ArticleNature communications2019
A Chlamydia pneumoniae adhesin induces phosphatidylserine exposure on host cells.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Mycobacterium marinum MMAR_0267-regulated copper utilization facilitates bacterial escape from phagolysosome.Communications biology · 2024Article
- Direct targeting of host microtubule and actin cytoskeletons by a chlamydial pathogenic effector protein.Journal of cell science · 2024Article
- The Chlamydia pneumoniae effector SemD exploits its host's endocytic machinery by structural and functional mimicry.Nature communications · 2024Article
- Clinical diagnosis and treatment of seven patients diagnosed pneumonia caused byFrontiers in medicine · 2024Article
- Ambroxol Treatment Suppresses the Proliferation ofMicroorganisms · 2021Article
- Development of membrane-insertable lipid scrambling peptides: A time-resolved small-angle neutron scattering study.Structural dynamics (Melville, N.Y.) · 2021Article
- Host cell death during infection with Chlamydia: a double-edged sword.FEMS microbiology reviews · 2021Review
- Insights Into aFrontiers in cellular and infection microbiology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In mammalian cells, the internal and external leaflets of the plasma membrane (PM) possess different phospholipids. Phosphatidylserine (PS) is normally confined to the inner (cytoplasmic) membrane leaflet. Here we report that the adhesin CPn0473 of the human pathogenic bacterium Chlamydia pneumoniae (Cpn) binds to the PM of human cells and induces PS externalization but unexpectedly not apoptosis. PS externalization is increased in human cells exposed to infectious Cpn cells expressing increased CPn0473 and reduced in exposure to Cpn expressing decreased CPn0473. CPn0473 binds specifically to synthetic membranes carrying PS and stimulates pore formation. Asymmetric giant unilamellar vesicles (GUVs) in which PS is restricted to the inner leaflet reveal that CPn0473 induces PS externalization in the absence of other proteins. Thus our identification of CPn0473 as a bacterial PS translocator capable of specific and apoptosis-independent PS externalization during infection extends the spectrum of mechanisms intracellular pathogens use to enter host cells.
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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.