Vicilin is a
legumin Legumin is family of globular proteins obtained from beans, peas, lentils, vetches, hemp (specifically edestin) and other leguminous seeds. Edestin is a biologically active legumin protein that is digestible for human bodies. Garden peas are a commo ...
-associated
globulin protein. Vicilin can be described as a storage protein found in
legumes such as the
pea or
lentil
The lentil (''Lens culinaris'' or ''Lens esculenta'') is an edible legume. It is an annual plant known for its lens-shaped seeds. It is about tall, and the seeds grow in pods, usually with two seeds in each. As a food crop, the largest pro ...
. Vicilin is a protein that protects plants from
fungi
A fungus (plural, : fungi or funguses) is any member of the group of Eukaryote, eukaryotic organisms that includes microorganisms such as yeasts and Mold (fungus), molds, as well as the more familiar mushrooms. These organisms are classified ...
and
microorganism
A microorganism, or microbe,, ''mikros'', "small") and ''organism'' from the el, ὀργανισμός, ''organismós'', "organism"). It is usually written as a single word but is sometimes hyphenated (''micro-organism''), especially in olde ...
. It has been hypothesized it's an allergen in pea allergy responses.
Function of Vicilin
Vicilin is a globulin present in
legumes that assists the storage of proteins.
Vicilins are 7S globulins. Sucrose binding, antifungal capabilities, and
oxidative stress are a few of the globulin's functions. Vicilin peptides produced by digestion using
trypsin or
chymotrypsin offer anti-hypersensitive properties.
Vicilin's function was best understood because to the addition of the copper ligand. Vicilin has various significant residues, four of which are involved in copper ion coordination. Vicilin belongs to the cupin family of proteins, therefore metal ligand coordination is common, but Vicilin is the only seed storage protein in this family known to have copper. Due to various enzymatic activities, this inclusion is crucial, because Vicilin's function and mechanism are impacted by these functions.
Vicilin Structure
Vicilin is made up of one alpha subunit, a single
glycerol
Glycerol (), also called glycerine in British English and glycerin in American English, is a simple triol compound. It is a colorless, odorless, viscous liquid that is sweet-tasting and non-toxic. The glycerol backbone is found in lipids know ...
, and a phosphate ion. The addition of a copper ligand is what helps the structure work out.
The
N-terminus and
C-terminus fold into cupin folds to produce conserved beta barrels. Cupin folds cluster in seed storage proteins, and the presence of a metal ligand influences the protein's catalytic action. The C-terminus and N-terminus generate a cupin fold that is symmetrically centered off the axis. This axis is responsible for all copper ligand incorporation. This copper center's structure has four main residues: Cys-338, Tyr-67, His-340, and His-379. The copper ligand is coupled by a
trigonal planar structure generated by cysteine's sulfur. The bond formed by a
hydroxyl group attached to Tyr-67 is longer than the previous three. The enzymatic activity is connected to copper binding via histidine residues. These copper ligands are known to perform a catalytic function on
proteins.
This copper center's structure has four main residues: Cys-338, Tyr-67, His-340, and His-379. The copper ligand is coupled by a
trigonal planar structure generated by cysteine's sulfur. The bond formed by a
hydroxyl group attached to Tyr-67 is longer than the previous three. The enzymatic activity is connected to copper binding via histidine residues. These copper ligands are known to perform a catalytic function on
proteins.
Allergen Related Information
Vicilin is a significant allergen found in legumes.
The LgE binding proteins found were closely related and belonged to the 7S globulin family of seed storage proteins, which helped identify the
allergen.
Cross-reactions with various legumes are common when Pis s 1 and vicilins are combined in other seeds.
Major Vicilin Allergens[Barre, Annick et al. “Vicilin Allergens of Peanut and Tree Nuts (walnut, Hazelnut and Cashew Nut) Share Structurally Related IgE-Binding Epitopes.” ''Molecular immunology'' 45.5 (2008): 1231–1240. Web.]
# Ana o 1 in cashew nut
# Ara h 1 in peanut
# Jug r 2 in walnut
# Cor a 11 in hazelnut
Vicilins have similar amino acid sequences and cross-reactivity happen between vicilin allergens.
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Plant proteins