Pro-hevein
| Pro-hevein | |||||||
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_1HEV.png) | |||||||
| Identifiers | |||||||
| Symbol | HEV1 | ||||||
| CAS number | |||||||
| 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]
The conformational epitope on hevein is called Hev b 6.02.[8][9]
References
- ^ Broekaert I, Lee HI, Kush A, Chua NH, Raikhel N (Oct 1990). "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. doi:10.1073/pnas.87.19.7633. PMC 54802. PMID 2217194.
- ^ Gidrol X, Chrestin H, Tan HL, Kush A (Mar 1994). "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. PMID 8132664.
- ^ Van Parijs J, Broekaert WF, Goldstein IJ, Peumans WJ (Jan 1991). "Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex". Planta. 183 (2): 258–64. doi:10.1007/BF00197797. PMID 24193629.
- ^ Alenius H, Kalkkinen N, Reunala T, Turjanmaa K, Palosuo T (Feb 1996). "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. PMID 8568268.
- ^ Dìaz-Perales A, Sánchez-Monge R, Blanco C, Lombardero M, Carillo T, Salcedo G (Mar 2002). "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. doi:10.1046/j.1365-2222.2002.01306.x. PMID 11940077.
- ^ Diaz-Perales A, Collada C, Blanco C, Sánchez-Monge R, Carrillo T, Aragoncillo C, Salcedo G (Jul 1998). "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. doi:10.1016/s0091-6749(98)70063-6. PMID 9679856.
- ^ Potter S, Uknes S, Lawton K, Winter AM, Chandler D, DiMaio J, Novitzky R, Ward E, Ryals J (1993). "Regulation of a hevein-like gene in Arabidopsis". Molecular Plant-Microbe Interactions. 6 (6): 680–5. doi:10.1094/mpmi-6-680. PMID 8118053.
- ^ Reyes-López CA, Hernández-Santoyo A, Pedraza-Escalona M, Mendoza G, Hernández-Arana A, Rodríguez-Romero A (Jan 2004). "Insights into a conformational epitope of Hev b 6.02 (hevein)". Biochemical and Biophysical Research Communications. 314 (1): 123–30. doi:10.1016/j.bbrc.2003.12.068. PMID 14715255.
- ^ Pedraza-Escalona M, Becerril-Luján B, Agundis C, Domínguez-Ramírez L, Pereyra A, Riaño-Umbarila L, Rodríguez-Romero A (Feb 2009). "Analysis of B-cell epitopes from the allergen Hev b 6.02 revealed by using blocking antibodies". Molecular Immunology. 46 (4): 668–76. doi:10.1016/j.molimm.2008.08.282. PMID 18930549.