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ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions
Molecular mimicry of host proteins by pathogens constitutes a strategy to hijack the host pathways. At present, there is no dedicated resource for mimicked domains and motifs in the host–pathogen interactome. In this work, the experimental host–pathogen (HP) and host–host (HH) protein–protein intera...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Vienna
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9054641/ https://www.ncbi.nlm.nih.gov/pubmed/35487995 http://dx.doi.org/10.1007/s00726-022-03163-3 |
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author | Tayal, Sonali Bhatia, Venugopal Mehrotra, Tanya Bhatnagar, Sonika |
author_facet | Tayal, Sonali Bhatia, Venugopal Mehrotra, Tanya Bhatnagar, Sonika |
author_sort | Tayal, Sonali |
collection | PubMed |
description | Molecular mimicry of host proteins by pathogens constitutes a strategy to hijack the host pathways. At present, there is no dedicated resource for mimicked domains and motifs in the host–pathogen interactome. In this work, the experimental host–pathogen (HP) and host–host (HH) protein–protein interactions (PPIs) were collated. The domains and motifs of these proteins were annotated using CD Search and ScanProsite, respectively. Host and pathogen proteins with a shared host interactor and similar domain/motif constitute a mimicry pair exhibiting global structural similarity (domain mimicry pair; DMP) or local sequence motif similarity (motif mimicry pair; MMP). Mimicry pairs are likely to be co-expressed and co-localized. 1,97,607 DMPs and 32,67,568 MMPs were identified in 49,265 experimental HP-PPIs and organized in a web-based resource, ImitateDB (http://imitatedb.sblab-nsit.net) that can be easily queried. The results are externally integrated using hyperlinked domain PSSM ID, motif ID, protein ID and PubMed ID. Kinase, UL36, Smc and DEXDc were frequent DMP domains whereas protein kinase C phosphorylation, casein kinase 2 phosphorylation, glycosylation and myristoylation sites were frequent MMP motifs. Novel DMP domains SANT, Tudor, PhoX and MMP motif microbody C-terminal targeting signal, cornichon signature and lipocalin signature were proposed. ImitateDB is a novel resource for identifying mimicry in interacting host and pathogen proteins. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s00726-022-03163-3. |
format | Online Article Text |
id | pubmed-9054641 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Springer Vienna |
record_format | MEDLINE/PubMed |
spelling | pubmed-90546412022-05-02 ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions Tayal, Sonali Bhatia, Venugopal Mehrotra, Tanya Bhatnagar, Sonika Amino Acids Original Article Molecular mimicry of host proteins by pathogens constitutes a strategy to hijack the host pathways. At present, there is no dedicated resource for mimicked domains and motifs in the host–pathogen interactome. In this work, the experimental host–pathogen (HP) and host–host (HH) protein–protein interactions (PPIs) were collated. The domains and motifs of these proteins were annotated using CD Search and ScanProsite, respectively. Host and pathogen proteins with a shared host interactor and similar domain/motif constitute a mimicry pair exhibiting global structural similarity (domain mimicry pair; DMP) or local sequence motif similarity (motif mimicry pair; MMP). Mimicry pairs are likely to be co-expressed and co-localized. 1,97,607 DMPs and 32,67,568 MMPs were identified in 49,265 experimental HP-PPIs and organized in a web-based resource, ImitateDB (http://imitatedb.sblab-nsit.net) that can be easily queried. The results are externally integrated using hyperlinked domain PSSM ID, motif ID, protein ID and PubMed ID. Kinase, UL36, Smc and DEXDc were frequent DMP domains whereas protein kinase C phosphorylation, casein kinase 2 phosphorylation, glycosylation and myristoylation sites were frequent MMP motifs. Novel DMP domains SANT, Tudor, PhoX and MMP motif microbody C-terminal targeting signal, cornichon signature and lipocalin signature were proposed. ImitateDB is a novel resource for identifying mimicry in interacting host and pathogen proteins. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s00726-022-03163-3. Springer Vienna 2022-04-30 2022 /pmc/articles/PMC9054641/ /pubmed/35487995 http://dx.doi.org/10.1007/s00726-022-03163-3 Text en © The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature 2022 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Original Article Tayal, Sonali Bhatia, Venugopal Mehrotra, Tanya Bhatnagar, Sonika ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions |
title | ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions |
title_full | ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions |
title_fullStr | ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions |
title_full_unstemmed | ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions |
title_short | ImitateDB: A database for domain and motif mimicry incorporating host and pathogen protein interactions |
title_sort | imitatedb: a database for domain and motif mimicry incorporating host and pathogen protein interactions |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9054641/ https://www.ncbi.nlm.nih.gov/pubmed/35487995 http://dx.doi.org/10.1007/s00726-022-03163-3 |
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