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. 2020 Aug 19;29(4):309–319. doi: 10.1016/j.tim.2020.07.002

Table 1.

Identified Direct Host Factor Interactions with HEV

Factor HEV binding partner Biological functiona Refs
ASGPR neHEV virion Attachment factor [20]
C1-inhibitor (SERPING1) ORF4 Altered complement activation or inhibitiona [39]
C3 RdRp, HVR Altered complement activation or inhibitiona [39]
C4a RdRp, HEL Altered complement activation or inhibitiona [39]
C8 RdRp, ORF4, HEL Altered complement activation or inhibitiona [39]
De-MARylation X-domain (macro domain) Immune evasiona [67]
De-PARylation X-domain (macro domain) Immune evasiona [67]
eEF1A1 RdRp, PCP, ORF4 Formation of a translation complexa, increased RdRp activity [12,39]
eIF3A RdRp, ORF4 Formation of a translation complexa [39]
eIF4A2 RdRp, HVR Formation of a translation complexa [39]
Factor Xa PCP Processing of the ORF1 polyproteina [38]
Ferritin X-domain (macro domain) [87]
hnRNPA2B1 Promoter regions in HEV RNA Structural (re-)arrangementsa [42]
hnRNPK Promoter regions in HEV RNA Structural (re-)arrangementsa [42]
HSPGs neHEV virion Attachment factor [16,22]
ISG15 MET-PCP Invading cellular antiviral pathwaysa [75]
ITGA3 neHEV virion Entry receptora [21]
Microtubules ORF3 Cytoskeleton rearrangementa [59,60]
PSMB1 X-domain (macro domain) Altered processing of MHC-I complexesa [39]
PSMB4 MET Altered processing of MHC-I complexesa [39]
RACK1 X-domain (macro domain) Part of the viral replication/translation complex [39]
Thrombin X-domain (macro domain), RdRp ORF1 polyprotein processinga [38]
TIM-1 Phosphatidylserine on eHEV virion Attachment factora [16]
TSG101 ORF3 Loading of virions into MVBs [61]
Ubiquitin HVR, MET-PCP Altered processing of MHC-I complexesa, invading cellular antiviral pathwaysa [39,75]
Unknown glycosylase ORF2 Production of immune decoysa [47,58]
Unknown kinase ORF3 Detecting virions ready for releasea [57,58]
Unknown palmitoyltransferase ORF3 Viral egress and subcellular localization [63]
Unknown protease ORF2 Production of immune decoysa [47,58]
a

Speculated.