ArticleOpen biology2013
A vitamin B₁₂ transporter in Mycobacterium tuberculosis.
Article in Open biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 99 citations in OpenAlex.
- The metallophosphoesterase Rv0805 regulates carbon flux and cell envelope homeostasis during growth of mycobacteria in propionate.Journal of bacteriology · 2026Article
- Cobamide metabolism, regulation, and adaptation inJournal of bacteriology · 2025Review
- Genome-wide phenotypic insights into mycobacterial virulence using Drosophila melanogaster.PLoS pathogens · 2025Article
- Family-based genetics identifies association of CUBN, IL1RL1 and PRKN variants with leprosy in Bangladesh.Scientific reports · 2025Article
- Total Synthesis and Structural Reassignment of the Antitubercular Natural Product Evybactin.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- A novel regulatory interplay between atypical B12 riboswitches and uORF translation in Mycobacterium tuberculosis.Nucleic acids research · 2024Article
- Vitamin BMicrobiology spectrum · 2024Article
- Propionate prevents loss of the PDIM virulence lipid in Mycobacterium tuberculosis.Nature microbiology · 2024Article
- Bidirectional ATP-driven transport of cobalamin by the mycobacterial ABC transporter BacA.Nature communications · 2024Article
- Dependency on host vitamin B12 has shaped Mycobacterium tuberculosis Complex evolution.Nature communications · 2024Article
- The PDIM paradox ofbioRxiv : the preprint server for biology · 2023Article
- A Comprehensive Review on the Roles of Metals Mediating Insect-Microbial Pathogen Interactions.Metabolites · 2023Review
- Genomic Insights into Bacterial Resistance to Proline-Rich Antimicrobial Peptide Bac7.Membranes · 2023Article
- Mycobacterial phosphodiesterase Rv0805 is a virulence determinant and its cyclic nucleotide hydrolytic activity is required for propionate detoxification.Molecular microbiology · 2023Article
- Interrogation of the Pathogen Box reveals small molecule ligands against the mycobacterial trehalose transporter LpqY-SugABC.RSC medicinal chemistry · 2022Article
- Critical discussion on drug efflux in Mycobacterium tuberculosis.FEMS microbiology reviews · 2022Review
- Phenotypic adaptation ofFrontiers in cellular and infection microbiology · 2022Review
- ATP-Binding Cassette Transporters: Snap-on Complexes?Sub-cellular biochemistry · 2022Article
- The immunometabolite itaconate inhibits heme synthesis and remodels cellular metabolism in erythroid precursors.Blood advances · 2021Article
- Cobalamin is present in cells of non-tuberculous mycobacteria, but not in Mycobacterium tuberculosis.Scientific reports · 2021Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Vitamin B₁₂-dependent enzymes function in core biochemical pathways in Mycobacterium tuberculosis, an obligate pathogen whose metabolism in vivo is poorly understood. Although M. tuberculosis can access vitamin B₁₂ in vitro, it is uncertain whether the organism is able to scavenge B₁₂ during host infection. This question is crucial to predictions of metabolic function, but its resolution is complicated by the absence in the M. tuberculosis genome of a direct homologue of BtuFCD, the only bacterial B₁₂ transport system described to date. We applied genome-wide transposon mutagenesis to identify M. tuberculosis mutants defective in their ability to use exogenous B₁₂. A small proportion of these mapped to Rv1314c, identifying the putative PduO-type ATP : co(I)rrinoid adenosyltransferase as essential for B₁₂ assimilation. Most notably, however, insertions in Rv1819c dominated the mutant pool, revealing an unexpected function in B₁₂ acquisition for an ATP-binding cassette (ABC)-type protein previously investigated as the mycobacterial BacA homologue. Moreover, targeted deletion of Rv1819c eliminated the ability of M. tuberculosis to transport B₁₂ and related corrinoids in vitro. Our results establish an alternative to the canonical BtuCD-type system for B₁₂ uptake in M. tuberculosis, and elucidate a role in B₁₂ metabolism for an ABC protein implicated in chronic mycobacterial infection.
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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.