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

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

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)
104 Downloads (Pure)

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.

Original languageEnglish
Article number7740
JournalScientific Reports
Volume11
Issue number1
DOIs
Publication statusPublished - Dec 2021

Fingerprint

Dive into the research topics of 'Identification of chlorophyll a-b binding protein AB96 as a novel TGFβ1 neutralizing agent'. Together they form a unique fingerprint.

Cite this