Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Aug 30;12:14754. doi: 10.1038/s41598-022-18580-3

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Conservation of antibody epitope in different species and reverse engineering of murine FGF23 to bind Burosumab. (a) The amino acid sequence alignment of FGF23 across binder (monkey and rabbit) and non-binder species (mouse and rat) is shown in a clustal omega format. The three distinct epitope regions (red box) were well conserved across, albeit with key species-specific differences. The residues that differentiate those binder species (monkey and rabbit) from non-binder species (mouse and rat) are shaded in yellow. The residues that make contact with Burosumab based on pose27 are colored in red. Secondary structures: β strand, α-helix, and a single disulfide formation between cysteine 93 and 113 are annotated as red arrow, red helix, and purple line, respectively. (b) The four putative cross-species determining residues: N49, R76, H117, and S159 (human FGF23 numbering) were mapped onto the surface of human and mouse FGF23. (c) Binding activity of mouse FGF23 mutants with reverse mutations measured by indirect ELISA. Combination of three reverse mutations: T49N, Q117H, and A159S was able to rescue mouse FGF23 binding to Burosumab nearly similar to the human FGF23 wild type. Curves were drawn by GraphPad Prism version 8.4.3. A450 refers to absorbance at 450 nm. Structures were created by PyMOL version 2.2.0.