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Mycobacterial surface-associated ESX-1 virulence factors play a role in mycobacterial adherence and invasion into lung epithelial cells

https://doi.org/10.1101/2020.10.13.337667

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/1873-3468.12072openalex-snapshot

Characterization of differential pore‐forming activities of ESAT‐6 proteins from Mycobacterium tuberculosis and Mycobacterium smegmatis

inferredcites →https://doi.org/10.1016/j.chembiol.2015.06.020openalex-snapshot

Genetically Encoded Spy Peptide Fusion System to Detect Plasma Membrane-Localized Proteins In Vivo

inferredcites →https://doi.org/10.1016/j.mib.2008.11.003openalex-snapshot

ESX/type VII secretion systems and their role in host–pathogen interaction

inferredcites →https://doi.org/10.1016/j.micinf.2005.12.023openalex-snapshot

A role for dendritic cells in the dissemination of mycobacterial infection

inferredcites →https://doi.org/10.1021/pr500484wopenalex-snapshot

Correlation of Phenotypic Profiles Using Targeted Proteomics Identifies Mycobacterial Esx-1 Substrates

inferredcites →https://doi.org/10.1038/cddis.2014.394openalex-snapshot

Mycobacterium tuberculosis ESAT-6 is a leukocidin causing Ca2+ influx, necrosis and neutrophil extracellular trap formation

inferredcites →https://doi.org/10.1038/ni0315-326bopenalex-snapshot

Erratum: Corrigendum: Direct extracellular interaction between the early secreted antigen ESAT-6 of Mycobacterium tuberculosis and TLR2 inhibits TLR signaling in macrophages

inferredcites →https://doi.org/10.1038/ni1468openalex-snapshot

Direct extracellular interaction between the early secreted antigen ESAT-6 of Mycobacterium tuberculosis and TLR2 inhibits TLR signaling in macrophages

inferredcites →https://doi.org/10.1038/nmeth.2089openalex-snapshot

NIH Image to ImageJ: 25 years of image analysis

inferredcites →https://doi.org/10.1038/nprot.2013.068openalex-snapshot

Evaluation of the pathogenesis and treatment of Mycobacterium marinum infection in zebrafish

inferredcites →https://doi.org/10.1038/sj.emboj.7600732openalex-snapshot

Structure and function of the complex formed by the tuberculosis virulence factors CFP‐10 and ESAT‐6

inferredcites →https://doi.org/10.1038/srep32618openalex-snapshot

EsxA membrane-permeabilizing activity plays a key role in mycobacterial cytosolic translocation and virulence: effects of single-residue mutations at glutamine 5

inferredcites →https://doi.org/10.1046/j.1365-2958.2002.03237.xopenalex-snapshot

Loss of RD1 contributed to the attenuation of the live tuberculosis vaccines Mycobacterium bovis BCG and Mycobacterium microti

inferredcites →https://doi.org/10.1046/j.1365-2958.2003.03844.xopenalex-snapshot

Individual RD1‐region genes are required for export of ESAT‐6/CFP‐10 and for virulence of Mycobacterium tuberculosis

inferredcites →https://doi.org/10.1073/pnas.0504922102openalex-snapshot

Mutually dependent secretion of proteins required for mycobacterial virulence

inferredcites →https://doi.org/10.1073/pnas.0800701105openalex-snapshot

Phenylalanine-427 of anthrax protective antigen functions in both pore formation and protein translocation

inferredcites →https://doi.org/10.1073/pnas.1115485109openalex-snapshot

Peptide tag forming a rapid covalent bond to a protein, through engineering a bacterial adhesin

inferredcites →https://doi.org/10.1073/pnas.1620133114openalex-snapshot

Mycobacterial ESX-1 secretion system mediates host cell lysis through bacterium contact-dependent gross membrane disruptions

inferredcites →https://doi.org/10.1073/pnas.1635213100openalex-snapshot

The primary mechanism of attenuation of bacillus Calmette–Guérin is a loss of secreted lytic function required for invasion of lung interstitial tissue

inferredcites →https://doi.org/10.1073/pnas.1911646117openalex-snapshot

The Mycobacterium marinum ESX-1 system mediates phagosomal permeabilization and type I interferon production via separable mechanisms

inferredcites →https://doi.org/10.1073/pnas.2235593100openalex-snapshot

Acute infection and macrophage subversion by Mycobacterium tuberculosis require a specialized secretion system

inferredcites →https://doi.org/10.1074/jbc.m111.234062openalex-snapshot

The Mycobacterium tuberculosis Early Secreted Antigenic Target of 6 kDa Inhibits T Cell Interferon-γ Production through the p38 Mitogen-activated Protein Kinase Pathway

inferredcites →https://doi.org/10.1074/jbc.m112.420869openalex-snapshot

Mycobacterium tuberculosis ESAT-6 Exhibits a Unique Membrane-interacting Activity That Is Not Found in Its Ortholog from Non-pathogenic Mycobacterium smegmatis

inferredcites →https://doi.org/10.1074/jbc.m114.622076openalex-snapshot

Characterization of Mycobacterium tuberculosis EsxA Membrane Insertion

inferredcites →https://doi.org/10.1074/jbc.m201625200openalex-snapshot

Conclusive Evidence That the Major T-cell Antigens of theMycobacterium tuberculosis Complex ESAT-6 and CFP-10 Form a Tight, 1:1 Complex and Characterization of the Structural Properties of ESAT-6, CFP-10, and the ESAT-6·CFP-10 Complex

inferredcites →https://doi.org/10.1074/jbc.m609869200openalex-snapshot

Insertion of Anthrax Protective Antigen into Liposomal Membranes

inferredcites →https://doi.org/10.1074/jbc.m800123200openalex-snapshot

Molecular Features Governing the Stability and Specificity of Functional Complex Formation by Mycobacterium tuberculosis CFP-10/ESAT-6 Family Proteins

inferredcites →https://doi.org/10.1074/jbc.ra119.012497openalex-snapshot

Nα-Acetylation of the virulence factor EsxA is required for mycobacterial cytosolic translocation and virulence

inferredcites →https://doi.org/10.1080/21505594.2020.1867438openalex-snapshot

Post-translational knockdown and post-secretional modification of EsxA determine contribution of EsxA membrane permeabilizing activity for mycobacterial intracellular survival

inferredcites →https://doi.org/10.1099/00221287-144-11-3195openalex-snapshot

A Mycobacterium tuberculosis operon encoding ESAT=6 and a novel low-molecular-mass culture filtrate protein (CFP-10)

inferredcites →https://doi.org/10.1111/febs.13408openalex-snapshot

Two distinct conformational states of Mycobacterium tuberculosis virulent factor early secreted antigenic target 6 kD a are behind the discrepancy around its biological functions

inferredcites →https://doi.org/10.1111/j.1365-2958.2004.04261.xopenalex-snapshot

A mycobacterial virulence gene cluster extending RD1 is required for cytolysis, bacterial spreading and ESAT‐6 secretion

inferredcites →https://doi.org/10.1111/j.1365-2958.2009.06959.xopenalex-snapshot

Potential role for ESAT6 in dissemination ofM. tuberculosisvia human lung epithelial cells

inferredcites →https://doi.org/10.1111/j.1462-5822.2006.00721.xopenalex-snapshot

The ESAT-6/CFP-10 secretion system of Mycobacterium marinum modulates phagosome maturation

inferredcites →https://doi.org/10.1111/j.1462-5822.2007.00892.xopenalex-snapshot

The ESAT6 protein of Mycobacterium tuberculosis induces apoptosis of macrophages by activating caspase expression

inferredcites →https://doi.org/10.1111/j.1462-5822.2012.01799.xopenalex-snapshot

ESX‐1‐mediated translocation to the cytosol controls virulence of mycobacteria

inferredcites →https://doi.org/10.1111/j.1742-4658.2006.05166.xopenalex-snapshot

Mycobacterium tuberculosis H37Rv ESAT‐6–CFP‐10 complex formation confers thermodynamic and biochemical stability

inferredcites →https://doi.org/10.1126/science.1090124openalex-snapshot

Bacterial Invasion: The Paradigms of Enteroinvasive Pathogens

inferredcites →https://doi.org/10.1128/iai.00614-08openalex-snapshot

Evidence for Pore Formation in Host Cell Membranes by ESX-1-Secreted ESAT-6 and Its Role in Mycobacterium marinum Escape from the Vacuole

inferredcites →https://doi.org/10.1128/iai.00803-18openalex-snapshot

Retention of EsxA in the Capsule-Like Layer of Mycobacterium tuberculosis Is Associated with Cytotoxicity and Is Counteracted by Lung Surfactant

inferredcites →https://doi.org/10.1128/iai.63.5.1710-1717.1995openalex-snapshot

Purification and characterization of a low-molecular-mass T-cell antigen secreted by Mycobacterium tuberculosis

inferredcites →https://doi.org/10.1128/iai.64.1.16-22.1996openalex-snapshot

Evidence for occurrence of the ESAT-6 protein in Mycobacterium tuberculosis and virulent Mycobacterium bovis and for its absence in Mycobacterium bovis BCG

inferredcites →https://doi.org/10.1128/iai.67.2.653-658.1999openalex-snapshot

An In Vitro Tissue Culture Bilayer Model To Examine Early Events inMycobacterium tuberculosisInfection

inferredcites →https://doi.org/10.1128/jb.00469-07openalex-snapshot

ESAT-6 from Mycobacterium tuberculosis Dissociates from Its Putative Chaperone CFP-10 under Acidic Conditions and Exhibits Membrane-Lysing Activity

inferredcites →https://doi.org/10.1128/jb.00967-13openalex-snapshot

Phenotypic Profiling of Mycobacterium tuberculosis EspA Point Mutants Reveals that Blockage of ESAT-6 and CFP-10 Secretion In Vitro Does Not Always Correlate with Attenuation of Virulence

inferredcites →https://doi.org/10.1128/jb.01502-14openalex-snapshot

A Novel ESX-1 Locus Reveals that Surface-Associated ESX-1 Substrates Mediate Virulence in Mycobacterium marinum

inferredcites →https://doi.org/10.1128/jb.178.5.1274-1282.1996openalex-snapshot

Molecular analysis of genetic differences between Mycobacterium bovis BCG and virulent M. bovis

inferredcites →https://doi.org/10.1371/journal.pone.0130832openalex-snapshot

The Disulfide Bond Cys255-Cys279 in the Immunoglobulin-Like Domain of Anthrax Toxin Receptor 2 Is Required for Membrane Insertion of Anthrax Protective Antigen Pore

inferredcites →https://doi.org/10.1371/journal.ppat.0040033openalex-snapshot

Control of M. tuberculosis ESAT-6 Secretion and Specific T Cell Recognition by PhoP

inferredcites →https://doi.org/10.1371/journal.ppat.1000794openalex-snapshot

Direct Visualization by Cryo-EM of the Mycobacterial Capsular Layer: A Labile Structure Containing ESX-1-Secreted Proteins

inferredcites →https://doi.org/10.1371/journal.ppat.1002378openalex-snapshot

Early Secreted Antigen ESAT-6 of Mycobacterium tuberculosis Promotes Protective T Helper 17 Cell Responses in a Toll-Like Receptor-2-dependent Manner

inferredcites →https://doi.org/10.1371/journal.ppat.1004446openalex-snapshot

The ESAT-6 Protein of Mycobacterium tuberculosis Interacts with Beta-2-Microglobulin (β2M) Affecting Antigen Presentation Function of Macrophage

inferredcites →https://doi.org/10.4049/jimmunol.154.7.3359openalex-snapshot

Recall of long-lived immunity to Mycobacterium tuberculosis infection in mice.

inferredcites →https://doi.org/10.4049/jimmunol.178.5.3143openalex-snapshot

The Type I IFN Response to Infection with Mycobacterium tuberculosis Requires ESX-1-Mediated Secretion and Contributes to Pathogenesis

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1073/pnas.2122161119openalex-snapshot

The C terminus of the mycobacterium ESX-1 secretion system substrate ESAT-6 is required for phagosomal membrane damage and virulence

inferred← citeshttps://doi.org/10.3390/cells10071645openalex-snapshot

A Small Protein but with Diverse Roles: A Review of EsxA in Mycobacterium–Host Interaction

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