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Identification of chlorophyll a-b binding protein AB96 as a novel TGFβ1 neutralizing agent
- Source :
- Scientific Reports, Vol 11, Iss 1, Pp 1-7 (2021), Scientific Reports, Lynham, S, Grundland Freie, F, Puri, N, O'Reilly, N, Mitchell, G, Wells, T, Willcox, M & Beatson, R 2021, ' Identification of chlorophyll a-b binding protein AB96 as a novel TGFβ1 neutralizing agent ', Scientific Reports, vol. 11, no. 1, 7740 . https://doi.org/10.1038/s41598-021-87454-x
- Publication Year :
- 2021
- Publisher :
- Nature Portfolio, 2021.
-
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.
- Subjects :
- 0301 basic medicine
Modern medicine
Science
Immunology
030231 tropical medicine
Asteraceae
Biology
Parasitic infection
Article
Transforming Growth Factor beta1
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Amino Acid Sequence
Plants, Medicinal
Multidisciplinary
Immune evasion
Binding protein
Vernonia amygdalina
biology.organism_classification
030104 developmental biology
chemistry
Biochemistry
Chlorophyll
Cytokines
Infectious diseases
Medicine
Identification (biology)
Chlorophyll Binding Proteins
Peptides
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 20452322
- Volume :
- 11
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Scientific Reports
- Accession number :
- edsair.doi.dedup.....5799dad87b1afd7a066090e73a045c7c
- Full Text :
- https://doi.org/10.1038/s41598-021-87454-x