ArticleJournal of bacteriology2011
Legionella pneumophila LbtU acts as a novel, TonB-independent receptor for the legiobactin siderophore.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 41 citations in OpenAlex.
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- Distribution characteristics of theInfection and immunity · 2024Article
- 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
- Structure and functional analysis of the Legionella pneumophila chitinase ChiA reveals a novel mechanism of metal-dependent mucin degradation.PLoS pathogens · 2020Article
- Structure, Dynamics and Cellular Insight Into Novel Substrates of theFrontiers in molecular biosciences · 2020Article
- Iron and Virulence inFrontiers in cellular and infection microbiology · 2017Review
- 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
- 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
- Nuclease activity of Legionella pneumophila Cas2 promotes intracellular infection of amoebal host cells.Infection and immunity · 2015Article
- Substrate uptake and subcellular compartmentation of anoxic cholesterol catabolism in Sterolibacterium denitrificans.The Journal of biological chemistry · 2015Article
- An update on iron acquisition by Legionella pneumophila: new pathways for siderophore uptake and ferric iron reduction.Future microbiology · 2015Review
- The novel Legionella pneumophila type II secretion substrate NttC contributes to infection of amoebae Hartmannella vermiformis and Willaertia magna.Microbiology (Reading, England) · 2014Article
- 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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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Gram-negative Legionella pneumophila produces a siderophore (legiobactin) that promotes lung infection. We previously determined that lbtA and lbtB are required for the synthesis and secretion of legiobactin. DNA sequence and reverse transcription-PCR (RT-PCR) analyses now reveal the presence of an iron-repressed gene (lbtU) directly upstream of the lbtAB-containing operon. In silico analysis predicted that LbtU is an outer membrane protein consisting of a 16-stranded transmembrane β-barrel, multiple extracellular domains, and short periplasmic tails. Immunoblot analysis of cell fractions confirmed an outer membrane location for LbtU. Although replicating normally in standard media, lbtU mutants, like lbtA mutants, were impaired for growth on iron-depleted agar media. While producing typical levels of legiobactin, lbtU mutants were unable to use supplied legiobactin to stimulate growth on iron-depleted media and displayed an inability to take up iron. Complemented lbtU mutants behaved as the wild type did. The lbtU mutants were also impaired for infection in a legiobactin-dependent manner. Together, these data indicate that LbtU is involved in the uptake of legiobactin and, based upon its location, is most likely the Legionella siderophore receptor. The sequence and predicted two-dimensional (2D) and 3D structures of LbtU were distinct from those of all known siderophore receptors, which generally contain a 22-stranded β-barrel and an extended N terminus that binds TonB in order to transduce energy from the inner membrane. This observation coupled with the fact that L. pneumophila does not encode TonB suggests that LbtU is a new type of receptor that participates in a form of iron uptake that is mechanistically distinct from the existing paradigm.
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