Roy Debjani, Ghosh Debajyoti, Gupta-Bhattacharya Swati
Bioinformatics Centre, Bose Institute, Kolkata, India.
Biochem Biophys Res Commun. 2003 Jul 25;307(2):422-9. doi: 10.1016/s0006-291x(03)01193-8.
Cross-reactivity among allergens is of considerable scientific as well as clinical interest. Proteins belonging to the allergenic cyclophilin family share a high degree of sequence homology and are cross-reactive. Until date no three-dimensional structural information is available on these proteins and the shared structural features of the epitopes which are the most important determinants of cross-reactivity. Cyclophilins are also known to bind with the immuno-suppressive drug cyclosporin. Comparative molecular modeling of these allergenic cyclophilin proteins of different sources was performed in order to investigate the structural basis of their cross-reactivity. All the proteins studied revealed a similarity in the shape of the cross-reactive epitopes with varying degrees of accessibility. Cyclosporin binding and allergenic properties of these proteins were also found to be structurally related.
