Please use this identifier to cite or link to this item: http://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/8600
Full metadata record
DC FieldValueLanguage
dc.contributor.authorPalande, Aseemen_US
dc.contributor.authorPatil, Saniyaen_US
dc.contributor.authorVeeram, Anjalien_US
dc.contributor.authorSAHOO, SOUMYA SWASTIKen_US
dc.contributor.authorLodhiya, Tejanen_US
dc.contributor.authorMaurya, Pankajen_US
dc.contributor.authorMuralikrishnan, Balajien_US
dc.contributor.authorCHUGH, JEETENDERen_US
dc.contributor.authorMukherjee, Rajuen_US
dc.date.accessioned2024-03-28T11:43:30Z
dc.date.available2024-03-28T11:43:30Z
dc.date.issued2024-03en_US
dc.identifier.citationACS Infectious Diseases, 10(03), 890–906.en_US
dc.identifier.issn2373-8227en_US
dc.identifier.urihttps://doi.org/10.1021/acsinfecdis.3c00517en_US
dc.identifier.urihttp://dr.iiserpune.ac.in:8080/xmlui/handle/123456789/8600
dc.description.abstractIncreased resistance to current antimycobacterial agents and a potential bias toward relatively hydrophobic chemical entities highlight an urgent need to understand how current anti-TB drugs enter the tubercle bacilli. While inner membrane proteins are well-studied, how small molecules cross the impenetrable outer membrane remains unknown. Here, we employed mass spectrometry-based proteomics to show that octyl-β-d-glucopyranoside selectively extracts the outer membrane proteins of Mycobacterium tuberculosis. Differentially expressed proteins between nutrient-replete and nutrient-depleted conditions were enriched to identify proteins involved in nutrient uptake. We demonstrate cell surface localization of seven new proteins using immunofluorescence and show that overexpression of the proteins LpqY and ProX leads to hypersensitivity toward streptomycin, while overexpression of SubI, SpmT, and Rv2041 exhibited higher membrane permeability, assessed through an EtBr accumulation assay. Further, proton NMR metabolomics suggests the role of six outer membrane proteins in glycerol uptake. This study identifies several outer membrane proteins that are involved in the permeation of small hydrophilic molecules and are potential targets for enhancing the uptake and efficacy of anti-TB drugs.en_US
dc.language.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.subjectBacteriaen_US
dc.subjectGeneticsen_US
dc.subjectHydrophilicityen_US
dc.subjectMembranesen_US
dc.subjectPeptides and proteinsen_US
dc.subject2024en_US
dc.subject2024-MAR-WEEK3en_US
dc.subjectTOC-MAR-2024en_US
dc.titleProteomic Analysis of the Mycobacterium tuberculosis Outer Membrane for Potential Implications in Uptake of Small Moleculesen_US
dc.typeArticleen_US
dc.contributor.departmentDept. of Chemistryen_US
dc.identifier.sourcetitleACS Infectious Diseasesen_US
dc.publication.originofpublisherForeignen_US
Appears in Collections:JOURNAL ARTICLES

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.