ArticleMicrobiology (Reading, England)2012
The major facilitator superfamily-type protein LbtC promotes the utilization of the legiobactin siderophore by Legionella pneumophila.
Article in Microbiology (Reading, England), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 39 citations in OpenAlex.
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- Legionella pneumophila Rhizoferrin Promotes Bacterial Biofilm Formation and Growth within Amoebae and Macrophages.Infection and immunity · 2023Article
- Legionella pneumophila Cas2 Promotes the Expression of Small Heat Shock Protein C2 That Is Required for Thermal Tolerance and Optimal Intracellular Infection.Infection and immunity · 2022Article
- Recent Advances in the Siderophore Biology ofFrontiers in microbiology · 2022Review
- A NovelmBio · 2020Article
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- Non-ribosomal peptide synthetases: Identifying the cryptic gene clusters and decoding the natural product.Journal of biosciences · 2017Review
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- Iron Availability Modulates the Persistence of Legionella pneumophila in Complex Biofilms.Microbes and environments · 2016Article
- Iron Limitation Triggers Early Egress by the Intracellular Bacterial Pathogen Legionella pneumophila.Infection and immunity · 2016Article
- Two parallel pathways for ferric and ferrous iron acquisition support growth and virulence of the intracellular pathogen Francisella tularensis Schu S4.MicrobiologyOpen · 2016Article
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- The Legionella pneumophila Siderophore Legiobactin Is a Polycarboxylate That Is Identical in Structure to Rhizoferrin.Infection and immunity · 2015Article
- MavN is a Legionella pneumophila vacuole-associated protein required for efficient iron acquisition during intracellular growth.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- IroT/mavN, a new iron-regulated gene involved in Legionella pneumophila virulence against amoebae and macrophages.Environmental microbiology · 2015Article
- An update on iron acquisition by Legionella pneumophila: new pathways for siderophore uptake and ferric iron reduction.Future microbiology · 2015Review
- The Yersinia pestis siderophore, yersiniabactin, and the ZnuABC system both contribute to zinc acquisition and the development of lethal septicaemic plague in mice.Molecular microbiology · 2014Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
The Gram-negative bacterium Legionella pneumophila elaborates the siderophore legiobactin. We previously showed that cytoplasmic LbtA helps mediate legiobactin synthesis, inner-membrane LbtB promotes export of legiobactin, and outer-membrane LbtU acts as the ferrisiderophore receptor. RT-PCR analyses now identified lbtC as an iron-repressed gene that is the final gene in an operon containing lbtA and lbtB. In silico analysis predicted that LbtC is an inner-membrane protein that belongs to the major facilitator superfamily (MFS). Although capable of normal growth in standard media, lbtC mutants were defective for growth on iron-depleted agar media. While producing normal levels of legiobactin, lbtC mutants were unable to utilize supplied legiobactin to stimulate growth on iron-depleted media and displayed an impaired ability to take up radiolabelled iron. All lbtC mutant phenotypes were complemented by reintroduction of an intact copy of lbtC. When a cloned copy of both lbtC and lbtU was introduced into a heterologous bacterium (Legionella longbeachae), the organism acquired the ability to utilize legiobactin to grow better on low-iron media. Together, these data indicate that LbtC is involved in the uptake of legiobactin, and based upon its predicted location is most likely the mediator of ferrilegiobactin transport across the inner membrane. The data are also a unique documentation of how an MFS protein can promote bacterial iron-siderophore import, standing in contrast to the vast majority of studies which have defined ABC-type permeases as the mediators of siderophore import across the Gram-negative inner membrane or the Gram-positive cytoplasmic membrane.
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