Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Title A name given to the resource Faculty Publications Article Faculty Publications -Articles Dublin Core The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/. Creator An entity primarily responsible for making the resource Menon, Arjun M.; Gopichand, Boinapalli; Thomas, Shwetha Susan; Abhinand, Kuniyil; Nair, Bipin G.; Kumar, Geetha B.; Babu, Pradeesh; Arun, K.B.; Edison, Lekshmi K.; Madhavan, Aravind Title A name given to the resource Rv1899c, an HDAC1ZBTB25-Interacting Protein of Mycobacterium tuberculosis, Promotes Stress Resistance and Immune Evasion in Infected Macrophages Date A point or period of time associated with an event in the lifecycle of the resource 01-01-2025 Source A related resource from which the described resource is derived International Journal of Molecular Sciences;Volume;26;Issue;22;Article No.;10872; Identifier An unambiguous reference to the resource within a given context <a href="https://doi.org/10.3390/ijms262210872" target="_blank" rel="noreferrer noopener">https://doi.org/10.3390/ijms262210872</a> <br /><br /><a href="https://www.scopus.com/pages/publications/105023078876?origin=resultslist" target="_blank" rel="noreferrer noopener">https://www.scopus.com/pages/publications/105023078876?origin=resultslist</a> Coverage The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant Menon A.M., School of Biotechnology, Amrita Vishwa Vidyapeetham, AmritapuriKerala, Kollam, 690525, India; Gopichand B., School of Biotechnology, Amrita Vishwa Vidyapeetham, AmritapuriKerala, Kollam, 690525, India; Thomas S.S., School of Biotechnology, Amrita Vishwa Vidyapeetham, AmritapuriKerala, Kollam, 690525, India; Abhinand K., School of Biotechnology, Amrita Vishwa Vidyapeetham, AmritapuriKerala, Kollam, 690525, India; Nair B.G., School of Biotechnology, Amrita Vishwa Vidyapeetham, AmritapuriKerala, Kollam, 690525, India; Kumar G.B., School of Biotechnology, Amrita Vishwa Vidyapeetham, AmritapuriKerala, Kollam, 690525, India; Babu P., School of Biotechnology, Amrita Vishwa Vidyapeetham, AmritapuriKerala, Kollam, 690525, India; Arun K.B., Department of Life Sciences, CHRIST (Deemed to be University), Karnataka, Bangalore, 560029, India; Edison L.K., Department of Comparative, Diagnostic, and Population Medicine, College of Veterinary Medicine, University of Florida, Gainesville, 32608, FL, United States; Madhavan A., School of Biotechnology, Amrita Vishwa Vidyapeetham, AmritapuriKerala, Kollam, 690525, India Description An account of the resource Rv1899c, a previously identified HDAC1ZBTB25-interacting protein of Mycobacterium tuberculosis, plays a crucial role in bacterial adaptation and immune modulation. Recombinant M. smegmatis-expressing Rv1899c (MS_ Rv1899c) showed enhanced survival under acidic and oxidative stress compared to vector controls, along with improved early intracellular growth in THP1-derived macrophages. This was accompanied by reduced reactive oxygen species (ROS), diminished cytokines associated with inflammation and downregulation of autophagy proteins ATG5, Beclin, and LC3, which ultimately skewed the immune response, suppressing the pro-inflammatory M1 macrophage population. Targeting Rv1899c with 3-aminobenzamide (3-AB) impaired intracellular bacterial survival and restored IL-12B expression, while its combination with the HDAC inhibitor C1994 significantly enhanced bacterial clearance. Structural modelling confirmed the high stereochemical quality of the Rv1899c macrodomain, and computational studies identified 3-AB as the strongest ligand (?5.75 kcal/mol), stabilized through hydrogen bonding and hydrophobic interactions with key residues. Molecular dynamics simulations conducted for 200 ns demonstrated stable proteinligand interactions with consistent parameters, while MM/GBSA analysis indicated favourable binding energy (?G_bind = ?6.6 kcal/mol), largely influenced by van der Waals and electrostatic forces. Together, these findings highlight Rv1899c as a mediator of stress resistance and immune evasion and propose it as a potential therapeutic target against M. tuberculosis. 2025 by the authors. Subject The topic of the resource autophagy; epigenetics; immune evasion; macrophage polarization; tuberculosis Publisher An entity responsible for making the resource available Multidisciplinary Digital Publishing Institute (MDPI) Relation A related resource ISSN: 16616596; Language A language of the resource English Type The nature or genre of the resource Article Rights Information about rights held in and over the resource All Open Access; Gold Open Access Format The file format, physical medium, or dimensions of the resource online