人磷脂爬行酶1在抗病毒感染中的研究进展

doi:10.3969/j.issn.1673-8640.2025.01.017

检验医学 ›› 2025, Vol. 40 ›› Issue (1): 96-101.DOI: 10.3969/j.issn.1673-8640.2025.01.017

人磷脂爬行酶1在抗病毒感染中的研究进展

马鑫鑫¹, 陆红祥², 史清海³()

1. 新疆医科大学研究生院，新疆乌鲁木齐 830000
2. 新疆军区总医院创伤骨科，新疆乌鲁木齐 830000
3. 新疆军区总医院全军临床检验诊断中心，新疆乌鲁木齐 830000

收稿日期:2024-05-06 修回日期:2024-09-27 出版日期:2025-01-30 发布日期:2025-02-17
通讯作者: 史清海，E-mail：shiqinghai@aliyun.com。
作者简介:马鑫鑫，女，1998年生，硕士，主要从事感染诊断标志物研究。
基金资助:
国家自然科学基金项目(82102276);新疆维吾尔自治区天山英才项目(2022TSYCCX0114);新疆维吾尔自治区自然科学基金项目(2022D01C843);新疆医科大学研究生创新创业项目(CXCY2024015)

Human phospholipid scramblase 1 in antiviral infection

MA Xinxin¹, LU Hongxiang², SHI Qinghai³()

1. Graduate School of Xinjiang Medical University，Urumqi 830000，Xinjiang，China
2. Clinical Laboratory Diagnostic Center，General Hospital of Xinjiang Military Command，Urumqi 830000，Xinjiang，China
3. Department of Traumatic Orthopedics，General Hospital of Xinjiang Military Command，Urumqi 830000，Xinjiang，China

Received:2024-05-06 Revised:2024-09-27 Online:2025-01-30 Published:2025-02-17

摘要/Abstract

摘要：

人磷脂爬行酶1（hPLSCR1）是跨膜蛋白家族的一员，以Ca²⁺依赖的方式介导膜磷脂的跨双层运动，并在细胞信号传导、成熟和凋亡中发挥重要作用，具有成为相关疾病治疗靶点或生物标志物的潜能。文章对hPLSCR1在抗病毒感染中的研究进展进行综述。

关键词: 人磷脂爬行酶1, 感染, 病毒

Abstract:

Human phospholipid scramblase 1（hPLSCR1）is a member of the transmembrane protein family that mediates the cross-layer movement of membrane phospholipids in a Ca²⁺ dependent manner and plays a role in cell signal transduction，maturation and apoptosis. It has the potential to become a therapeutic target or biomarker for related diseases. This review focuses on the research progress of hPLSCR1 in antiviral infection.

Key words: Human phospholipid scramblase 1, Infection, Virus

中图分类号:

R446.1

马鑫鑫, 陆红祥, 史清海. 人磷脂爬行酶1在抗病毒感染中的研究进展[J]. 检验医学, 2025, 40(1): 96-101.

MA Xinxin, LU Hongxiang, SHI Qinghai. Human phospholipid scramblase 1 in antiviral infection[J]. Laboratory Medicine, 2025, 40(1): 96-101.

参考文献 51

[1]	RAYALA S, SIVAGNANAM U, GUMMADI S N. Biophysical characterization of the DNA binding motif of human phospholipid scramblase 1[J]. Eur Biophys J, 2022, 51(7-8):579-593.
[2]	SAKURAGI T, NAGATA S. Regulation of phospholipid distribution in the lipid bilayer by flippases and scramblases[J]. Nat Rev Mol Cell Biol, 2023, 24(8):576-596.
[3]	WANG Y, KINOSHITA T. The role of lipid scramblases in regulating lipid distributions at cellular membranes[J]. Biochem Soc Trans, 2023, 51(5):1857-1869.
[4]	TANG D, WANG Y, DONG X, et al. Scramblases and virus infection[J]. Bioessays, 2022, 44(12):e2100261.
[5]	XU D, JIANG W, WU L, et al. PLSCR1 is a cell-autonomous defence factor against SARS-CoV-2 infection[J]. Nature, 2023, 619(7971):819-827.
[6]	DAL COL J, LAMBERTI M J, NIGRO A, et al. Phospholipid scramblase 1:a protein with multiple functions via multiple molecular interactors[J]. Cell Commun Signal, 2022, 20(1):78.
[7]	MERTOWSKA P, SMOLAK K, MERTOWSKI S, et al. Immunomodulatory role of interferons in viral and bacterial infections[J]. Int J Mol Sci, 2023, 24(12):10115.
[8]	LI M. Fortifying immunity:PLSCR1 picks battle against SARS-CoV-2[J]. Cell Host Microbe, 2023, 31(9):1417-1419.
[9]	KOUSATHANAS A, PAIRO-CASTINEIRA E, RAWLIK K, et al. Whole-genome sequencing reveals host factors underlying critical COVID-19[J]. Nature, 2022, 607(7917):97-103.
[10]	HILLIGAN K L, NAMASIVAYAM S, CLANCY C S, et al. Bacterial-induced or passively administered interferon gamma conditions the lung for early control of SARS-CoV-2[J]. Nat Commun, 2023, 14(1):8229. DOI PMID
[11]	OUDIT G Y, WANG K, VIVEIROS A, et al. Angiotensin-converting enzyme 2-at the heart of the COVID-19 pandemic[J]. Cell, 2023, 186(5):906-922. DOI PMID
[12]	THIRUMUGAM G, RADHAKRISHNAN Y, RAMAMURTHI S, et al. A systematic review on impact of SARS-CoV-2 infection[J]. Microbiol Res, 2023, 271:127364.
[13]	LE PEN J, PANICCIA G, KINAST V, et al. A genome-wide arrayed CRISPR screen identifies PLSCR1 as an intrinsic barrier to SARS-CoV-2 entry that recent virus variants have evolved to resist[J]. PLoS Biol, 2024, 22(9):e3002767.
[14]	YANG H, DONG Y, BIAN Y, et al. The influenza virus PB2 protein evades antiviral innate immunity by inhibiting JAK1/STAT signalling[J]. Nat Commun, 2022, 13(1):6288. DOI PMID
[15]	陈丹阳, 郑思钰, 郑锐林, 等. 流感病毒研究进展[J]. 检验医学, 2023, 38(7):696-703. DOI
[16]	LUO W, ZHANG J, LIANG L, et al. Phospholipid scramblase 1 interacts with influenza A virus NP,impairing its nuclear import and thereby suppressing virus replication[J]. PLoS Pathog, 2018, 14(1):e1006851.
[17]	LIU Y, LIN S, XIE Y, et al. ILDR1 promotes influenza A virus replication through binding to PLSCR1[J]. Sci Rep, 2022, 12(1):8515. DOI PMID
[18]	SHAN S, ZHAO X, JIA J. Comprehensive approach to controlling chronic hepatitis B in China[J]. Clin Mol Hepatol, 2024, 30(2):135-143. DOI PMID
[19]	YANG J, ZHU X, LIU J, et al. Inhibition of Hepatitis B virus replication by phospholipid scramblase 1 in vitro and in vivo[J]. Antiviral Res, 2012, 94(1):9-17.
[20]	ASHOURI S, KHOR S S, HITOMI Y, et al. Genome-wide association study for chronic hepatitis B infection in the Thai population[J]. Front Genet, 2022, 13:887121.
[21]	WANG F, SONG H, XU F, et al. Role of hepatitis B virus non-structural protein HBx on HBV replication,interferon signaling,and hepatocarcinogenesis[J]. Front Microbiol, 2023, 14:1322892.
[22]	CHOONNASARD A, SHOFA M, OKABAYASHI T, et al. Conserved functions of Orthohepadnavirus X proteins to inhibit type-Ⅰ interferon signaling[J]. Int J Mol Sci, 2024, 25(7):3753.
[23]	HILLAIRE M L B, LAWRENCE P, LAGRANGE B. IFN-γ:a crucial player in the fight against HBV infection?[J]. Immune Netw, 2023, 23(4):e30.
[24]	SANCHEZ V, BRITT W. Human cytomegalovirus egress:overcoming barriers and co-opting cellular functions[J]. Viruses, 2021, 14(1):15.
[25]	AMSLER L, VERWEIJ M, DEFILIPPIS V R. The tiers and dimensions of evasion of the type I interferon response by human cytomegalovirus[J]. J Mol Biol, 2013, 425(24):4857-4871. DOI PMID
[26]	DELL'OSTE V,BIOLATTI M,GALITSKA G,et al. Tuning the orchestra:HCMV vs. Innate Immunity[J]. Front Microbiol, 2020, 11:661.
[27]	SADANARI H, TAKEMOTO M, ISHIDA T, et al. The interferon-inducible human PLSCR1 protein is a restriction factor of human cytomegalovirus[J]. Microbiol Spectr, 2022, 10(1):e0134221.
[28]	FRAPPIER L. Epstein-Barr virus is an agent of genomic instability[J]. Nature, 2023, 616(7957):441-442.
[29]	UDDIN M K, WATANABE T, ARATA M, et al. Epstein-Barr virus BBLF1 mediates secretory vesicle transport to facilitate mature virion release[J]. J Virol, 2023, 97(6):e0043723.
[30]	KUSANO S, IKEDA M. Interaction of phospholipid scramblase 1 with the Epstein-Barr virus protein BZLF1 represses BZLF1-mediated lytic gene transcription[J]. J Biol Chem, 2019, 294(41):15104-15116. DOI PMID
[31]	World Health Organization. HIV[EB/OL]. (2023-12-31)[2024-09-26]. https://www.who.int/data/gho/data/themes/hiv-aids.
[32]	The Joint United Nations Programme on HIV/AIDS. Global HIV & AIDS statistics-fact sheet[EB/OL]. (2023-12-31)[2024-03-31]. https://www.unaids.org/en/resources/fact-sheet.
[33]	DHARAN A, BACHMANN N, TALLEY S, et al. Nuclear pore blockade reveals that HIV-1 completes reverse transcription and uncoating in the nucleus[J]. Nat Microbiol, 2020, 5(9):1088-1095. DOI PMID
[34]	MÜLLER T G, ZILA V, MÜLLER B, et al. Nuclear capsid uncoating and reverse transcription of HIV-1[J]. Annu Rev Virol, 2022, 9(1):261-284. DOI PMID
[35]	JÄGER N, PÖHLMANN S, RODNINA M V, et al. Interferon-stimulated genes that target retrovirus translation[J]. Viruses, 2024, 16(6):933.
[36]	CAFARO A, SCHIETROMA I, SERNICOLA L, et al. Role of HIV-1 Tat protein interactions with host receptors in HIV infection and pathogenesis[J]. Int J Mol Sci, 2024, 25(3):1704.
[37]	MOUSSEAU G, ANEJA R, CLEMENTZ M A, et al. Resistance to the Tat inhibitor didehydro-cortistatin A is mediated by heightened basal HIV-1 transcription[J]. mBio, 2019, 10(4):e01750-18.
[38]	KUSANO S, EIZURU Y. Interaction of the phospholipid scramblase 1 with HIV-1 Tat results in the repression of Tat-dependent transcription[J]. Biochem Biophys Res Commun, 2013, 433(4):438-444.
[39]	SPECTOR C, MELE A R, WIGDAHL B, et al. Genetic variation and function of the HIV-1 Tat protein[J]. Med Microbiol Immunol, 2019, 208(2):131-169.
[40]	VAN RYK D, VIMONPATRANON S, HIATT J, et al. The V2 domain of HIV gp120 mimics an interaction between CD4 and integrin α4β7[J]. PLoS Pathog, 2023, 19(12):e1011860.
[41]	CHEN Q, ZHAO Y, ZHANG Y, et al. HIV associated cell death:peptide-induced apoptosis restricts viral transmission[J]. Front Immunol, 2023, 14:1096759.
[42]	SPONAUGLE A, WEIDEMAN A M K, RANEK J, et al. Dominant CD4⁺ T cell receptors remain stable throughout antiretroviral therapy-mediated immune restoration in people with HIV[J]. Cell Rep Med, 2023, 4(11):101268.
[43]	PY B, BASMACIOGULLARI S, BOUCHET J, et al. The phospholipid scramblases 1 and 4 are cellular receptors for the secretory leukocyte protease inhibitor and interact with CD4 at the plasma membrane[J]. PLoS One, 2009, 4(3):e5006.
[44]	MORRISON C S, CHEN P L, YAMAMOTO H, et al. Concomitant imbalances of systemic and mucosal immunity increase HIV acquisition risk[J]. J Acquir Immune Defic Syndr, 2020, 84(1):85-91. DOI PMID
[45]	GOVENDER Y, MORRISON C S, CHEN P L, et al. Cervical and systemic innate immunity predictors of HIV risk linked to genital herpes acquisition and time from HSV-2 seroconversion[J]. Sex Transm Infect, 2023, 99(5):311-316.
[46]	LEGRAND N, MCGREGOR S, BULL R, et al. Clinical and public health implications of human T-lymphotropic virus type 1 infection[J]. Clin Microbiol Rev, 2022, 35(2):e0007821.
[47]	KALEMERA M D, MAHER A K, DOMINGUEZ-VILLAR M, et al. Cell culture evaluation hints widely available HIV drugs are primed for success if repurposed for HTLV-1 prevention[J]. Pharmaceuticals(Basel), 2024, 17(6):730.
[48]	HLEIHEL R, SKAYNEH H, DE THÉ H, et al. Primary cells from patients with adult T cell leukemia/lymphoma depend on HTLV-1 Tax expression for NF-κB activation and survival[J]. Blood Cancer J, 2023, 13(1):67. DOI PMID
[49]	NOZUMA S, KUBOTA R, JACOBSON S. Human T-lymphotropic virus type 1(HTLV-1)and cellular immune response in HTLV-1-associated myelopathy/tropical spastic paraparesis[J]. J Neurovirol, 2020, 26(5):652-663.
[50]	KUSANO S, EIZURU Y. Human phospholipid scramblase 1 interacts with and regulates transactivation of HTLV-1 tax[J]. Virology, 2012, 432(2):343-352. DOI PMID
[51]	CARCONE A, JOURNO C, DUTARTRE H. Is the HTLV-1 retrovirus targeted by host restriction factors?[J]. Viruses, 2022, 14(8):1611.

人磷脂爬行酶1在抗病毒感染中的研究进展

Human phospholipid scramblase 1 in antiviral infection

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