Biology:Oleosin

From HandWiki
Oleosin
Identifiers
SymbolOleosin
PfamPF01277
Pfam clanCL0111
InterProIPR000136
PROSITEPDOC00639

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]

Components

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

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 highly refined, so the oleosins are removed, but commercial-grade sesame oil is typically an unrefined product with a measurable 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]

Usage

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.

References

  1. Hsieh, Kai; Anthony H.C. Huang (September 2005). "Lipid-rich tapetosomes in Brassica tapetum are composed of oleosin-coated oil droplets and vesicles, both assembled in and then detached from the endoplasmic reticulum". The Plant Journal 43 (6): 889–99. doi:10.1111/j.1365-313X.2005.02502.x. PMID 16146527. 
  2. "Characterization of the charged components and their topology on the surface of plant seed oil bodies". J. Biol. Chem. 267 (22): 15626–34. August 1992. doi:10.1016/S0021-9258(19)49582-3. PMID 1639802. 
  3. oleosin
  4. "Relevance of Lipophilic Allergens in Food Allergy Diagnosis". Curr Allergy Asthma Rep 17 (9): 61. August 2017. doi:10.1007/s11882-017-0731-0. PMID 28795292. 
  5. 5.0 5.1 "Oil body-associated hazelnut allergens including oleosins are underrepresented in diagnostic extracts but associated with severe symptoms". Clin Transl Allergy 4 (1): 4. February 2014. doi:10.1186/2045-7022-4-4. PMID 24484687. 
  6. 6.0 6.1 "Diagnosing IgE-mediated hypersensitivity to sesame by an immediate-reading "contact test" with sesame oil". J Allergy Clin Immunol 127 (6): 1627–29. June 2011. doi:10.1016/j.jaci.2011.01.050. PMID 21377720. 
  7. 7.0 7.1 "Identification of oleosins as major allergens in sesame seed allergic patients". Allergy 61 (3): 349–56. March 2006. doi:10.1111/j.1398-9995.2006.01013.x. PMID 16436145. 
  8. 8.0 8.1 "Sesame seed and sesame seed oil contain masked allergens of growing importance". Allergy 51 (12): 952–7. December 1996. doi:10.1111/j.1398-9995.1996.tb02141.x. PMID 9020427. 
This article incorporates text from the public domain Pfam and InterPro: IPR000136