FIGURE

Fig 1

ID
ZDB-FIG-230406-68
Publication
Hong et al., 2023 - Essential role of an ERV-derived Env38 protein in adaptive humoral immunity against an exogenous SVCV infection in a zebrafish model
Other Figures
All Figure Page
Back to All Figure Page
Fig 1

Bioinformatic characterization of ERV-E5.1.38-DanRer element and Env38 molecule.

(A) Genomic localization of ERV-E5.1.38-DanRer element in zebrafish. The locus of ERV-E5.1.38-DanRer element on zebrafish chromosome 5 is indicated in red arrow. The ERV-E5.1.38-DanRer is distributed inside si:zfos-375h5.1. The upstream hspb1, ywhag1, tspoap1, supt4h1, hsf5 and downstream rpain, c1qbp, znhit3, myo19 genes of ERV-E5.1.38-DanRer are presented, and att means attachment site. (B) Schematic diagram showing the transcription and splicing of env38 gene, as well as the structural characterization of Env38 protein, in which a signal peptide (1–18 amino acid), a furin cleavage site (R/K-X-R/K-R, 227–230 amino acid), an immunosuppressive domain (ISD, 309–325 amino acid), a transmembrane (TM) domain (383–405 amino acid) and conserved C-X-X-C and C-X5/6/7-C motifs are presented. The LTR consists of U3, R, and U5. The transcription of env38 begins at 5’-LTR-R and ends at 3’-LTR-R. (C) The five predicted N-glycosylation sites in SU subunit and two in TM subunit are marked with ASN residues. SU: surface subunit; TM: transmembrane subunit. (D) Hydrophobicity analysis of Env38 protein showed that the fusion peptide next to the furin-cleavage site was partial hydrophobic. FP: fusion peptide; NHR: N-terminal heptad repeats; CHR: C-terminal heptad repeats; TM: transmembrane domain. (E) Tertiary structure of Env38 monomer modeled by I-TASSER. Prominent central α-helical coiled-coil (CC) structures were found in the TM subunit of Env38 monomer protein. The top five threading templates were 6vkm, 6rx3A, 6vkm, 6fgzA, and 5yfpH. TM: transmembrane subunit; SU: surface subunit. (F) Tertiary structure of the NHR-CHR trimeric domain of Env38 TM subunit predicted by SWISS-MODEL program with crystal structures of human Syncytin 1 in post-fusion conformation (SMTL ID: 6rx1.1) as a model. A homotrimer with a fusion core structure was formed by three NHR-CHR domains in which three helical NHR peptides formed a central core and three helical CHR peptides packed into the grooves on the surface of the central core.

Expression Data

Expression Detail
Antibody Labeling
Phenotype Data

Phenotype Detail
Acknowledgments
This image is the copyrighted work of the attributed author or publisher, and ZFIN has permission only to display this image to its users. Additional permissions should be obtained from the applicable author or publisher of the image. Full text @ PLoS Pathog.