ArticleMicrobiology (Reading, England)2007
Beta-lactamase can function as a reporter of bacterial protein export during Mycobacterium tuberculosis infection of host cells.
Article in Microbiology (Reading, England), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 30 citations in OpenAlex.
- Proteomics from compartment-specific APEX2 labeling in Mycobacterium tuberculosis reveals Type VII secretion substrates in the cell wall.Cell chemical biology · 2024Article
- Inflammation-Related Immune-Modulatory SLURP1 Prevents the Proliferation of Human Colon Cancer Cells, and Its Delivery byPharmaceutics · 2023Article
- The biogenesis of β-lactamase enzymes.Microbiology (Reading, England) · 2022Review
- Optimized APEX2 peroxidase-mediated proximity labeling in fast- and slow-growing mycobacteria.Methods in enzymology · 2022Article
- Biochemical and phenotypic characterisation of theCell surface (Amsterdam, Netherlands) · 2021Article
- The final assembly of trehalose polyphleates takes place within the outer layer of the mycobacterial cell envelope.The Journal of biological chemistry · 2020Article
- Article
- Ferric Citrate Regulator FecR Is Translocated across the Bacterial Inner Membrane via a Unique Twin-Arginine Transport-Dependent Mechanism.Journal of bacteriology · 2020Article
- Compartment-Specific Labeling of Bacterial Periplasmic Proteins by Peroxidase-Mediated Biotinylation.ACS infectious diseases · 2018Article
- Monitoring Protein Secretion inFrontiers in microbiology · 2018Article
- Evaluating a New High-throughput Twin-Arginine Translocase Assay in Bacteria for Therapeutic Applications.Current microbiology · 2017Article
- Green Fluorescent Protein as a protein localization and topological reporter in mycobacteria.Tuberculosis (Edinburgh, Scotland) · 2017Article
- Article
- Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2.BMC microbiology · 2013Article
- Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Journal of bacteriology · 2013Article
- Article
- A β-Lactamase based reporter system for ESX dependent protein translocation in mycobacteria.PloS one · 2012Article
- Genome-wide identification of Mycobacterium tuberculosis exported proteins with roles in intracellular growth.Journal of bacteriology · 2011Article
- Protein export systems of Mycobacterium tuberculosis: novel targets for drug development?Future microbiology · 2010Review
- Sec- and Tat-dependent translocation of beta-lactamases across the Escherichia coli inner membrane.Antimicrobial agents and chemotherapy · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Mycobacterium tuberculosis is an intracellular pathogen that is able to avoid destruction by host immune defences. Exported proteins of M. tuberculosis, which include proteins localized to the bacterial surface or secreted into the extracellular environment, are ideally situated to interact with host factors. As a result, these proteins are attractive candidates for virulence factors, drug targets and vaccine components. Here we describe a beta-lactamase reporter system capable of identifying exported proteins of M. tuberculosis during growth in host cells. Because beta-lactams target bacterial cell-wall synthesis, beta-lactamases must be exported beyond the cytoplasm to protect against these drugs. When used in protein fusions, beta-lactamase can report on the subcellular location of another protein as measured by protection from beta-lactam antibiotics. Here we demonstrate that a truncated TEM-1 beta-lactamase lacking a signal sequence for export ('BlaTEM-1) can be used in this manner directly in a mutant strain of M. tuberculosis lacking the major beta-lactamase, BlaC. The 'BlaTEM-1 reporter conferred beta-lactam resistance when fused to both Sec and Tat export signal sequences. We further demonstrate that beta-lactamase fusion proteins report on protein export while M. tuberculosis is growing in THP-1 macrophage-like cells. This genetic system should facilitate the study of proteins exclusively exported in the host environment by intracellular M. tuberculosis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.