Microbe induced cardiovascular diseases (CVDs) are less studied at present. Host-pathogen interactions (HPIs) between human proteins and microbial proteins associated with CVD can be found dispersed in existing molecular interaction databases. MorCVD database is a curated resource that combines 23,377 protein interactions between human host and 432 unique pathogens involved in CVDs in a single intuitive web application. It covers endocarditis, myocarditis, pericarditis and 16 other microbe induced CVDs. The HPI information has been compiled, curated, and presented in a freely accessible web interface (http://morcvd.sblab-nsit.net/About). Apart from organization, enrichment of the HPI data was done by adding hyperlinked protein ID, PubMed, gene ontology records. For each protein in the database, drug target and interactors (same as well as different species) information has been provided. The database can be searched by disease, protein ID, pathogen name or interaction detection method. Interactions detected by more than one method can also be listed. The information can be presented in tabular form or downloaded. A comprehensive help file has been developed to explain the various options available. Hence, MorCVD acts as a unified resource for retrieval of HPI data for researchers in CVD and microbiology.

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.

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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.