Skip to main content
Fig. 1 | Journal of Biomedical Science

Fig. 1

From: Neutralizing antibodies targeting a novel epitope on envelope protein exhibited broad protection against flavivirus without risk of disease enhancement

Fig. 1

Sequence alignment and PyMOL structural analysis of flavivirus E protein conserved bc loop epitope. A Alignment of the E protein amino acid sequences of flaviviruses, highlighting the RCPTTGE and RCPTQGE epitope region with a green box. Amino acid positions are numbered from 1 to 112. Completely conserved epitope residues are labeled in red (aa 74, 75, 78 and 79), while highly conserved epitope residues are colored in blue (aa 73, 76 and 77). B Ribbon structure of the E dimer from DENV-2 (PDB: 1TG8) with the bc loop (RCPTQGE) highlighted in magenta and annotated with residue numbers 73–79. C Ribbon structures of E proteins from various viruses, including JEV (PDB: 5MV2), DENV-1 (PDB: 7A3R), DENV-2 (PDB: 1TG8), DENV-3 (PDB: 1UZG), DENV-4 (PDB: 3UAJ), and ZIKV (PDB: 5JHM), were aligned using PyMOL. The alignment highlights the conserved bc loops among the viruses, with JEV residues 73–79 (RCPTTGE) and DENV-2 residues 73–79 (RCPTQGE) annotated with residue numbers and colored in yellow and magenta, respectively

Back to article page