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|Title:||Structures of two major allergens, Bla g 4 and Per a 4, from cockroaches and their IgE binding epitopes||Authors:||Yih, W.T.
|Issue Date:||30-Jan-2009||Citation:||Yih, W.T., Siew, L.C., Tan, C.O., Le, Y.Y., Yuen, S.T., Fook, T.C., Sivaraman, J., Yu, K.M. (2009-01-30). Structures of two major allergens, Bla g 4 and Per a 4, from cockroaches and their IgE binding epitopes. Journal of Biological Chemistry 284 (5) : 3148-3157. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M807209200||Abstract:||Inhalant allergens from cockroaches are an important cause of asthma to millions of individuals worldwide. Here we report for the first time the structures of two major cockroach allergens, Bla g 4 and Per a 4, that adopt a typical lipocalin fold but with distinct structural features as compared with other known lipocalin allergens. Both Bla g 4 and Per a 4 contain two long-range disulfide bonds linking the N and C termini to a β-barrel. The C-terminal helix of Bla g 4 is bent and greatly extended toward the N terminus. Bla g 4 is found to be a monomer, whereas Per a 4 exists as a dimer in solution with a novel dimeric interface involving residues from loops at the top and bottom of the β-barrel. Putative ligand binding sites of both allergens are determined by docking of the juvenile hormone III inside the β-barrel and found to interact with the ligand using non-conserved residues. Bla g 4 and Per a 4 are found to be cross-reactive in sera IgE binding, at least in the Singaporean Chinese population tested. A major IgE binding epitope unique to Per a 4 is found on the loops at the bottom of the β-barrel that may aid the development of hypoallergens for immunotherapy. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.||Source Title:||Journal of Biological Chemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/101780||ISSN:||00219258||DOI:||10.1074/jbc.M807209200|
|Appears in Collections:||Staff Publications|
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