PUBLICATION
Characterization of the Fusion Core in Zebrafish Endogenous Retroviral Envelope Protein
- Authors
- Shi, J., Zhang, H., Gong, R., Xiao, G.
- ID
- ZDB-PUB-150326-9
- Date
- 2015
- Source
- Biochemical and Biophysical Research Communications 460(3): 633-8 (Journal)
- Registered Authors
- Xiao, Gengfu
- Keywords
- coiled-coil trimer, envelope protein, fusion, heptad repeats, zebrafish endogenous retrovirus
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- DNA Primers
- Endogenous Retroviruses/metabolism*
- Molecular Sequence Data
- Polymerase Chain Reaction
- Recombinant Fusion Proteins/chemistry
- Recombinant Fusion Proteins/metabolism*
- Viral Proteins/chemistry
- Viral Proteins/metabolism*
- Zebrafish
- PubMed
- 25804638 Full text @ Biochem. Biophys. Res. Commun.
Citation
Shi, J., Zhang, H., Gong, R., Xiao, G. (2015) Characterization of the Fusion Core in Zebrafish Endogenous Retroviral Envelope Protein. Biochemical and Biophysical Research Communications. 460(3):633-8.
Abstract
Zebrafish endogenous retrovirus (ZFERV) is the unique endogenous retrovirus in zebrafish, as yet, containing intact open reading frames of its envelope protein gene in zebrafish genome. Similarly, several envelope proteins of endogenous retroviruses in human and other mammalian animal genomes (such as syncytin-1 and 2 in human, syncytin-A and B in mouse) were identified and shown to be functional in induction of cell-cell fusion involved in placental development. ZFERV envelope protein (Env) gene appears to be also functional in vivo because it is expressible. After sequence alignment, we found ZFERV Env shares similar structural profiles with syncytin and other type I viral envelopes, especially in the regions of N- and C-terminal heptad repeats (NHR and CHR) which were crucial for membrane fusion. We expressed the regions of N+C protein in the ZFERV Env (residues 459-567, including predicted NHR and CHR) to characterize the fusion core structure. We found N+C protein could form a stable coiled-coil trimer that consists of three helical NHR regions forming a central trimeric core, and three CHR regions packing into the grooves on the surface of the central core. The structural characterization of the fusion core revealed the possible mechanism of fusion mediated by ZFERV Env. These results gave comprehensive explanation of how the ancient virus infects the zebrafish and integrates into the genome million years ago, and showed a rational clue for discovery of physiological significance (e.g., medicate cell-cell fusion).
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping