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ImitateDB: A Resource for Domain and Motif Mimicry in Host and Pathogen Proteins
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  • Sonali Tayal,
  • Venugopal Bhatia,
  • Tanya Mehrotra,
  • Sonika Bhatnagar
Sonali Tayal
Netaji Subhas University of Technology
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Venugopal Bhatia
Netaji Subhas Institute of Technology
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Tanya Mehrotra
Netaji Subhas University of Technology
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Sonika Bhatnagar
Netaji Subhas University of Technology
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The host pathogen interactome can be visualized as a vast continuous network in which molecular mimicry of host proteins by pathogens constitutes a strategy to hijack the host pathways. Despite extensive work in this field, there is no dedicated resource for mimicked domains and motifs in host pathogen interactome. In this work, we collated all the data regarding the experimental host pathogen (HP) and host-host (HH) protein-protein interactions (PPIs). The domains and sequence linear motifs of the proteins were annotated using CD Search and ScanProsite. Host and pathogen proteins with a shared host interactor and similar domain/motif constitute a linear pair. A linear pair that exhibits global structural domain similarity (Domain linear pair; DLP) or local sequence motif similarity (Motif Linear Pair; MLP) has a high probability of being co-expressed and co-localized. 2,06,449 DLPs and 38,45,643 MLPs were identified in 50,812 experimental HP-PPIs and organized in a web- based resource, ImitateDB, accessible at http://imitatedb.sblab-nsit.net. ImitateDB provides user-friendly access to the mimicry data. It can be queried by protein UniProt ID, pathogen, domain, motif, or interaction detection method. The results are externally integrated using hyperlinked domain PSSM ID, motif ID and protein ID. Kinase, UL36, Smc and DEXDc were frequent DLP domains whereas Protein Kinase C, Casein Kinase 2, glycosylation and myristoylation sites were frequent MLP motifs. Novel DLP domains SANT, Tudor, PhoX and MLP motifs Microbodies C-terminal targeting signal, Ubiquitin-interacting motif and Lipocalin signature were proposed. ImitateDB constitutes a resource for researchers in the field of infectious diseases and microbiology.

Peer review status:UNDER REVIEW

07 Jul 2021Submitted to PROTEINS: Structure, Function, and Bioinformatics
08 Jul 2021Assigned to Editor
08 Jul 2021Submission Checks Completed
22 Jul 2021Reviewer(s) Assigned