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PNAS: NLRX1 prevents mitochondrial induced apoptosis and enhances macrophage antiviral immunity by interacting with influenza virus PB1-F2 protein

tetano

Editor, Senior Moderator
NLRX1 prevents mitochondrial induced apoptosis and enhances macrophage antiviral immunity by interacting with influenza virus PB1-F2 protein

Joanna Jaworskaa,
Fran?ois Coulombea,
Jeffrey Downeya,
Fanny Tzelepisa,
Karim Shalabya,
Ivan Tattolib,
Julie Berubea,
Simon Rousseaua,
James G. Martina,
Stephen E. Girardinb,
Jonathan A. McCullersc,d, and
Maziar Divangahia,1

Author Affiliations

Edited by Peter Palese, Icahn School of Medicine at Mount Sinai, New York, NY, and approved April 11, 2014 (received for review November 26, 2013)

Abstract
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Significance

Apoptosis refers to the ability of a cell to undergo programmed cell death under normal physiological conditions or in response to stress signals. During infection, influenza A viruses have the capacity to induce early apoptosis of immune cells, thereby preventing them from performing their antiviral function. In this study, we identified that a host innate immune sensor [NLRX1 (nucleotide-binding oligomerization domain-like receptor X1)] has the capacity to bind a small death-inducing protein from influenza A virus [PB1-F2 (polymerase basic protein 1-frame 2)] and defend immune cells against virus-driven apoptosis. This phenomenon allows the immune cells to survive longer and effectively restrict viral replication, protecting the host against the detrimental consequences of influenza.
Abstract

To subvert host immunity, influenza A virus (IAV) induces early apoptosis in innate immune cells by disrupting mitochondria membrane potential via its polymerase basic protein 1-frame 2 (PB1-F2) accessory protein. Whether immune cells have mechanisms to counteract PB1-F2?mediated apoptosis is currently unknown. Herein, we define that the host mitochondrial protein nucleotide-binding oligomerization domain-like receptor (NLR)X1 binds to viral protein PB1-F2, preventing IAV-induced macrophage apoptosis and promoting both macrophage survival and type I IFN signaling. We initially observed that Nlrx1-deficient mice infected with IAV exhibited increased pulmonary viral replication, as well as enhanced inflammatory-associated pulmonary dysfunction and morbidity. Analysis of the lungs of IAV-infected mice revealed markedly enhanced leukocyte recruitment but impaired production of type I IFN in Nlrx1−/− mice. Impaired type I IFN production and enhanced viral replication was recapitulated in Nlrx1−/− macrophages and was associated with increased mitochondrial mediated apoptosis. Through gain- and loss-of-function strategies for protein interaction, we identified that NLRX1 directly bound PB1-F2 in the mitochondria of macrophages. Using a recombinant virus lacking PB1-F2, we confirmed that deletion of PB1-F2 abrogated NLRX1-dependent macrophage type I IFN production and apoptosis. Thus, our results demonstrate that NLRX1 acts as a mitochondrial sentinel protecting macrophages from PB1-F2?induced apoptosis and preserving their antiviral function. We further propose that NLRX1 is critical for macrophage immunity against IAV infection by sensing the extent of viral replication and maintaining a protective balance between antiviral immunity and excessive inflammation within the lungs.


http://www.pnas.org/content/early/2...ract?sid=1ac368bc-80f3-4de8-a7bf-79b1f3c66b94
 
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