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NLRX1 protein attenuates inflammatory responses to infection by interfering with the RIG-I-MAVS and TRAF6-NF-κB signaling pathways.

Abstract：

:The nucleotide-binding domain and leucine-rich-repeat-containing (NLR) proteins regulate innate immunity. Although the positive regulatory impact of NLRs is clear, their inhibitory roles are not well defined. We showed that Nlrx1(-/-) mice exhibited increased expression of antiviral signaling molecules IFN-β, STAT2, OAS1, and IL-6 after influenza virus infection. Consistent with increased inflammation, Nlrx1(-/-) mice exhibited marked morbidity and histopathology. Infection of these mice with an influenza strain that carries a mutated NS-1 protein, which normally prevents IFN induction by interaction with RNA and the intracellular RNA sensor RIG-I, further exacerbated IL-6 and type I IFN signaling. NLRX1 also weakened cytokine responses to the 2009 H1N1 pandemic influenza virus in human cells. Mechanistically, Nlrx1 deletion led to constitutive interaction of MAVS and RIG-I. Additionally, an inhibitory function is identified for NLRX1 during LPS activation of macrophages where the MAVS-RIG-I pathway was not involved. NLRX1 interacts with TRAF6 and inhibits NF-κB activation. Thus, NLRX1 functions as a checkpoint of overzealous inflammation.

journal_name

Immunity

journal_title

Immunity

authors

Allen IC,Moore CB,Schneider M,Lei Y,Davis BK,Scull MA,Gris D,Roney KE,Zimmermann AG,Bowzard JB,Ranjan P,Monroe KM,Pickles RJ,Sambhara S,Ting JP

doi

10.1016/j.immuni.2011.03.026

subject

Has Abstract

pub_date

2011-06-24 00:00:00

pages

854-65

issue

6

eissn

1074-7613

issn

1097-4180

pii

S1074-7613(11)00226-3

journal_volume

34

pub_type

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