Morphogenesis of Hepatitis E Virus.
Morphogenesis
Naked HEV
Quasi-enveloped
Virions
Journal
Advances in experimental medicine and biology
ISSN: 0065-2598
Titre abrégé: Adv Exp Med Biol
Pays: United States
ID NLM: 0121103
Informations de publication
Date de publication:
2023
2023
Historique:
medline:
26
5
2023
pubmed:
24
5
2023
entrez:
24
5
2023
Statut:
ppublish
Résumé
Hepatitis E virus, a leading cause of acute hepatitis worldwide, has been recognized as non-enveloped virus since its discovery in the 1980s. However, the recent identification of lipid membrane-associated form termed as "quasi-enveloped" HEV has changed this long-held notion. Both naked HEV and quasi-enveloped HEV play important roles in the pathogenesis of hepatitis E. However, the biogenesis and the mechanisms underlying the composition, biogenesis regulation, and functions of the novel quasi-enveloped virions remain enigmatic. In this chapter, we highlight the most recent discoveries on the dual life cycle of these two different types of virions, and further discuss the implication of the quasi-envelopment in our understanding of the molecular biology of HEV.
Identifiants
pubmed: 37223865
doi: 10.1007/978-981-99-1304-6_11
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
159-169Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Nature Singapore Pte Ltd.
Références
Balayan MS et al (1983) Evidence for a virus in non-A, non-B hepatitis transmitted via the fecal-oral route. Intervirology 20:23–31. https://doi.org/10.1159/000149370
doi: 10.1159/000149370
pubmed: 6409836
Takahashi M et al (2010) Hepatitis E Virus (HEV) strains in serum samples can replicate efficiently in cultured cells despite the coexistence of HEV antibodies: characterization of HEV virions in blood circulation. J Clin Microbiol 48:1112–1125. https://doi.org/10.1128/JCM.02002-09
doi: 10.1128/JCM.02002-09
pubmed: 20107086
pmcid: 2849599
Barnaud E, Rogee S, Garry P, Rose N, Pavio N (2012) Thermal inactivation of infectious hepatitis E virus in experimentally contaminated food. Appl Environ Microbiol 78:5153–5159. https://doi.org/10.1128/AEM.00436-12
doi: 10.1128/AEM.00436-12
pubmed: 22610436
pmcid: 3416424
Behrendt P et al (2022) Hepatitis E virus is highly resistant to alcohol-based disinfectants. J Hepatol 76:1062–1069. https://doi.org/10.1016/j.jhep.2022.01.006
doi: 10.1016/j.jhep.2022.01.006
pubmed: 35085595
Yin X, Ambardekar C, Lu Y, Feng Z (2016) Distinct entry mechanisms for nonenveloped and quasi-enveloped hepatitis E viruses. J Virol 90:4232–4242. https://doi.org/10.1128/JVI.02804-15
doi: 10.1128/JVI.02804-15
pubmed: 26865708
pmcid: 4810531
Nagashima S et al (2017) Characterization of the quasi-enveloped hepatitis E virus particles released by the cellular exosomal pathway. J Virol 91:e00822–e00817. https://doi.org/10.1128/JVI.00822-17
doi: 10.1128/JVI.00822-17
pubmed: 28878075
pmcid: 5660490
Nagashima S et al (2011) Tumour susceptibility gene 101 and the vacuolar protein sorting pathway are required for the release of hepatitis E virions. J Gen Virol 92:2838–2848. https://doi.org/10.1099/vir.0.035378-0
doi: 10.1099/vir.0.035378-0
pubmed: 21880841
Nagashima S et al (2014) Hepatitis E virus egress depends on the exosomal pathway, with secretory exosomes derived from multivesicular bodies. J Gen Virol 95:2166–2175. https://doi.org/10.1099/vir.0.066910-0
doi: 10.1099/vir.0.066910-0
pubmed: 24970738
Xing L et al (2010) Structure of hepatitis E virion-sized particle reveals an RNA-dependent viral assembly pathway. J Biol Chem 285:33175–33183. https://doi.org/10.1074/jbc.M110.106336
doi: 10.1074/jbc.M110.106336
pubmed: 20720013
pmcid: 2963395
Xing L et al (1999) Recombinant hepatitis E capsid protein self-assembles into a dual-domain T = 1 particle presenting native virus epitopes. Virology 265:35–45. https://doi.org/10.1006/viro.1999.0005
doi: 10.1006/viro.1999.0005
pubmed: 10603315
Guu TS et al (2009) Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding. Proc Natl Acad Sci U S A 106:12992–12997. https://doi.org/10.1073/pnas.0904848106
doi: 10.1073/pnas.0904848106
pubmed: 19622744
pmcid: 2722310
Yamashita T et al (2009) Biological and immunological characteristics of hepatitis E virus-like particles based on the crystal structure. Proc Natl Acad Sci U S A 106:12986–12991. https://doi.org/10.1073/pnas.0903699106
doi: 10.1073/pnas.0903699106
pubmed: 19620712
pmcid: 2722322
Tyagi S, Korkaya H, Zafrullah M, Jameel S, Lal SK (2002) The phosphorylated form of the ORF3 protein of hepatitis E virus interacts with its non-glycosylated form of the major capsid protein, ORF2. J Biol Chem 277:22759–22767. https://doi.org/10.1074/jbc.M200185200
doi: 10.1074/jbc.M200185200
pubmed: 11934888
Kenney SP, Wentworth JL, Heffron CL, Meng XJ (2015) Replacement of the hepatitis E virus ORF3 protein PxxP motif with heterologous late domain motifs affects virus release via interaction with TSG101. Virology 486:198–208. https://doi.org/10.1016/j.virol.2015.09.012
doi: 10.1016/j.virol.2015.09.012
pubmed: 26457367
Ding Q et al (2017) Hepatitis E virus ORF3 is a functional ion channel required for release of infectious particles. Proc Natl Acad Sci U S A 114:1147–1152. https://doi.org/10.1073/pnas.1614955114
doi: 10.1073/pnas.1614955114
pubmed: 28096411
pmcid: 5293053
Aicart-Ramos C, Valero RA, Rodriguez-Crespo I (1808) Protein palmitoylation and subcellular trafficking. Biochim Biophys Acta 2981-2994:2011. https://doi.org/10.1016/j.bbamem.2011.07.009
doi: 10.1016/j.bbamem.2011.07.009
Gouttenoire J et al (2018) Palmitoylation mediates membrane association of hepatitis E virus ORF3 protein and is required for infectious particle secretion. PLoS Pathog 14:e1007471. https://doi.org/10.1371/journal.ppat.1007471
doi: 10.1371/journal.ppat.1007471
pubmed: 30532200
pmcid: 6307819
Emerson SU et al (2010) Release of genotype 1 hepatitis E virus from cultured hepatoma and polarized intestinal cells depends on open reading frame 3 protein and requires an intact PXXP motif. J Virol 84:9059–9069. https://doi.org/10.1128/jvi.00593-10
doi: 10.1128/jvi.00593-10
pubmed: 20610720
pmcid: 2937629
Allweiss L et al (2016) Human liver chimeric mice as a new model of chronic hepatitis E virus infection and preclinical drug evaluation. J Hepatol 64:1033–1040. https://doi.org/10.1016/j.jhep.2016.01.011
doi: 10.1016/j.jhep.2016.01.011
pubmed: 26805671
Sayed IM et al (2017) Study of hepatitis E virus infection of genotype 1 and 3 in mice with humanised liver. Gut 66:920–929. https://doi.org/10.1136/gutjnl-2015-311109
doi: 10.1136/gutjnl-2015-311109
pubmed: 27006186
He S et al (2008) Putative receptor-binding sites of hepatitis E virus. J Gen Virol 89:245–249. https://doi.org/10.1099/vir.0.83308-0
doi: 10.1099/vir.0.83308-0
pubmed: 18089748
Cao D, Meng XJ (2012) Molecular biology and replication of hepatitis E virus. Emerg Microbes Infect 1:e17. https://doi.org/10.1038/emi.2012.7
doi: 10.1038/emi.2012.7
pubmed: 26038426
pmcid: 3630916
Kalia M, Chandra V, Rahman SA, Sehgal D, Jameel S (2009) Heparan sulfate proteoglycans are required for cellular binding of the hepatitis E virus ORF2 capsid protein and for viral infection. J Virol 83:12714–12724. https://doi.org/10.1128/JVI.00717-09
doi: 10.1128/JVI.00717-09
pubmed: 19812150
pmcid: 2786843
Yu H et al (2011) Homology model and potential virus-capsid binding site of a putative HEV receptor Grp78. J Mol Model 17:987–995. https://doi.org/10.1007/s00894-010-0794-5
doi: 10.1007/s00894-010-0794-5
pubmed: 20628775
Zhang L et al (2016) Asialoglycoprotein receptor facilitates infection of PLC/PRF/5 cells by HEV through interaction with ORF2. J Med Virol 88:2186–2195. https://doi.org/10.1002/jmv.24570
doi: 10.1002/jmv.24570
pubmed: 27155063
Shukla P et al (2011) Cross-species infections of cultured cells by hepatitis E virus and discovery of an infectious virus-host recombinant. Proc Natl Acad Sci U S A 108:2438–2443. https://doi.org/10.1073/pnas.1018878108
doi: 10.1073/pnas.1018878108
pubmed: 21262830
pmcid: 3038723
Shukla P et al (2012) Adaptation of a genotype 3 hepatitis E virus to efficient growth in cell culture depends on an inserted human gene segment acquired by recombination. J Virol 86:5697–5707. https://doi.org/10.1128/JVI.00146-12
doi: 10.1128/JVI.00146-12
pubmed: 22398290
pmcid: 3347312
Li TC, Wakita T (2018) Small animal models of hepatitis E virus infection. Cold Spring Harb Perspect Med 9:a032581. https://doi.org/10.1101/cshperspect.a032581
doi: 10.1101/cshperspect.a032581
Das A et al (2017) TIM1 (HAVCR1) is not essential for cellular entry of either quasi-enveloped or naked hepatitis A virions. MBio 8:e00969. https://doi.org/10.1128/mBio.00969-17
doi: 10.1128/mBio.00969-17
pubmed: 28874468
pmcid: 5587907
Rivera-Serrano EE, Gonzalez-Lopez O, Das A, Lemon SM (2019) Cellular entry and uncoating of naked and quasi-enveloped human hepatoviruses. elife 8:e43983. https://doi.org/10.7554/eLife.43983
doi: 10.7554/eLife.43983
pubmed: 30801249
pmcid: 6422491
Grove J, Marsh M (2011) The cell biology of receptor-mediated virus entry. J Cell Biol 195:1071–1082. https://doi.org/10.1083/jcb.201108131
doi: 10.1083/jcb.201108131
pubmed: 22123832
pmcid: 3246895
Kapur N, Thakral D, Durgapal H, Panda SK (2012) Hepatitis E virus enters liver cells through receptor-dependent clathrin-mediated endocytosis. J Viral Hepat 19:436–448. https://doi.org/10.1111/j.1365-2893.2011.01559.x
doi: 10.1111/j.1365-2893.2011.01559.x
pubmed: 22571906
Yin X, Li X, Feng Z (2016) Role of envelopment in the HEV life cycle. Viruses 8:229. https://doi.org/10.3390/v8080229
doi: 10.3390/v8080229
pubmed: 27548201
pmcid: 4997591
Tuthill TJ et al (2009) Equine rhinitis A virus and its low pH empty particle: clues towards an aphthovirus entry mechanism? PLoS Pathog 5:e1000620. https://doi.org/10.1371/journal.ppat.1000620
doi: 10.1371/journal.ppat.1000620
pubmed: 19816570
pmcid: 2752993
Wang X et al (2015) Hepatitis A virus and the origins of picornaviruses. Nature 517:85–88. https://doi.org/10.1038/nature13806
doi: 10.1038/nature13806
pubmed: 25327248
Drexler JF et al (2015) Evolutionary origins of hepatitis A virus in small mammals. Proc Natl Acad Sci U S A 112:15190–15195. https://doi.org/10.1073/pnas.1516992112
doi: 10.1073/pnas.1516992112
pubmed: 26575627
pmcid: 4679062
Zhao X et al (2019) Human neonatal Fc receptor is the cellular uncoating receptor for enterovirus B. Cell 177:1553
doi: 10.1016/j.cell.2019.04.035
pubmed: 31104841
pmcid: 7111318
Bergelson JM et al (1994) Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses. Proc Natl Acad Sci U S A 91:6245–6248. https://doi.org/10.1073/pnas.91.13.6245
doi: 10.1073/pnas.91.13.6245
pubmed: 7517044
pmcid: 44175
Renou C, Roque-Afonso AM, Pavio N (2014) Foodborne transmission of hepatitis E virus from raw pork liver sausage, France. Emerg Infect Dis 20:1945–1947. https://doi.org/10.3201/eid2011.140791
doi: 10.3201/eid2011.140791
pubmed: 25340356
pmcid: 4214313
Berto A et al (2013) Hepatitis E virus in pork liver sausage, France. Emerg Infect Dis 19:264–266. https://doi.org/10.3201/eid1902.121255
doi: 10.3201/eid1902.121255
pubmed: 23347828
pmcid: 3563277
Colson P et al (2010) Pig liver sausage as a source of hepatitis E virus transmission to humans. J Infect Dis 202:825–834. https://doi.org/10.1086/655898
doi: 10.1086/655898
pubmed: 20695796
Sayed IM et al (2016) Study of hepatitis E virus infection of genotype 1 and 3 in mice with humanised liver. Gut 66:920. https://doi.org/10.1136/gutjnl-2015-311109
doi: 10.1136/gutjnl-2015-311109
pubmed: 27006186
Jones MK et al (2014) Enteric bacteria promote human and mouse norovirus infection of B cells. Science 346:755–759. https://doi.org/10.1126/science.1257147
doi: 10.1126/science.1257147
pubmed: 25378626
pmcid: 4401463
Marion O, Lhomme S, Nayrac M, Dubois M, Izopet J (2019) Hepatitis E virus replication in human intestinal cells. Gut 69:901
doi: 10.1136/gutjnl-2019-319004
pubmed: 31727684
Williams TP et al (2001) Evidence of extrahepatic sites of replication of the hepatitis E virus in a swine model. J Clin Microbiol 39:3040–3046
doi: 10.1128/JCM.39.9.3040-3046.2001
pubmed: 11526125
pmcid: 88293
van de Garde MD et al (2016) Hepatitis E virus (HEV) genotype 3 infection of human liver chimeric mice as a model for chronic HEV infection. J Virol 90:4394–4401. https://doi.org/10.1128/JVI.00114-16
doi: 10.1128/JVI.00114-16
pubmed: 26889028
pmcid: 4836345
Hewitt PE et al (2014) Hepatitis E virus in blood components: a prevalence and transmission study in southeast England. Lancet 384:1766–1773. https://doi.org/10.1016/S0140-6736(14)61034-5
doi: 10.1016/S0140-6736(14)61034-5
pubmed: 25078306
Gallian P et al (2014) Hepatitis E virus infections in blood donors, France. Emerg Infect Dis 20:1914–1917. https://doi.org/10.3201/eid2011.140516
doi: 10.3201/eid2011.140516
pubmed: 25340881
pmcid: 4214305
Kurihara T et al (2016) Chronic hepatitis E virus infection after living donor liver transplantation via blood transfusion: a case report. Surg Case Rep 2:32. https://doi.org/10.1186/s40792-016-0159-0
doi: 10.1186/s40792-016-0159-0
pubmed: 27059470
pmcid: 4826363
Elayan H, Kennedy B, Ziegler MG (1992) Propranolol reduces rat dopamine-beta-hydroxylase activity and catecholamine levels. Eur J Pharmacol 212:259–262. https://doi.org/10.1016/0014-2999(92)90339-6
doi: 10.1016/0014-2999(92)90339-6
pubmed: 1601068
Zhou X et al (2017) Hepatitis E virus infects neurons and brains. J Infect Dis 215:1197–1206. https://doi.org/10.1093/infdis/jix079
doi: 10.1093/infdis/jix079
pubmed: 28199701
Drave SA et al (2016) Extra-hepatic replication and infection of hepatitis E virus in neuronal-derived cells. J Viral Hepat 23:512–521. https://doi.org/10.1111/jvh.12515
doi: 10.1111/jvh.12515
pubmed: 26891712