Linked Life Data

10820263

Source:http://linkedlifedata.com/resource/pubmed/id/10820263

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2000-6-21
pubmed:abstractText
In the past decade, there has been an increase in allergic reactions to peanut proteins, sometimes resulting in fatal anaphylaxis. The development of improved methods for diagnosis and treatment of peanut allergies requires a better understanding of the structure of the allergens. Ara h 1, a major peanut allergen belonging to the vicilin family of seed storage proteins, is recognized by serum IgE from >90% of peanut-allergic patients. In this communication, Ara h 1 was shown to form a highly stable homotrimer. Hydrophobic interactions were determined to be the main molecular force holding monomers together. A molecular model of the Ara h 1 trimer was constructed to view the stabilizing hydrophobic residues in the three dimensional structure. Hydrophobic amino acids that contribute to trimer formation are at the distal ends of the three dimensional structure where monomer-monomer contacts occur. Coincidentally, the majority of the IgE-binding epitopes are also located in this region, suggesting that they may be protected from digestion by the monomer-monomer contacts. On incubation of Ara h 1 with digestive enzymes, various protease-resistant fragments containing IgE-binding sites were identified. The highly stable nature of the Ara h 1 trimer, the presence of digestion resistant fragments, and the strategic location of the IgE-binding epitopes indicate that the quaternary structure of a protein may play a significant role in overall allergenicity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
164
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5844-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10820263-Acids, pubmed-meshheading:10820263-Adult, pubmed-meshheading:10820263-Allergens, pubmed-meshheading:10820263-Antigens, Plant, pubmed-meshheading:10820263-Arachis hypogaea, pubmed-meshheading:10820263-Binding Sites, Antibody, pubmed-meshheading:10820263-Computer Simulation, pubmed-meshheading:10820263-Digestive System, pubmed-meshheading:10820263-Epitopes, pubmed-meshheading:10820263-Glycoproteins, pubmed-meshheading:10820263-Humans, pubmed-meshheading:10820263-Hydrogen-Ion Concentration, pubmed-meshheading:10820263-Hydrolysis, pubmed-meshheading:10820263-Immunoglobulin E, pubmed-meshheading:10820263-Models, Molecular, pubmed-meshheading:10820263-Plant Proteins, pubmed-meshheading:10820263-Protein Conformation, pubmed-meshheading:10820263-Sodium Chloride, pubmed-meshheading:10820263-Structure-Activity Relationship
pubmed:year
2000
pubmed:articleTitle
Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation.
pubmed:affiliation
Departments ofPediatrics and Biochemistry and Molecular Biology and Biomedical Visualization Center, University of Arkansas for Medical Sciences, Arkansas Children's Hospital Research Institute, Little Rock, AR 72205, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't