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Title: Phosphatidic acid produced by phospholipase D promotes RNA replication of a plant RNA virus
Authors: Hyodo, Kiwamu
Taniguchi, Takako
Manabe, Yuki  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-5663-0074 (unconfirmed)
Kaido, Masanori  kyouindb  KAKEN_id
Mise, Kazuyuki  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0003-4348-6023 (unconfirmed)
Sugawara, Tatsuya  kyouindb  KAKEN_id  orcid https://orcid.org/0000-0002-1203-5521 (unconfirmed)
Taniguchi, Hisaaki
Okuno, Tetsuro
Author's alias: 三瀬, 和之
奥野, 哲郎
Issue Date: 28-May-2015
Publisher: Public Library of Science
Journal title: PLOS Pathogens
Volume: 11
Issue: 5
Thesis number: e1004909
Abstract: Eukaryotic positive-strand RNA [(+)RNA] viruses are intracellular obligate parasites replicate using the membrane-bound replicase complexes that contain multiple viral and host components. To replicate, (+)RNA viruses exploit host resources and modify host metabolism and membrane organization. Phospholipase D (PLD) is a phosphatidylcholine- and phosphatidylethanolamine-hydrolyzing enzyme that catalyzes the production of phosphatidic acid (PA), a lipid second messenger that modulates diverse intracellular signaling in various organisms. PA is normally present in small amounts (less than 1% of total phospholipids), but rapidly and transiently accumulates in lipid bilayers in response to different environmental cues such as biotic and abiotic stresses in plants. However, the precise functions of PLD and PA remain unknown. Here, we report the roles of PLD and PA in genomic RNA replication of a plant (+)RNA virus, Red clover necrotic mosaic virus (RCNMV). We found that RCNMV RNA replication complexes formed in Nicotiana benthamiana contained PLDα and PLDβ. Gene-silencing and pharmacological inhibition approaches showed that PLDs and PLDs-derived PA are required for viral RNA replication. Consistent with this, exogenous application of PA enhanced viral RNA replication in plant cells and plant-derived cell-free extracts. We also found that a viral auxiliary replication protein bound to PA in vitro, and that the amount of PA increased in RCNMV-infected plant leaves. Together, our findings suggest that RCNMV hijacks host PA-producing enzymes to replicate.
Rights: © 2015 Hyodo et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited
URI: http://hdl.handle.net/2433/213951
DOI(Published Version): 10.1371/journal.ppat.1004909
PubMed ID: 26020241
Appears in Collections:Journal Articles

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