{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9"],"submitter":["Chaurasia R"],"pubmed_abstract":["Mechanisms of leptospirosis pathogenesis remain unclear despite the identification of a number of potential leptospiral virulence factors. We recently demonstrated potential mechanisms by which the virulence-modifying (VM) proteins-defined as containing a Domain of Unknown function (DUF1561), encoded by the PF07598 gene family-found only in group 1 pathogenic <i>Leptospira</i>-might mediate the clinical pathogenesis of leptospirosis. VM proteins belongs to classical AB toxin paradigm though have a unique AB domain architecture, unlike other AB toxins such as diphtheria toxin, pertussis toxin, shiga toxin, or ricin toxin which are typically encoded by two or more genes and self-assembled into a multi-domain holotoxin. Leptospiral VM proteins are secreted R-type lectin domain-containing exot"],"journal":["Frontiers in molecular biosciences"],"pagination":["1092197"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9900628"],"repository":["biostudies-literature"],"pubmed_title":["<i>In silico</i> prediction of molecular mechanisms of toxicity mediated by the leptospiral PF07598 gene family-encoded virulence-modifying proteins."],"pmcid":["PMC9900628"],"pubmed_authors":["Vinetz JM","Chaurasia R"],"additional_accession":[]},"is_claimable":false,"name":"<i>In silico</i> prediction of molecular mechanisms of toxicity mediated by the leptospiral PF07598 gene family-encoded virulence-modifying proteins.","description":"Mechanisms of leptospirosis pathogenesis remain unclear despite the identification of a number of potential leptospiral virulence factors. We recently demonstrated potential mechanisms by which the virulence-modifying (VM) proteins-defined as containing a Domain of Unknown function (DUF1561), encoded by the PF07598 gene family-found only in group 1 pathogenic <i>Leptospira</i>-might mediate the clinical pathogenesis of leptospirosis. VM proteins belongs to classical AB toxin paradigm though have a unique AB domain architecture, unlike other AB toxins such as diphtheria toxin, pertussis toxin, shiga toxin, or ricin toxin which are typically encoded by two or more genes and self-assembled into a multi-domain holotoxin. Leptospiral VM proteins are secreted R-type lectin domain-containing exot","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2026-04-08T13:31:29.601Z","creation":"2024-11-07T08:50:54.417Z"},"accession":"S-EPMC9900628","cross_references":{"pubmed":["36756251"],"doi":["10.3389/fmolb.2022.1092197"]}}