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Editorial
. 2023 Mar 22:12:e87047.
doi: 10.7554/eLife.87047.

Learning more about hepatitis E virus

Altaira D Dearborn #  1 , Ashish Kumar #  1 , Joseph Marcotrigiano  1
Affiliations
Editorial

Learning more about hepatitis E virus

Altaira D Dearborn et al. Elife. .

Abstract

A domain in the ORF1 polyprotein of the hepatitis E virus that was previously thought to be a protease is actually a zinc-binding domain.

Keywords: Hepatitis E virus; infectious disease; microbiology; replication; viral hepatitis; virus infection; viruses.

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Conflict of interest statement

AD, AK, JM No competing interests declared

Figures

Figure 1.
Figure 1.. Comparing four RNA viruses.
The seven domains of the ORF1 polyprotein for the hepatitis E virus (HEV; top) are shown schematically and compared to polyproteins from rubella, Chikungunya (CHIKV), and hepatitis C virus (HCV). All four viruses contain a helicase enzyme (Hel) and an RNA polymerase enzyme (RdRp). Rubella, CHIKV and HCV contain proteases, but LeDesma et al. have shown that the PCP domain in HEV that was previously thought to be a protease is a zinc-binding domain. The locations of the zinc-binding motifs are represented by coloured spheres: green for 6Cys (HEV); orange for HisGluHis (HEV); blue for 3Cys1His (Rubella and HCV), yellow for 4Cys (CHIKV and HCV). MeT: methyltransferase; Y: Y-domain; PCP: papain-like cysteine protease; HVR: hypervariable region; X: macro-domain; AUD: alphavirus unique domain; NS/nsP: non-structural protein.
See this image and copyright information in PMC

Comment on

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