Biology:Pro-hevein
| Pro-hevein | |||||||
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_1HEV.png) | |||||||
| Identifiers | |||||||
| Organism | ? | ||||||
| Symbol | HEV1 | ||||||
| CAS number | 137295-60-4 | ||||||
| UniProt | P02877 | ||||||
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Pro-hevein (Alternative name: Major hevein, gene name: HEV1) is a wound-induced[1] and a lectin-like protein from Hevea brasiliensis (rubber tree) where it is involved in the coagulation of latex.[2]
The 187 amino-acid propeptide pro-hevein is cleaved in two fragments: a N-terminal 43 amino-acid Hevein bearing a chitin-binding type-1 domain (also known as CBM18 carbohydrate-binding module) that binds to chitin and a 138 amino-acid Win-like protein bearing a Barwin domain.
It has antifungal properties.[3]
Role of hevein in latex allergy
Hevein is the main IgE-binding epitope of the major latex allergen prohevein[4] as are hevein-like protein domains in fruit class I chitinases.[5] Therefore it is a possible cause for allergen cross-reactivity between latex and banana or other fruits like chestnuts or avocadoes.[6] Hevein-like genes can be found in many plants including Arabidopsis thaliana.[7]
Hevein is called Hev b 6 under the WHO allergen nomenclature.[8][9] There are three entries under this classification, corresponding to the conformational epitopes Hev b 6.01, Hev b 6.03, and Hev b 6.03. They correspond to the full Pro-Havein protein, the matur Hevein (N-terminal), and the C-terminal Barwin domain respectively.[10]
References
- ↑ "Wound-induced accumulation of mRNA containing a hevein sequence in laticifers of rubber tree (Hevea brasiliensis)". Proceedings of the National Academy of Sciences of the United States of America 87 (19): 7633–7. Oct 1990. doi:10.1073/pnas.87.19.7633. PMID 2217194. Bibcode: 1990PNAS...87.7633B.
- ↑ "Hevein, a lectin-like protein from Hevea brasiliensis (rubber tree) is involved in the coagulation of latex". The Journal of Biological Chemistry 269 (12): 9278–83. Mar 1994. doi:10.1016/S0021-9258(17)37104-1. PMID 8132664.
- ↑ "Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex". Planta 183 (2): 258–64. Jan 1991. doi:10.1007/BF00197797. PMID 24193629. https://deepblue.lib.umich.edu/bitstream/2027.42/47477/1/425_2004_Article_BF00197797.pdf.
- ↑ "The main IgE-binding epitope of a major latex allergen, prohevein, is present in its N-terminal 43-amino acid fragment, hevein". Journal of Immunology 156 (4): 1618–25. Feb 1996. PMID 8568268.
- ↑ "What is the role of the hevein-like domain of fruit class I chitinases in their allergenic capacity?". Clinical and Experimental Allergy 32 (3): 448–54. Mar 2002. doi:10.1046/j.1365-2222.2002.01306.x. PMID 11940077.
- ↑ "Class I chitinases with hevein-like domain, but not class II enzymes, are relevant chestnut and avocado allergens". The Journal of Allergy and Clinical Immunology 102 (1): 127–33. Jul 1998. doi:10.1016/s0091-6749(98)70063-6. PMID 9679856.
- ↑ "Regulation of a hevein-like gene in Arabidopsis". Molecular Plant-Microbe Interactions 6 (6): 680–5. 1993. doi:10.1094/mpmi-6-680. PMID 8118053.
- ↑ "Insights into a conformational epitope of Hev b 6.02 (hevein)". Biochemical and Biophysical Research Communications 314 (1): 123–30. Jan 2004. doi:10.1016/j.bbrc.2003.12.068. PMID 14715255.
- ↑ "Analysis of B-cell epitopes from the allergen Hev b 6.02 revealed by using blocking antibodies". Molecular Immunology 46 (4): 668–76. Feb 2009. doi:10.1016/j.molimm.2008.08.282. PMID 18930549.
- ↑ "Hev b 6 Allergen Details". http://www.allergen.org/viewallergen.php?aid=364.
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