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.