title: P39, a novel soybean protein allergen, belongs to a plant-specific protein family and is present in protein storage vacuoles.
abstract: Soybean lecithins are seeing increasing use in industry as an emulsifier and food additive. They are also a growing source of human food allergies, which arise principally from the proteins fractionating with the lecithin fraction during manufacture. A previous study (Gu, X.; Beardslee, T.; Zeece, M.; Sarath, G.; Markwwell, J. Int Arch. Allergy Immunol. 2001, 126, 218-225) identified several allergenic proteins in soybean lecithins and a soybean IgE-binding protein termed P39 was discovered. However, very little was known about this protein except that it was coded by the soybean genome. This paper investigates key biological and immunological properties of this potential soybean lecithin allergen. P39 is encoded by a multigene family in soybeans and in several other higher plants. The soybean P39-1 protein and its essentially indistinguishable homologue, P39-2, have been cloned and studied. These proteins and their homologues belong to a family of plant-specific proteins of unknown function. In soybeans, P39-1 is seed specific, and its transcript levels are highest in developing seeds and decline during seed maturation. In contrast, P39 protein was detectable only in the fully mature, dry seed. Subcellular fractionation revealed that P39 protein was strongly associated with oil bodies; however, immunolocalization indicated P39 was distributed in the matrix of the protein storage vacuoles, suggesting that association with oil bodies was an artifact arising from the extraction procedure. By the use of recombinant techniques it has also been documented that IgE-binding epitopes are present on several different portions of the P39-1 polypeptide.
authors.affiliation: British Columbia Cancer Agency, Vancouver, British Columbia V5Z 1L3, Canada.
authors.forename: Ping
authors.initials: P
authors.lastname: Xiang
authors.forename: Lisa M
authors.initials: LM
authors.lastname: Baird
authors.forename: Rudolf
authors.initials: R
authors.lastname: Jung
authors.forename: Michael G
authors.initials: MG
authors.lastname: Zeece
authors.forename: John
authors.initials: J
authors.lastname: Markwell
authors.forename: Gautam
authors.initials: G
authors.lastname: Sarath
mesh_terms: D000485:Allergens / Q000032:analysis* / Q000276:immunology; D000595:Amino Acid Sequence; D052179:Antigens, Plant / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D005503:Food Additives / Q000737:chemistry; D015870:Gene Expression; D007073:Immunoglobulin E / Q000378:metabolism; D054709:Lecithins / Q000737:chemistry / Q000276:immunology; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000032:analysis; D011994:Recombinant Proteins; D012639:Seeds / Q000737:chemistry / Q000254:growth & development / Q000648:ultrastructure*; D016415:Sequence Alignment; D030262:Soybean Proteins / Q000032:analysis* / Q000276:immunology*; D014617:Vacuoles / Q000737:chemistry*
chemical_list: D000485:Allergens; D052179:Antigens, Plant; D005503:Food Additives; D054709:Lecithins; C529390:P39-1 allergen, Glycine max; D012333:RNA, Messenger; D011994:Recombinant Proteins; D030262:Soybean Proteins; D007073:Immunoglobulin E