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Amino acid pattern reveals multi-functionality of ORF3 protein from HEV



Zoya Shafat1, Asimul Islam1 & Shama Parveen*, 1



1Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India; *Corresponding author



Shama Parveen - E-mail: sparveen2@jmi.ac.in

Zoya Shafat - E-mail: zoya179695@st.jmi.ac.in

Asimul Islam - E-mail: aislam@jmi.ac.in


Article Type

Research Article



Received February 1, 2024; Revised February 29, 2024; Accepted February 29, 2024, Published February 29, 2024



The smallest open reading frame (ORF) encoded protein ORF3 of hepatitis E virus (HEV), recently, has been demonstrated to perform multiple functions besides accessory roles. ORF3 could act as a target for vaccine against HEV infections. The IDR (intrinsically disordered region); IDP (ID protein)/IDPR (ID protein region), plays critical role in various regulatory functions of viruses. The dark proteome of HEV-ORF3 protein including its structure and function was systematically examined by computer predictors to explicate its role in viral pathogenesis and drug resistance beyond its functions as accessory viral protein. Amino acid distribution showed ORF3 enrichment with disorder-promoting residues (Ala, Pro, Ser, Gly) while deficiency in order-promoting residues (Asn, Ile, Phe, Tyr and Trp). Initial investigation revealed ORF3 as IDP (entirely disordered protein) or IDPR (proteins consisting of IDRs with structured globular domains). Structural examination revealed preponderance of disordered regions interpreting ORF3 as moderately/highly disordered protein. Further disorder predictors categorized ORF3 as highly disordered protein/IDP. Identified sites and associated-crucial molecular functions revealed ORF3 involvement in diverse biological processes, substantiating them as targets of regulation. As ORF3 functions are yet to completely explored, thus, data on its disorderness could help in elucidating its disorder related functions.



Hepatitis E virus (HEV), Open reading frame 3 (ORF3), amino acid composition, structural analysis, Disorder variant, moderately disordered protein, highly disordered protein, Intrinsically Disordered Protein Region (IDPR), Intrinsically Disordered Protein (IDP)



Shafat et al. Bioinformation 20(2): 121-135 (2024)


Edited by

P Kangueane






Biomedical Informatics



This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.