Rubber Elongation Factor (REF), a Major Allergen Component in Hevea brasiliensis Latex Has Amyloid Properties
Open Access
- 25 October 2012
- journal article
- research article
- Published by Public Library of Science (PLoS) in PLOS ONE
- Vol. 7 (10), e48065
- https://doi.org/10.1371/journal.pone.0048065
Abstract
REF (Hevb1) and SRPP (Hevb3) are two major components of Hevea brasiliensis latex, well known for their allergenic properties. They are obviously taking part in the biosynthesis of natural rubber, but their exact function is still unclear. They could be involved in defense/stress mechanisms after tapping or directly acting on the isoprenoid biosynthetic pathway. The structure of these two proteins is still not described. In this work, it was discovered that REF has amyloid properties, contrary to SRPP. We investigated their structure by CD, TEM, ATR-FTIR and WAXS and neatly showed the presence of β-sheet organized aggregates for REF, whereas SRPP mainly fold as a helical protein. Both proteins are highly hydrophobic but differ in their interaction with lipid monolayers used to mimic the monomembrane surrounding the rubber particles. Ellipsometry experiments showed that REF seems to penetrate deeply into the monolayer and SRPP only binds to the lipid surface. These results could therefore clarify the role of these two paralogous proteins in latex production, either in the coagulation of natural rubber or in stress-related responses. To our knowledge, this is the first report of an amyloid formed from a plant protein. This suggests also the presence of functional amyloid in the plant kingdom.Keywords
This publication has 64 references indexed in Scilit:
- Metabolic routes affecting rubber biosynthesis in Hevea brasiliensis latexJournal of Experimental Botany, 2011
- MEGA5: Molecular Evolutionary Genetics Analysis Using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony MethodsMolecular Biology and Evolution, 2011
- Recruitment of Class I Hydrophobins to the Air:Water Interface Initiates a Multi-step Process of Functional Amyloid FormationOnline Journal of Public Health Informatics, 2011
- The toxicity of an “artificial” amyloid is related to how it interacts with membranesPrion, 2010
- The protein kingdom extended: Ordered and intrinsically disordered proteins, their folding, supramolecular complex formation, and aggregationProgress in Biophysics and Molecular Biology, 2010
- Amyloid fibers provide structural integrity to Bacillus subtilis biofilmsProceedings of the National Academy of Sciences of the United States of America, 2010
- The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerizationProceedings of the National Academy of Sciences of the United States of America, 2007
- Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteinsNature Biotechnology, 2004
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Microhelices in Hevea latexJournal of Ultrastructure Research, 1975