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Identification of chlorophyll a-b binding protein AB96 as a novel TGFβ1 neutralizing agent

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Steven Lynham, Fabio Grundland Freie, Natasha Puri, Nicola O'Reilly, Graham Mitchell, Timothy Wells, Merlin Willcox, Richard Beatson

Original languageEnglish
Article number7740
JournalScientific Reports
Volume11
Issue number1
DOIs
Accepted/In press15 Mar 2021
PublishedDec 2021

Bibliographical note

Funding Information: Professor Joy Burchell (KCL) for allowing this research to be carried out in her laboratory, and support. Professor Brian de Sousa (LSHTM/UCL) for advice and strategic input. Dr Sandrine Sellam (Bio-Techne) for providing reagents. Professor Simon Croft (LSHTM) and Professor Adrian Hayday (KCL/CRICK) for support. Professor Daniel Rifkin (NYU) for the use of the TGFβ1 reporter cell line. Dr Marc Davies for helpful discussion. Finally, Kato Sailus .K and Wasswa Drake .D for sharing their knowledge of this plant, inspiring this project and providing materials. This work was supported by MRC Grant MR/R000026/1. Publisher Copyright: © 2021, The Author(s). Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

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Abstract

The discovery of compounds and proteins from plants has greatly contributed to modern medicine. Vernonia amygdalina Del. (Compositae) is used by humans and primates for a variety of conditions including parasitic infection. This paper describes the serendipitous discovery that V. amygdalina extract was able to bind to, and functionally inhibit, active TGFβ1. The binding agent was isolated and identified as chlorophyll a-b binding protein AB96. Given that active TGFβ1 contributes to the pathology of many infectious diseases, inhibiting these processes may explain some of the benefits associated with the ingestion of this species. This is the first plant-derived cytokine-neutralizing protein to be described and paves the way for further such discoveries.

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