PINLYP-mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection.

Many viruses alter the phospholipid metabolism to benefit their own life cycles. It is unclear whether the host or the virus is driving phospholipid metabolism reprogramming, and how virus infections are affected by the metabolic status. Here we report that phospholipase A2 inhibitor and LY6/PLAUR d...

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Main Authors: Zhangmengxue Lei, Wendi Wei, Mingyu Wang, Yun Xu, Lei Bai, Ying Gao, Congwei Jiang, Fangxia Li, Na Tian, Linlin Kuang, Ruiliang Zhu, Gang Pang, Ke Lan, Suihan Feng, Xiaozhen Liang
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2025-05-01
Series:PLoS Pathogens
Online Access:https://doi.org/10.1371/journal.ppat.1013146
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author Zhangmengxue Lei
Wendi Wei
Mingyu Wang
Yun Xu
Lei Bai
Ying Gao
Congwei Jiang
Fangxia Li
Na Tian
Linlin Kuang
Ruiliang Zhu
Gang Pang
Ke Lan
Suihan Feng
Xiaozhen Liang
author_facet Zhangmengxue Lei
Wendi Wei
Mingyu Wang
Yun Xu
Lei Bai
Ying Gao
Congwei Jiang
Fangxia Li
Na Tian
Linlin Kuang
Ruiliang Zhu
Gang Pang
Ke Lan
Suihan Feng
Xiaozhen Liang
author_sort Zhangmengxue Lei
collection DOAJ
description Many viruses alter the phospholipid metabolism to benefit their own life cycles. It is unclear whether the host or the virus is driving phospholipid metabolism reprogramming, and how virus infections are affected by the metabolic status. Here we report that phospholipase A2 inhibitor and LY6/PLAUR domain-containing protein (PINLYP) inhibits Kaposi's sarcoma-associated herpesvirus (KSHV) lytic reactivation by remodeling phospholipid metabolism and especially triacylglycerol (TAG) biosynthesis. PINLYP deficiency led to increased phospholipase cPLA2α activity, cPLA2α-mediated AKT phosphorylation, and KSHV lytic reactivation. Analyses of RNA-seq and lipidomics reveal that PINLYP regulates long-chain fatty acid CoA ligase ACSL5 expression and TAG production. The inhibition of ACSL5 activity or TAG biosynthesis suppresses AKT phosphorylation and KSHV lytic reactivation, restoring the phenotype of PINLYP deficiency. This finding underscores the pivotal role of PINLYP in remodeling phospholipid metabolism and promoting viral latency, which sheds new light on how phospholipid metabolism is regulated by herpesvirus and provides a potential target for controlling chronic herpesvirus infection.
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institution DOAJ
issn 1553-7366
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language English
publishDate 2025-05-01
publisher Public Library of Science (PLoS)
record_format Article
series PLoS Pathogens
spelling doaj-art-ea47968009a34590a55c42ee5c16bb0b2025-08-20T03:13:39ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742025-05-01215e101314610.1371/journal.ppat.1013146PINLYP-mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection.Zhangmengxue LeiWendi WeiMingyu WangYun XuLei BaiYing GaoCongwei JiangFangxia LiNa TianLinlin KuangRuiliang ZhuGang PangKe LanSuihan FengXiaozhen LiangMany viruses alter the phospholipid metabolism to benefit their own life cycles. It is unclear whether the host or the virus is driving phospholipid metabolism reprogramming, and how virus infections are affected by the metabolic status. Here we report that phospholipase A2 inhibitor and LY6/PLAUR domain-containing protein (PINLYP) inhibits Kaposi's sarcoma-associated herpesvirus (KSHV) lytic reactivation by remodeling phospholipid metabolism and especially triacylglycerol (TAG) biosynthesis. PINLYP deficiency led to increased phospholipase cPLA2α activity, cPLA2α-mediated AKT phosphorylation, and KSHV lytic reactivation. Analyses of RNA-seq and lipidomics reveal that PINLYP regulates long-chain fatty acid CoA ligase ACSL5 expression and TAG production. The inhibition of ACSL5 activity or TAG biosynthesis suppresses AKT phosphorylation and KSHV lytic reactivation, restoring the phenotype of PINLYP deficiency. This finding underscores the pivotal role of PINLYP in remodeling phospholipid metabolism and promoting viral latency, which sheds new light on how phospholipid metabolism is regulated by herpesvirus and provides a potential target for controlling chronic herpesvirus infection.https://doi.org/10.1371/journal.ppat.1013146
spellingShingle Zhangmengxue Lei
Wendi Wei
Mingyu Wang
Yun Xu
Lei Bai
Ying Gao
Congwei Jiang
Fangxia Li
Na Tian
Linlin Kuang
Ruiliang Zhu
Gang Pang
Ke Lan
Suihan Feng
Xiaozhen Liang
PINLYP-mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection.
PLoS Pathogens
title PINLYP-mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection.
title_full PINLYP-mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection.
title_fullStr PINLYP-mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection.
title_full_unstemmed PINLYP-mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection.
title_short PINLYP-mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection.
title_sort pinlyp mediated phospholipid metabolism reprogramming contributes to chronic herpesvirus infection
url https://doi.org/10.1371/journal.ppat.1013146
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