Conclusion
Pathogens have evolved a large number of ways of impersonating human proteins over a period of time. Pathogen proteins may mimic domain and motifs of the first interactors of the interacting host protein, and thus disturb the various signalling pathways of the humans. Imitate DB lists all the mimicked domains and motifs among HP-PPIs. The integration of HP-PPI data with domain and domain/motif mimicry is likely to predict the mimicry candidates with higher confidence. An exception to this would be when the proteins in a DLP or MLP have distinct temporal or spatial interaction. The limitation of our method is that the mimicry candidates will only be identified for those organisms and proteins for which the experimental PPIs have been reported in the databases. The curated information in ImitateDB will help in identifying frequent, unique, and novel mimicry domains and motifs among the interacting hosts and pathogens. Additionally, MLPs or DLPs allows us to easily identify and model the host protein motif or domain at which the competition for binding sites is taking place. The disruption of these HP-PPIs can be regarded as a strategy for developing novel broad-spectrum therapeutics against multiple infectious diseases.
Author Contributions
ST carried out data cleaning, enrichment and organisation, development of the database, analysis, and manuscript preparation. VB developed the backend and front end of the web interface. TM carried out data acquisition and cleaning. S.B. was involved in conception, design, analysis and supervision of the study. The manuscript was reviewed by all the authors.