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

. 2023 Jan 13;6:42. doi: 10.1038/s42003-023-04431-y

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

© The Author(s) 2023

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 2 — a Illustration of the aE11-CDRs (coloured, blue, green, red) on the antibody and its corresponding primary sequence. b Focused view of the opened aE11-polyC9 interface (split by 180°) that defines the MAC neoepitope. Left: close-up structure of the aE11-CDRs. Right: Transparent surface and cartoon illustration of the leading (light blue) and lagging (grey) C9 subunits, where the footprints of heavy and light chain binding regions are shaded red and yellow, respectively. A dashed line illustrates the buried surfaces of the interface. c–e Key regions of antibody binding to C9. Locations of these regions correspond to the boxed regions in (b). Mutated residues for validation studies are encircled in a red outline. f Slot immunoblot of aE11 binding to the oligomeric C9 component of whole MAC. Oligomeric human C9 is recognised by aE11, but not oligomeric mouse C9. MAC assembly intermediates (C5b6, C5b-7, C5b-8) are included as controls. Concentrations of C5b6 are marked for each condition. The C7, C8αβγ, and C9 concentrations were constant at 30, 30, and 7 nM, respectively. g Sequence alignment of the linear regions of human and murine C9 that contribute to the quaternary discontinuous epitope.