ArticleCommunications biology2021
Streamlined copper defenses make Bordetella pertussis reliant on custom-made operon.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- A new family of TonB-dependent copper transporters linked to respiratory oxidase function.The Journal of biological chemistry · 2026Article
- CrpH ofFrontiers in microbiology · 2026Article
- Multinuclear non-haem iron-dependent oxidative enzymes: landscape of their substrates, partner proteins and biosynthetic gene clusters.Microbial genomics · 2025Article
- Copper management strategies in obligate bacterial symbionts: balancing cost and benefit.Emerging topics in life sciences · 2024Article
- Moving metals: How microbes deliver metal cofactors to metalloproteins.Molecular microbiology · 2023Article
- Copper Efflux System Required in Murine Lung Infection by Haemophilus influenzae Composed of a Canonical ATPase Gene and Tandem Chaperone Gene Copies.Infection and immunity · 2023Article
- Article
- Conquering the host:Frontiers in microbiology · 2022Review
- Pathogenicity and virulence ofVirulence · 2021Review
Corrections and comments
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Authors and funding
12 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Copper is both essential and toxic to living beings, which tightly controls its intracellular concentration. At the host-pathogen interface, copper is used by phagocytic cells to kill invading microorganisms. We investigated copper homeostasis in Bordetella pertussis, which lives in the human respiratory mucosa and has no environmental reservoir. B. pertussis has considerably streamlined copper homeostasis mechanisms relative to other Gram-negative bacteria. Its single remaining defense line consists of a metallochaperone diverted for copper passivation, CopZ, and two peroxide detoxification enzymes, PrxGrx and GorB, which together fight stresses encountered in phagocytic cells. Those proteins are encoded by an original, composite operon assembled in an environmental ancestor, which is under sensitive control by copper. This system appears to contribute to persistent infection in the nasal cavity of B. pertussis-infected mice. Combining responses to co-occurring stresses in a tailored operon reveals a strategy adopted by a host-restricted pathogen to optimize survival at minimal energy expenditure.
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Registered trials
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