies to tightly regulate their expression. It has been shown that LGP2, a helicase protein lacking CARDs at its N-terminus, acts as a negative regulator by sequestering viral RNA from RIG-I [18][19][20][21].…”

Section: Introductionmentioning

confidence: 99%