Pro-hevein

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Pro-hevein
Hevein (hev b 6.02) 1HEV.png
Identifiers
Organism?
SymbolHEV1
CAS number 137295-60-4
UniProt P02877
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Structures Swiss-model
Domains InterPro

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]

Contents

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]

Related Research Articles

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<span class="mw-page-title-main">Antibody</span> Protein(s) forming a major part of an organisms immune system

An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses. The antibody recognizes a unique molecule of the pathogen, called an antigen. Each tip of the "Y" of an antibody contains a paratope that is specific for one particular epitope on an antigen, allowing these two structures to bind together with precision. Using this binding mechanism, an antibody can tag a microbe or an infected cell for attack by other parts of the immune system, or can neutralize it directly.

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Chitinases are hydrolytic enzymes that break down glycosidic bonds in chitin. They catalyse the following reaction:

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<span class="mw-page-title-main">Epitope mapping</span> Identifying the binding site of an antibody on its target antigen

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References

  1. 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. Bibcode:1990PNAS...87.7633B. doi: 10.1073/pnas.87.19.7633 . PMC   54802 . PMID   2217194.
  2. 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. doi: 10.1016/S0021-9258(17)37104-1 . PMID   8132664.
  3. Van Parijs J, Broekaert WF, Goldstein IJ, Peumans WJ (Jan 1991). "Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex" (PDF). Planta. 183 (2): 258–64. doi:10.1007/BF00197797. hdl: 2027.42/47477 . PMID   24193629. S2CID   2490528.
  4. 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.
  5. 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. hdl: 10553/128107 . PMID   11940077. S2CID   26003685.
  6. 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.
  7. 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.
  8. 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.
  9. 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.
  10. "Hev b 6 Allergen Details". www.allergen.org.