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A Slam-dependent hemophore contributes to heme acquisition in the bacterial pathogen Acinetobacter baumannii

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Listed:
  • Thomas J. Bateman

    (University of Toronto)

  • Megha Shah

    (University of Toronto)

  • Timothy Pham Ho

    (University of Toronto)

  • Hyejin Esther Shin

    (University of Toronto)

  • Chuxi Pan

    (University of Toronto)

  • Greg Harris

    (National Research Council Canada, Human Health Therapeutics (HHT) Research Center)

  • Jamie E. Fegan

    (University of Toronto)

  • Epshita A. Islam

    (University of Toronto)

  • Sang Kyun Ahn

    (University of Toronto)

  • Yogesh Hooda

    (University of Toronto)

  • Scott D. Gray-Owen

    (University of Toronto)

  • Wangxue Chen

    (National Research Council Canada, Human Health Therapeutics (HHT) Research Center)

  • Trevor F. Moraes

    (University of Toronto)

Abstract

Nutrient acquisition systems are often crucial for pathogen growth and survival during infection, and represent attractive therapeutic targets. Here, we study the protein machinery required for heme uptake in the opportunistic pathogen Acinetobacter baumannii. We show that the hemO locus, which includes a gene encoding the heme-degrading enzyme, is required for high-affinity heme acquisition from hemoglobin and serum albumin. The hemO locus includes a gene coding for a heme scavenger (HphA), which is secreted by a Slam protein. Furthermore, heme uptake is dependent on a TonB-dependent receptor (HphR), which is important for survival and/or dissemination into the vasculature in a mouse model of pulmonary infection. Our results indicate that A. baumannii uses a two-component receptor system for the acquisition of heme from host heme reservoirs.

Suggested Citation

  • Thomas J. Bateman & Megha Shah & Timothy Pham Ho & Hyejin Esther Shin & Chuxi Pan & Greg Harris & Jamie E. Fegan & Epshita A. Islam & Sang Kyun Ahn & Yogesh Hooda & Scott D. Gray-Owen & Wangxue Chen &, 2021. "A Slam-dependent hemophore contributes to heme acquisition in the bacterial pathogen Acinetobacter baumannii," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-26545-9
    DOI: 10.1038/s41467-021-26545-9
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    References listed on IDEAS

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    1. Chi T. Wong & Yingqi Xu & Akshari Gupta & James A. Garnett & Steve J. Matthews & Stephen A. Hare, 2015. "Structural analysis of haemoglobin binding by HpuA from the Neisseriaceae family," Nature Communications, Nature, vol. 6(1), pages 1-11, December.
    2. Christian Brix Folsted Andersen & Morten Torvund-Jensen & Marianne Jensby Nielsen & Cristiano Luis Pinto de Oliveira & Hans-Petter Hersleth & Niels Højmark Andersen & Jan Skov Pedersen & Gregers Rom A, 2012. "Structure of the haptoglobin–haemoglobin complex," Nature, Nature, vol. 489(7416), pages 456-459, September.
    3. Jin-Long Gao & Ann H. Kwan & Anthony Yammine & Xiaoyan Zhou & Jill Trewhella & Barbara M. Hugrass & Daniel A. T. Collins & James Horne & Ping Ye & Derek Harty & Ky-Anh Nguyen & David A. Gell & Neil Hu, 2018. "Structural properties of a haemophore facilitate targeted elimination of the pathogen Porphyromonas gingivalis," Nature Communications, Nature, vol. 9(1), pages 1-13, December.
    4. Kristian Stødkilde & Morten Torvund-Jensen & Søren K. Moestrup & Christian B. F. Andersen, 2014. "Structural basis for trypanosomal haem acquisition and susceptibility to the host innate immune system," Nature Communications, Nature, vol. 5(1), pages 1-8, December.
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