Untitled

Abstract

Introduction: Gliadin intake causes celiac disease in selected population of Homo sapiens. Short motifs in α/β gliadin wheat protein were behind this food related disorder. Materials and Methods: Fold based template selection software GenTHREADER was considered for template selection and Modeller software was used for modelling wheat gliadin. T-Coffee software was used for the sequence alignment. Finally, antigenic region was identified. Results: Through in silico based study, we identified a novel motif 'HNxxH' in α/β gliadin wheat gliadin in C-terminal region which shows striking resemblance with the helical zinc binding motif 'HExxH' of metalloproteases.Interestingly, this short segment of gliadin is reported to be both an antigen and toxin which aligns well with the zinc binding site of the metalloproteases. Sequence analysis reports a spatial arrangement of the first two histidine residues from predicted motif of gliadin very much similar to the arrangement exhibited by the histidine residues in the selected metalloproteases like Astacin, Matrix metalloproteases and Predicted metal-dependent hydrolase. Additionally, glutamic acid, glycine and histidine from 2 nd , 8 th and 11 th position were substituted by asparagine, isoleucine and glutamine, respectively in this domain. Conclusion: A wet lab based analysis could certainly confirm the evolutionary relatedness of both gliadin and metalloproteases from sequential, structural and immunological perspective.