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Global Reprogramming of Host SUMOylation during Influenza Virus Infection.

Abstract：

:Dynamic nuclear SUMO modifications play essential roles in orchestrating cellular responses to proteotoxic stress, DNA damage, and DNA virus infection. Here, we describe a non-canonical host SUMOylation response to the nuclear-replicating RNA pathogen, influenza virus, and identify viral RNA polymerase activity as a major contributor to SUMO proteome remodeling. Using quantitative proteomics to compare stress-induced SUMOylation responses, we reveal that influenza virus infection triggers unique re-targeting of SUMO to 63 host proteins involved in transcription, mRNA processing, RNA quality control, and DNA damage repair. This is paralleled by widespread host deSUMOylation. Depletion screening identified ten virus-induced SUMO targets as potential antiviral factors, including C18orf25 and the SMC5/6 and PAF1 complexes. Mechanistic studies further uncovered a role for SUMOylation of the PAF1 complex component, parafibromin (CDC73), in potentiating antiviral gene expression. Our global characterization of influenza virus-triggered SUMO redistribution provides a proteomic resource to understand host nuclear SUMOylation responses to infection.

journal_name

Cell Rep

journal_title

Cell reports

authors

Domingues P,Golebiowski F,Tatham MH,Lopes AM,Taggart A,Hay RT,Hale BG

doi

10.1016/j.celrep.2015.10.001

subject

Has Abstract

pub_date

2015-11-17 00:00:00

pages

1467-1480

issue

7

issn

2211-1247

pii

S2211-1247(15)01139-0

journal_volume

13

pub_type

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