脂筏参与冠状病毒感染的机制及其应用的研究进展

doi:10.11843/j.issn.0366-6964.2025.05.012

摘要/Abstract

摘要：

冠状病毒严重危害人类及动物健康，其基因组极易发生突变和重组，给冠状病毒病防控带来极大困难和挑战。除了安全高效的疫苗，急需广谱抗病毒药物。针对病毒复制依赖的宿主因子的抗病毒药物具有广谱性和不易产生耐药性的优点。脂筏是位于细胞膜表面的一类特殊脂质微结构域，也是多种病毒入侵宿主细胞的结合位点，在冠状病毒感染过程中起到至关重要的作用。本文就脂筏的结构和功能、冠状病毒入侵及其与脂筏的关联性、脂筏参与冠状病毒感染的研究、脂筏在冠状病毒病防治中应用的最新进展进行综述，旨在为冠状病毒治疗靶点的研发提供方向和参考。

关键词: 脂筏, 冠状病毒, 入侵机制, 应用

Abstract:

Coronavirus seriously endangers human and animal health, and its genome is prone to mutation and recombination, which brings great difficulties and challenges to the prevention and control of coronavirus disease. In addition to safe and effective vaccines, broad-spectrum antivirals are urgently needed. Antiviral drugs targeting host factors dependent on viral replication have the advantages of broad spectrum and being less susceptible to resistance. Lipid rafts are a kind of special lipid microdomain located on the surface of cell membrane, which is also the binding site for many viruses to invade host cells, and play a crucial role in the process of coronavirus infection. This review summarized the structure and functions of lipid rafts, coronavirus invasion and its correlation with lipid rafts, the research on lipid rafts ' involvement in coronavirus infection, and the recent application of lipid rafts in the prevention and treatment of coronavirus diseases, aiming to provide direction and reference for the research and development of therapeutic targets for coronaviruses.

Key words: lipid rafts, coronavirus, invasion mechanism, application

中图分类号:

S852.65

吴芊卉, 张愉, 张桃妮, 磨美兰. 脂筏参与冠状病毒感染的机制及其应用的研究进展[J]. 畜牧兽医学报, 2025, 56(5): 2112-2122.

WU Qianhui, ZHANG Yu, ZHANG Taoni, MO Meilan. Research Progress on Mechanism of Lipid Raft Involved in Coronavirus Infection and Its Application[J]. Acta Veterinaria et Zootechnica Sinica, 2025, 56(5): 2112-2122.

图/表 2

图 1

表 1

参考文献 71

1	SIDDELL S , WEGE H , TER MEULEN V . The biology of coronaviruses[J]. J Gen Virol, 1983, 64 (4): 761- 776. doi: 10.1099/0022-1317-64-4-761
2	ZHOU P , YANG X L , WANG X G , et al. A pneumonia outbreak associated with a new coronavirus of probable bat origin[J]. Nature, 2020, 579 (7798): 270- 273. doi: 10.1038/s41586-020-2012-7
3	FURUKAWA K , OHMI Y , HAMAMURA K , et al. Signaling domains of cancer-associated glycolipids[J]. Glycoconj, 2022, 39 (2): 145- 155. doi: 10.1007/s10719-022-10051-1
4	WANG H Y , BHARTI D , LEVENTAL I . Membrane heterogeneity beyond the plasma membrane[J]. Front Cell Dev Biol, 2020, 8, 580814. doi: 10.3389/fcell.2020.580814
5	PRALLE A , KELLER P , FLORIN E L , et al. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells[J]. J Cell Biol, 2000, 148 (5): 997- 1008. doi: 10.1083/jcb.148.5.997
6	SAPOŃ K , MANŃKA R , JANAS T , et al. The role of lipid rafts in vesicle formation[J]. J Cell Biol, 2023, 136 (9): jcs260887.
7	TRYBUS M , HRYNIEWICZ-JANKOWSKA A , WóJTOWICZ K , et al. EFR3A: a new raft domain organizing protein?[J]. Cell Mol Biol Lett, 2023, 28 (1): 86. doi: 10.1186/s11658-023-00497-y
8	HIRANO K , KINOSHITA M , MATSUMORI N . Impact of sphingomyelin acyl chain heterogeneity upon properties of raft-like membranes[J]. Biochim Biophys Acta Biomembr, 2022, 1864 (12): 184036. doi: 10.1016/j.bbamem.2022.184036
9	LEVENTAL I , LYMAN E . Regulation of membrane protein structure and function by their lipid nano-environment[J]. Nat Rev Mol Cell Biol, 2023, 24 (2): 107- 122. doi: 10.1038/s41580-022-00524-4
10	CONTRERAS F X , ERNST A M , HABERKANT P , et al. Molecular recognition of a single sphingolipid species by a protein 's transmembrane domain[J]. Nature, 2012, 481 (7382): 525- 529. doi: 10.1038/nature10742
11	SAPOŃ K , JANAS T , SIKORSKI A F , et al. Polysialic acid chains exhibit enhanced affinity for ordered regions of membranes[J]. Biochim Biophys Acta Biomembr, 2019, 1861 (1): 245- 255. doi: 10.1016/j.bbamem.2018.07.008
12	CHOI K S , AIZAKI H , LAI M M C . Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release[J]. J Virol, 2005, 79 (15): 9862- 9871. doi: 10.1128/JVI.79.15.9862-9871.2005
13	SCHEIFFELE P , ROTH M G , SIMONS K . Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain[J]. EMBO J, 1997, 16 (18): 5501- 5508. doi: 10.1093/emboj/16.18.5501
14	PICKL W F , PIMENTEL-MUIÑOS F X , SEED B . Lipid rafts and pseudotyping[J]. J Virol, 2001, 75 (15): 7175- 7183. doi: 10.1128/JVI.75.15.7175-7183.2001
15	BAVARI S , BOSIO C M , WIEGAND E , et al. Lipid raft microdomains: a gateway for compartmentalized trafficking of Ebola and Marburg viruses[J]. J Exp Med, 2002, 195 (5): 593- 602. doi: 10.1084/jem.20011500
16	YANG Q , ZHANG Q , TANG J , et al. Lipid rafts both in cellular membrane and viral envelope are critical for PRRSV efficient infection[J]. Virology, 2015, 484, 170- 180. doi: 10.1016/j.virol.2015.06.005
17	CHAZAL N , GERLIER D . Virus entry, assembly, budding, and membrane rafts[J]. Microbiol Mol Biol Rev, 2003, 67 (2): 226- 237. doi: 10.1128/MMBR.67.2.226-237.2003
18	MAÑES S , DEL REAL G , MARTÍNEZ-A C . Pathogens: raft hijackers[J]. Nat Rev Immunol, 2003, 3 (7): 557- 568. doi: 10.1038/nri1129
19	ONO A , FREED E O . Role of lipid rafts in virus replication[J]. Adv Virus Res, 2005, 64, 311- 358.
20	VERMA D K , GUPTA D , LAL S K . Host lipid rafts play a major role in binding and endocytosis of influenza a virus[J]. Viruses, 2018, 10 (11): 650. doi: 10.3390/v10110650
21	AZZAZ F , YAHI N , DI SCALA C , et al. Ganglioside binding domains in proteins: physiological and pathological mechanisms[J]. Adv Protein Chem Struct Biol, 2022, 128, 289- 324.
22	FANTINI J , YAHI N , AZZAZ F , et al. Structural dynamics of SARS-CoV-2 variants: a health monitoring strategy for anticipating Covid-19 outbreaks[J]. J Infect, 2021, 83 (2): 197- 206. doi: 10.1016/j.jinf.2021.06.001
23	SUZUKI Y . [Variation of influenza viruses and their recognition of the receptor sialo-sugar chains][J]. Yakugaku Zasshi, 1993, 113 (8): 556- 578. doi: 10.1248/yakushi1947.113.8_556
24	MARKWELL M A , SVENNERHOLM L , PAULSON J C . Specific gangliosides function as host cell receptors for Sendai virus[J]. Proc Natl Acad Sci U S A, 1981, 78 (9): 5406- 5410. doi: 10.1073/pnas.78.9.5406
25	CAMPANERO-RHODES M A , SMITH A , CHAI W G , et al. N-glycolyl GM1 ganglioside as a receptor for simian virus 40[J]. J Virol, 2007, 81 (23): 12846- 12858. doi: 10.1128/JVI.01311-07
26	MAGINNIS M S . Virus-receptor interactions: the key to cellular invasion[J]. J Mol Biol, 2018, 430 (17): 2590- 2611. doi: 10.1016/j.jmb.2018.06.024
27	ROLSMA M D , KUHLENSCHMIDT T B , GELBERG H B , et al. Structure and function of a ganglioside receptor for porcine rotavirus[J]. J Virol, 1998, 72 (11): 9079- 9091. doi: 10.1128/JVI.72.11.9079-9091.1998
28	HAMMACHE D , YAHI N , MARESCA M , et al. Human erythrocyte glycosphingolipids as alternative cofactors for human immunodeficiency virus type 1 (HIV-1) entry: evidence for CD4-induced interactions between HIV-1 gp120 and reconstituted membrane microdomains of glycosphingolipids (Gb3 and GM3)[J]. J Virol, 1999, 73 (6): 5244- 5248. doi: 10.1128/JVI.73.6.5244-5248.1999
29	FANTINI J , CHAHINIAN H , YAHI N . Convergent evolution dynamics of SARS-CoV-2 and HIV surface envelope glycoproteins driven by host cell surface receptors and lipid rafts: lessons for the future[J]. Int J Mol Sci, 2023, 24 (3): 1923. doi: 10.3390/ijms24031923
30	CHAN J F W , KOK K H , ZHU Z , et al. Genomic characterization of the 2019 novel human-pathogenic coronavirus isolated from a patient with atypical pneumonia after visiting Wuhan[J]. Emerg Microbes Infect, 2020, 9 (1): 221- 236. doi: 10.1080/22221751.2020.1719902
31	鲁丹, 方一泰, 罗德炎, 等. 外泌体参与新冠病毒感染的机制及其应用的研究进展[J]. 病毒学报, 2024, 40 (1): 160- 168.
	LU D , FANG Y T , LUO D Y , et al. Research progress on the functions of exosomes during SARS-CoV-2 infection, diagnosis, treatment and prophylaxis[J]. Chinese Journal of Virology, 2024, 40 (1): 160- 168.
32	LI X W , ZHU W H , FAN M Y , et al. Dependence of SARS-CoV-2 infection on cholesterol-rich lipid raft and endosomal acidification[J]. Comput Struct Biotechnol J, 2021, 19, 1933- 1943. doi: 10.1016/j.csbj.2021.04.001
33	KHATTAB E S A E H , RAGAB A , ABOL-FTOUH M A , et al. Therapeutic strategies for Covid-19 based on molecular docking and dynamic studies to the ACE-2 receptors, Furin, and viral spike proteins[J]. J Biomol Struct Dyn, 2022, 40 (23): 13291- 13309. doi: 10.1080/07391102.2021.1989036
34	孙亚娟, 张达, 汤傲星, 等. α属冠状病毒入侵宿主所需宿主因子研究进展[J]. 病毒学报, 2024, 40 (1): 215- 224.
	SUN Y J , ZHANG D , TANG A X , et al. Research progress on host factor required of alpha-coronavirus invasion[J]. Chinese Journal of Virology, 2024, 40 (1): 215- 224.
35	FANTINI J , AZZAZ F , CHAHINIAN H , et al. Electrostatic surface potential as a key parameter in virus transmission and evolution: how to manage future virus pandemics in the post-COVID-19 era[J]. Viruses, 2023, 15 (2): 284. doi: 10.3390/v15020284
36	WANG H L , YANG P , LIU K T , et al. SARS coronavirus entry into host cells through a novel clathrin-and caveolae-independent endocytic pathway[J]. Cell Res, 2008, 18 (2): 290- 301. doi: 10.1038/cr.2008.15
37	CARONI P . New EMBO memberserreview: actin cytoskeleton regulation through modulation of PI(4, 5)P(2) rafts[J]. EMBO J, 2001, 20 (16): 4332- 4336. doi: 10.1093/emboj/20.16.4332
38	CUI J , LI F , SHI Z L . Origin and evolution of pathogenic coronaviruses[J]. Nat Rev Microbiol, 2019, 17 (3): 181- 192. doi: 10.1038/s41579-018-0118-9
39	LEDNICKY J A , TAGLIAMONTE M S , WHITE S K , et al. Independent infections of porcine deltacoronavirus among Haitian children[J]. Nature, 2021, 600 (7887): 133- 137. doi: 10.1038/s41586-021-04111-z
40	SEYRAN M , TAKAYAMA K , UVERSKY V N , et al. The structural basis of accelerated host cell entry by SARS-CoV-2[J]. FEBS J, 2021, 288 (17): 5010- 5020. doi: 10.1111/febs.15651
41	SUN X L . The role of cell surface sialic acids for SARS-CoV-2 infection[J]. Glycobiology, 2021, 31 (10): 1245- 1253. doi: 10.1093/glycob/cwab032
42	FANTINI J , CHAHINIAN H , YAHI N . Leveraging coronavirus binding to gangliosides for innovative vaccine and therapeutic strategies against COVID-19[J]. Biochem Biophys Res Commun, 2021, 538, 132- 136. doi: 10.1016/j.bbrc.2020.10.015
43	BAKILLAH A , HEJJI F A , ALMASAUD A , et al. Lipid raft integrity and cellular cholesterol homeostasis are critical for SARS-CoV-2 entry into cells[J]. Nutrients, 2022, 14 (16): 3417. doi: 10.3390/nu14163417
44	FANTINI J , CHAHINIAN H , YAHI N . A vaccine strategy based on the identification of an annular ganglioside binding motif in monkeypox virus protein E8L[J]. Viruses, 2022, 14 (11): 2531. doi: 10.3390/v14112531
45	DARWISH S , LIU L P , ROBINSON T O , et al. COVID-19 plasma extracellular vesicles increase the density of lipid rafts in human small airway epithelial cells[J]. Int J Mol Sci, 2023, 24 (2): 1654. doi: 10.3390/ijms24021654
46	LAN J , GE J , YU J , et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor[J]. Nature, 2020, 581 (7807): 215- 220. doi: 10.1038/s41586-020-2180-5
47	PALACIOS-RÁPALO S N , DE JESÚS-GONZÁLEZ L A , CORDERO-RIVERA C D , et al. Cholesterol-rich lipid rafts as platforms for SARS-CoV-2 entry[J]. Front Immunol, 2021, 12, 796855. doi: 10.3389/fimmu.2021.796855
48	FANTINI J , DI SCALA C , CHAHINIAN H , et al. Structural and molecular modelling studies reveal a new mechanism of action of chloroquine and hydroxychloroquine against SARS-CoV-2 infection[J]. Int J Antimicrob Agents, 2020, 55 (5): 105960. doi: 10.1016/j.ijantimicag.2020.105960
49	PAK A J , YU A , KE Z L , et al. Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery core[J]. Nat Commun, 2022, 13 (1): 1002. doi: 10.1038/s41467-022-28654-5
50	THORP E B , GALLAGHER T M . Requirements for CEACAMs and cholesterol during murine coronavirus cell entry[J]. J Virol, 2004, 78 (6): 2682- 2692. doi: 10.1128/JVI.78.6.2682-2692.2004
51	LU Y N , LIU D X , TAM J P . Lipid rafts are involved in SARS-CoV entry into Vero E6 cells[J]. Biochem Biophys Res Commun, 2008, 369 (2): 344- 349. doi: 10.1016/j.bbrc.2008.02.023
52	JEFFERS S A , TUSELL S M , GILLIM-ROSS L , et al. CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus[J]. Proc Natl Acad Sci U S A, 2004, 101 (44): 15748- 15753. doi: 10.1073/pnas.0403812101
53	GUO H C , HUANG M , YUAN Q , et al. The important role of lipid raft-mediated attachment in the infection of cultured cells by coronavirus infectious bronchitis virus beaudette strain[J]. PLoS One, 2017, 12 (1): e0170123. doi: 10.1371/journal.pone.0170123
54	LORIZATE M , KRÄUSSLICH H G . Role of lipids in virus replication[J]. Cold Spring Harb Perspect Biol, 2011, 3 (10): a004820. doi: 10.1101/cshperspect.a004820
55	WEI X N , SHE G L , WU T T , et al. PEDV enters cells through clathrin-, caveolae-, and lipid raft-mediated endocytosis and traffics via the endo-/lysosome pathway[J]. Vet Res, 2020, 51 (1): 10. doi: 10.1186/s13567-020-0739-7
56	PRATELLI A , COLAO V . Role of the lipid rafts in the life cycle of canine coronavirus[J]. J Gen Virol, 2015, 96 (Pt 2): 331- 337.
57	GRAHAM D R M , CHERTOVA E , HILBURN J M , et al. Cholesterol depletion of human immunodeficiency virus type 1 and simian immunodeficiency virus withβ-cyclodextrin inactivates and permeabilizes the virions: evidence for virion-associated lipid rafts[J]. J Virol, 2003, 77 (15): 8237- 8248. doi: 10.1128/JVI.77.15.8237-8248.2003
58	SVIRIDOV D , MILLER Y I , BALLOUT R A , et al. Targeting lipid rafts-a potential therapy for COVID-19[J]. Front Immunol, 2020, 11, 574508. doi: 10.3389/fimmu.2020.574508
59	ALBONI S , SECCO V , PAPOTTI B , et al. Hydroxypropyl-β-cyclodextrin depletes membrane cholesterol and inhibits SARS-CoV-2 entry into HEK293T-ACE^hi cells[J]. Pathogens, 2023, 12 (5): 647. doi: 10.3390/pathogens12050647
60	MAO S J , REN J , XU Y , et al. Studies in the antiviral molecular mechanisms of 25-hydroxycholesterol: disturbing cholesterol homeostasis and post-translational modification of proteins[J]. Eur J Pharmacol, 2022, 926, 175033. doi: 10.1016/j.ejphar.2022.175033
61	PAOLACCI S , KIANI A K , SHREE P , et al. Scoping review on the role and interactions of hydroxytyrosol and alpha-cyclodextrin in lipid-raft-mediated endocytosis of SARS-CoV-2 and bioinformatic molecular docking studies[J]. Eur Rev Med Pharmacol Sci, 2021, 25 (1 Suppl): 90- 100.
62	WANG Y Y , ZHANG Y Y , ZHANG C C , et al. Cholesterol-rich lipid rafts in the cellular membrane play an essential role in avian reovirus replication[J]. Front Microbiol, 2020, 11, 597794. doi: 10.3389/fmicb.2020.597794
63	WANG N , HAN S L , LIU R , et al. Chloroquine and hydroxychloroquine as ACE2 blockers to inhibit viropexis of 2019-nCoV Spike pseudotyped virus[J]. Phytomedicine, 2020, 79, 153333. doi: 10.1016/j.phymed.2020.153333
64	WANG M L , CAO R Y , ZHANG L K , et al. Remdesivir and chloroquine effectively inhibit the recently emerged novel coronavirus (2019-nCoV) in vitro[J]. Cell Res, 2020, 30 (3): 269- 271. doi: 10.1038/s41422-020-0282-0
65	WANG S B , LI W Y , HUI H , et al. Cholesterol 25-hydroxylase inhibits SARS-CoV-2 and other coronaviruses by depleting membrane cholesterol[J]. EMBO J, 2020, 39 (21): e106057. doi: 10.15252/embj.2020106057
66	FANTINI J , CHAHINIAN H , YAHI N . Synergistic antiviral effect of hydroxychloroquine and azithromycin in combination against SARS-CoV-2:what molecular dynamics studies of virus-host interactions reveal[J]. Int J Antimicrob Agents, 2020, 56 (2): 106020. doi: 10.1016/j.ijantimicag.2020.106020
67	ANDREANI J , LE BIDEAU M , DUFLOT I , et al. In vitro testing of combined hydroxychloroquine and azithromycin on SARS-CoV-2 shows synergistic effect[J]. Microb Pathog, 2020, 145, 104228. doi: 10.1016/j.micpath.2020.104228
68	DAS T , MUKHOPADHYAY C . Identification of possible binding modes of SARS-CoV-2 spike N-terminal domain for ganglioside GM1[J]. Chem Phys Lett, 2023, 812, 140260. doi: 10.1016/j.cplett.2022.140260
69	GUÉRIN P , YAHI N , AZZAZ F , et al. Structural dynamics of the SARS-CoV-2 spike protein: a 2-year retrospective analysis of SARS-CoV-2 variants (from alpha to omicron) reveals an early divergence between conserved and variable epitopes[J]. Molecules, 2022, 27 (12): 3851. doi: 10.3390/molecules27123851
70	HU J , PENG P , CAO X X , et al. Increased immune escape of the new SARS-CoV-2 variant of concern Omicron[J]. Cell Mol Immunol, 2022, 19 (2): 293- 295. doi: 10.1038/s41423-021-00836-z
71	MOULANA A , DUPIC T , PHILLIPS A M , et al. Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA. 1[J]. Nat Commun, 2022, 13 (1): 7011. doi: 10.1038/s41467-022-34506-z

靶点 Target	药物 Drug	特性 Characteristic
胆固醇 Cholesterol	25-羟基胆固醇 25-hydroxycholesterol (25HC)	1)抑制固醇调节元件结合蛋白2，刺激酰基辅酶A以减少膜脂筏；2)抑制氧化固醇结合蛋白或尼曼匹克C1前体蛋白来损害内体途径，导致病毒无法释放核酸；3)抑制固醇调节元件结合蛋白途径，增加聚糖对内糖苷酶的敏感性来糖基化，从而干扰病毒蛋白的前酰化
	α-环糊精 α-cyclodextrin	单独或联合羟基酪醇与S蛋白及ACE2相互作用，降低SARS-CoV-2内吞作用效率
	甲基-β-环糊精 Methyl-β-cyclodextrin	可在早期阶段阻断多种人类和动物病毒感染，包括SARS-CoV和SARS-CoV-2
	羟丙基-β-环糊精 Hydroxypropyl-β-cyclodextrin	是用作SARS-CoV-2预防剂的候选药物
	羟基酪醇 Hydroxytyrosol	具有抗病毒特性
	美伐他汀 Mevastatin	消耗胆固醇，破坏脂筏
	菲利平 Filipin	消耗胆固醇，破坏脂筏
神经节苷脂 Ganglioside	氯喹 Chloroquine	已被证明在体外有效抑制SARS-CoV-2
	羟氯喹 Hydroxychloroquine	可识别呼吸道上皮细胞表达的神经节苷脂，并竞争性阻断SARS-CoV-2与这些细胞的结合
鞘糖脂 Glycosphingolipid	苯基棕榈酰胺吗啡丙醇(PPMP) DL-threo-1-phenyl-2- palmitoylamino-3- morpholino-1-propanol	在体外，用PPMP(鞘糖脂合酶抑制剂)进行可逆处理，暂时破坏脂筏足以防止病毒感染细胞
N-末端结构域 NTD	阿奇霉素 Azithromycin	与SARS-CoV-2蛋白NTD的神经节苷脂结合结构域相互作用阻断S蛋白与脂筏的结合；与羟氯喹在体外预防SARS-CoV-2感染具有协同作用

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