Three dimensional structure directs T-cell epitope dominance associated with allergy 英文参考文献.docVIP

Clinical and Molecular Allergy BioMedCentral Research Open Access Three dimensional structure directs T-cell epitope dominance associated with allergy Scott J Melton*1 and Samuel J Landry2 Address: 1Biomedical Sciences Graduate Program, Tulane University Health Sciences Center, New Orleans, LA, 70112, USA and 2Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, LA, 70112, USA Email: Scott J Melton* - smelton@; Samuel J Landry - landry@ * Corresponding author Published: 15 September 2008 Received: 6 February 2008 Accepted: 15 September 2008 Clinical and Molecular Allergy 2008, 6:9 doi:10.1186/1476-7961-6-9 This article is available from: /content/6/1/9 ? 2008 Melton and Landry; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Abstract Background: CD4+ T-cell epitope immunodominance is not adequately explained by peptide selectivity in class II major histocompatibility proteins, but it has been correlated with adjacent segments of conformational flexibility in several antigens. Methods: The published T-cell responses to two venom allergens and two aeroallergens were used to construct profiles of epitope dominance, which were correlated with the distribution of conformational flexibility, as measured by crystallographic B factors, solvent-accessible surface, COREX residue stability, and sequence entropy. Results: Epitopes associated with allergy tended to be excluded from and lie adjacent to flexible segments of the allergen. Conclusion: During the initiation of allergy, the N- and/or C-terminal ends of proteolytic processing intermediates were preferentially loaded into antigen presenting proteins for the priming of CD4+ T cells. CD4+