Oleosin | |||||||||
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Identifiers | |||||||||
Symbol | Oleosin | ||||||||
Pfam | PF01277 | ||||||||
Pfam clan | CL0111 | ||||||||
InterPro | IPR000136 | ||||||||
PROSITE | PDOC00639 | ||||||||
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Oleosins are structural proteins found in vascular plant oil bodies and in plant cells. Oil bodies are not considered organelles because they have a single layer membrane and lack the pre-requisite double layer membrane in order to be considered an organelle. They are found in plant parts with high oil content that undergo extreme desiccation as part of their maturation process, and help stabilize the bodies. [1]
Oleosins are proteins of 16 kDa to 24 kDa and are composed of three domains: an N-terminal hydrophilic region of variable length (from 30 to 60 residues); a central hydrophobic domain of about 70 residues and a C-terminal amphipathic region of variable length (from 60 to 100 residues). The central hydrophobic domain is proposed to be made up of beta-strand structure and to interact with the lipids. It is the only domain whose sequence is conserved. [2] Models show oleosins having a hairpin-like hydrophobic shape that is inserted inside the triacylglyceride (TAG), while the hydrophilic parts are left outside oil bodies. [3]
Oleosins have been found on oil bodies of seeds, tapetum cells, and pollen but not fruits. Instead of a stabilizer of oil bodies, oleosins are believed to be involved in water-uptaking of pollen on stigma.
Allergic reactions to oleosins from hazelnut, peanut and sesame oils have been confirmed, ranging from contact dermatitis to anaphylactic shock. [4] [5] [6] [7] [8] These oil body associated proteins are at ~14 and ~17 kDa, named, respectively, Ses i 5 and Ses i 4. [5] [7] Commercial-grade peanut oil is often highly refined, which makes it safe for most peanut allergic individuals. In contrast, commercial-grade sesame oil is typically an unrefined product with a measurably higher protein content. [6] In addition to being a food ingredient, sesame oil can be present in drug products, dietary supplements and topically applied cosmetics. [8]
Oleosins provide an easy way of purifying proteins which have been produced recombinantly in plants. If the protein is made as a fusion protein with oleosin and a protease recognition site is incorporated between them, the fusion protein will sit in the membrane of the oil body, which can be easily isolated by centrifugation. The oil droplets can then be mixed with aqueous medium again, and oleosin cleaved from the protein of interest. Centrifugation will cause two phases to separate again, and the aqueous medium now contains the purified protein.
Allergies, also known as allergic diseases, are various conditions caused by hypersensitivity of the immune system to typically harmless substances in the environment. These diseases include hay fever, food allergies, atopic dermatitis, allergic asthma, and anaphylaxis. Symptoms may include red eyes, an itchy rash, sneezing, coughing, a runny nose, shortness of breath, or swelling. Note that food intolerances and food poisoning are separate conditions.
The peanut, also known as the groundnut, goober (US), goober pea, pindar (US) or monkey nut (UK), is a legume crop grown mainly for its edible seeds. It is widely grown in the tropics and subtropics by small and large commercial producers, both as grain legume and as an oil crop. Atypically among legumes, peanut pods develop underground leading botanist Carl Linnaeus to name peanuts hypogaea, which means "under the earth".
An allergen is an otherwise harmless substance that triggers an allergic reaction in sensitive individuals by stimulating an immune response.
Sesame is a plant in the genus Sesamum, also called simsim, benne or gingelly. Numerous wild relatives occur in Africa and a smaller number in India. It is widely naturalized in tropical regions around the world and is cultivated for its edible seeds, which grow in pods. World production in 2018 was 6 million tonnes, with Sudan, Myanmar, and India as the largest producers.
A nut is a fruit consisting of a hard or tough nutshell protecting a kernel which is usually edible. In general usage and in a culinary sense, many dry seeds are called nuts. In a botanical context, "nut" implies that the shell does not open to release the seed (indehiscent).
A food allergy is an abnormal immune response to food. The symptoms of the allergic reaction may range from mild to severe. They may include itchiness, swelling of the tongue, vomiting, diarrhea, hives, trouble breathing, or low blood pressure. This typically occurs within minutes to several hours of exposure. When the symptoms are severe, it is known as anaphylaxis. A food intolerance and food poisoning are separate conditions, not due to an immune response.
Latex allergy is a medical term encompassing a range of allergic reactions to the proteins present in natural rubber latex. It generally develops after repeated exposure to products containing natural rubber latex. When latex-containing medical devices or supplies come in contact with mucous membranes, the membranes may absorb latex proteins. In some susceptible people, the immune system produces antibodies that react immunologically with these antigenic proteins. Many items contain or are made from natural rubber, including shoe soles, pen grips, hot water bottles, elastic bands, rubber gloves, condoms, baby-bottle nipples, and balloons; consequently, there are many possible routes of exposure that may trigger a reaction. People with latex allergies may also have or develop allergic reactions to some fruits, such as bananas.
Allergen immunotherapy, also known as desensitization or hypo-sensitization, is a medical treatment for environmental allergies and asthma. Immunotherapy involves exposing people to larger and larger amounts of allergens in an attempt to change the immune system's response.
Peanut allergy is a type of food allergy to peanuts. It is different from tree nut allergies, because peanuts are legumes and not true nuts. Physical symptoms of allergic reaction can include itchiness, hives, swelling, eczema, sneezing, asthma attack, abdominal pain, drop in blood pressure, diarrhea, and cardiac arrest. Anaphylaxis may occur. Those with a history of asthma are more likely to be severely affected.
Oral allergy syndrome (OAS) or pollen-food allergy syndrome (PFAS) is a type of allergy classified by a cluster of allergic reactions in the mouth and throat in response to eating certain fruits, nuts, and vegetables. It typically develops in adults with hay fever. It is not usually serious.
Egg allergy is an immune hypersensitivity to proteins found in chicken eggs, and possibly goose, duck, or turkey eggs. Symptoms can be either rapid or gradual in onset. The latter can take hours to days to appear. The former may include anaphylaxis, a potentially life-threatening condition which requires treatment with epinephrine. Other presentations may include atopic dermatitis or inflammation of the esophagus.
A tree nut allergy is a hypersensitivity to dietary substances from tree nuts and edible tree seeds causing an overreaction of the immune system which may lead to severe physical symptoms. Tree nuts include almonds, Brazil nuts, cashews, chestnuts, filberts/hazelnuts, macadamia nuts, pecans, pistachios, shea nuts and walnuts.
Wheat allergy is an allergy to wheat which typically presents itself as a food allergy, but can also be a contact allergy resulting from occupational exposure. Like all allergies, wheat allergy involves immunoglobulin E and mast cell response. Typically the allergy is limited to the seed storage proteins of wheat. Some reactions are restricted to wheat proteins, while others can react across many varieties of seeds and other plant tissues. Wheat allergy is rare. Prevalence in adults was estimated to be 0.21% in a 2012 study in Japan.
Eosinophil cationic protein (ECP) also known as ribonuclease 3 is a basic protein located in the eosinophil primary matrix. In humans, the eosinophil cationic protein is encoded by the RNASE3 gene.
An oil body is a lipid-containing structure found in plant cells. The term can refer to at least two distinct kinds of structures in different kinds of plants.
Plant lipid transfer proteins, also known as plant LTPs or PLTPs, are a group of highly-conserved proteins of about 7-9kDa found in higher plant tissues. As its name implies, lipid transfer proteins facilitate the shuttling of phospholipids and other fatty acid groups between cell membranes. LTPs are divided into two structurally related subfamilies according to their molecular masses: LTP1s (9 kDa) and LTP2s (7 kDa). Various LTPs bind a wide range of ligands, including fatty acids with a C10–C18 chain length, acyl derivatives of coenzyme A, phospho- and galactolipids, prostaglandin B2, sterols, molecules of organic solvents, and some drugs.
Ara h 1 is a seed storage protein from Arachis hypogaea (peanuts). It is a heat stable 7S vicilin-like globulin with a stable trimeric form that comprises 12-16% of the total protein in peanut extracts. Ara h 1 is known because sensitization to it was found in 95% of peanut-allergic patients from North America. In spite of this high percentage, peanut-allergic patients of European populations have fewer sensitizations to Ara h 1.
Vicilin is a legumin-associated globulin protein. It is a storage protein found in legumes such as the pea or lentil that protects plants from fungi and microorganism. It is believed to be an allergen in pea and peanut allergy responses.
Ara h 3 is a seed storage protein from Arachis hypogaea (peanuts). It is a heat stable 11S legumin-like globulin with a stable trimeric form that comprises 19% of the total protein in peanut extracts.
A food allergy to sesame seeds has prevalence estimates in the range of 0.1–0.2% of the general population, and are higher in the Middle East and other countries where sesame seeds are used in traditional foods. Reporting of sesame seed allergy has increased in the 21st century, either due to a true increase from exposure to more sesame foods or due to an increase in awareness. Increasing sesame allergy rates have induced more countries to regulate food labels to identify sesame ingredients in products and the potential for allergy. In the United States, sesame became the ninth food allergen with mandatory labeling, effective 1 January 2023.