Supplemental DataMtb H37Rv short-linear PDZ-binding motif proteins at the host‒pathogen interface

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Supplemental Data File: This spreadsheet file provides a comprehensive dataset and subsequent analysis of the Mtb PDZbm proteome. The data is organized across multiple tabs for clarity and depth. Sheet 1: “List of PDZbm proteins” contains the complete inventory of PDZbm proteins identified in the study, organized by their unique Accession Number. For ease of cross-referencing and functional interpretation, the corresponding Gene ID and standardized Gene Name from the DAVID knowledgebase are provided in adjacent columns. Sheets 2-7: “GOTERMS” present the results of systematic ontology and pathway enrichment analyses performed on the protein list from Sheet 1. These analyses identify the most relevant biological processes, molecular functions and cellular components, from the PDZbm proteome. Sheet 8: “ShinyGO_Reactome_Pathways” results from the ShinyGO analysis against the Reactome database, clustering proteins by their involvement in specific, curated biological pathways. Sheet 9: “Overlapping_GO_Reactome”: A consolidated view highlighting the most relevant and overlapping functional terms from both the GO and Reactome analyses.Supplemental Fig S1. PDZbm interactions between syntenin-1 and the C-terminal pentapeptides of Esx H, N, T and Amutant proteins. Molecular docking models of syntenin-1 domain 1 and 2 with Esx H (A,B), EsxN (C,D), EsxT (E,F) and EsxAmut (G,H) respectively. Top panel: Molecular representations of the hydrogen bond and electrostatic interactions in the complexes Blue ribbons: syntenin-1 domain 1. Gold ribbons: syntenin-1 domain 2. Bottom panel: Hydrogen bonds (dashed lines) and hydrophobic interactions (red semicircles) for the structures resulting from docking.Supplemental Fig S2. PDZbm interactions between syntenin-1 and the C-terminal pentapeptides of Esx B, C, D and U proteins. Molecular docking models of syntenin-1 domain 1 and 2 with EsxB (A,B), EsxC (C,D), EsxD (E,F) and EsxU (G,H) respectively. Top panel: Molecular representations of the hydrogen bond and electrostatic interactions in the complexes Blue ribbons: syntenin-1 domain 1. Gold ribbons: syntenin-1 domain 2. Bottom panel: Hydrogen bonds (dashed lines) and hydrophobic interactions (red semicircles) for the structures resulting from docking.

Ce résumé expose les affirmations des auteurs. BNTIC ne l’interprète pas comme une validation indépendante des résultats.