John A. Jenkins, PhD, Heimo Breiteneder, PhD, E. N. Clare Mills, PhD

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Volume 95, Issue 2, Pages (October 1998)

Presentation transcript:

Evolutionary distance from human homologs reflects allergenicity of animal food proteins John A. Jenkins, PhD, Heimo Breiteneder, PhD, E. N. Clare Mills, PhD Journal of Allergy and Clinical Immunology Volume 120, Issue 6, Pages 1399-1405 (December 2007) DOI: 10.1016/j.jaci.2007.08.019 Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 1 Distribution of animal food allergens into Pfam families. Allergens were from either version 2.1 of the InformAll (www.foodallergens.ifr.ac.uk; dark bars) or version 5.0 of FARRP (www.allergenonline.com; gray bars) databases. Pfam family names are given apart from very low density lipoprotein (VLDL), arginine kinase, and ovomucin, which represent proteins with multiple different domains. BPTI, Bovine pancreatic trypsin inhibitor. Journal of Allergy and Clinical Immunology 2007 120, 1399-1405DOI: (10.1016/j.jaci.2007.08.019) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 2 Unrooted dendrograms of tropomyosin (A) and parvalbumin (B) sequences. Representative allergens including the closest human homologs and homologs present in foods that have not been reported as allergens were selected for each family. The scale bar shows the branch length corresponding to 0.1 changes per residue, and identities were ordered by similarity to human α-parvalbumin. Journal of Allergy and Clinical Immunology 2007 120, 1399-1405DOI: (10.1016/j.jaci.2007.08.019) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 3 Conservation of residues on the contact surface of parvalbumins. A, B, D, E, The surface of carp β-parvalbumin colored to show conserved side (red) and main chain residues (pink), substituted side chain residues (green), and the C-terminal main chain (green). The ribbon diagram of carp parvalbumin shows the less conserved (C) and more conserved faces (F) with the calcium atoms as pink balls and a dotted molecular contact surface. Models show the less conserved face comparing (A) cod (Q90YK9) to carp (P02618), (B) cod (Q90YK9) to frog (P02617), and (D) cod (Q90YK9) to human being (P20472). E, The rotation of 180° of D around a vertical axis shows the more conserved calcium binding face comparing cod (Q90YK9) to human being (P20472). Journal of Allergy and Clinical Immunology 2007 120, 1399-1405DOI: (10.1016/j.jaci.2007.08.019) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions

Fig 4 Unrooted dendrogram of α-caseins and β-caseins. The human αS2-casein sequence is not expressed and was not used in this analysis. The scale bar shows the branch length corresponding to 0.1 changes per residue. Journal of Allergy and Clinical Immunology 2007 120, 1399-1405DOI: (10.1016/j.jaci.2007.08.019) Copyright © 2007 American Academy of Allergy, Asthma & Immunology Terms and Conditions