Tracing the evolutionary history of hepadnaviruses in terms of e antigen and middle envelope protein expression or processing.
Amino Acid Sequence
Antigens, Viral
/ genetics
Biological Evolution
Evolution, Molecular
Gene Expression Regulation, Viral
Genome, Viral
Genomics
/ methods
Hepadnaviridae
/ genetics
Hepadnaviridae Infections
/ immunology
Hepatitis B
/ immunology
Hepatitis B e Antigens
/ genetics
Hepatitis B virus
/ genetics
Humans
Viral Envelope Proteins
/ chemistry
Evolution
Hepadnavirus
Hepatitis B virus
Middle envelope protein
Myristoylation
e antigen
Journal
Virus research
ISSN: 1872-7492
Titre abrégé: Virus Res
Pays: Netherlands
ID NLM: 8410979
Informations de publication
Date de publication:
15 01 2020
15 01 2020
Historique:
received:
26
09
2019
revised:
25
11
2019
accepted:
26
11
2019
pubmed:
1
12
2019
medline:
18
11
2020
entrez:
1
12
2019
Statut:
ppublish
Résumé
Hepatitis B virus (HBV) is the prototype of hepadnaviruses, which can be subgrouped into orthohepadnaviruses infecting mammals, avihehepadnaviruses of birds, metahepadnaviruses of fish, and herpetohepadnaviruses of amphibians and reptiles. The middle (M) envelope protein and e antigen are new additions in the evolution of hepadnaviruses. They are alternative translation products of the transcripts for small (S) envelope and core proteins, respectively. For HBV, e antigen is converted from precore/core protein by removal of N-terminal signal peptide followed by furin-mediated cleavage of the basic C-terminus. This study compared old and newly discovered hepadnaviruses for their envelope protein and e antigen expression or processing. The S protein of bat hepatitis B virus (BHBV) and two metahepadnaviruses is probably myristoylated, in addition to two avihepadnaviruses. While most orthohepadnaviruses express a functional M protein with N-linked glycosylation near the amino-terminus, most metahepadnaviruses and herpetohepadnaviruses probably do not. These viruses and one orthohepadnavirus, the shrew hepatitis B virus, lack an open precore region required for e antigen expression. Potential furin cleavage sites (RXXR sequence) can be found in e antigen precursors of orthohepadnaviruses and avihepadnaviruses. Despite much larger precore/core proteins of avihepadnaviruses and their limited sequence homology with those of orthohepadnaviruses, their proximal RXXR motif can be aligned with a distal RXXR motif for orthohepadnaviruses. Thus, furin or another basic endopeptidase is probably the shared enzyme for hepadnaviral e antigen maturation. A precore-derived cysteine residue is involved in forming intramolecular disulfide bond of HBV e antigen to prevent particle formation, and such a cysteine residue is conserved for both orthohepadnaviruses and avihepadnaviruses. All orthohepadnaviruses have an X gene, while all avihepadnaviruses can express the e antigen. M protein expression appears to be the most recent event in the evolution of hepadnaviruses.
Identifiants
pubmed: 31785305
pii: S0168-1702(19)30696-3
doi: 10.1016/j.virusres.2019.197825
pmc: PMC6942179
mid: NIHMS1545986
pii:
doi:
Substances chimiques
Antigens, Viral
0
Hepatitis B e Antigens
0
Viral Envelope Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
197825Subventions
Organisme : NIAID NIH HHS
ID : R01 AI116639
Pays : United States
Organisme : NIAID NIH HHS
ID : R21 AI142456
Pays : United States
Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.
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