ArticleNature communications2020
Structure and mechanism of the Nap adhesion complex from the human pathogen Mycoplasma genitalium.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Role of P38 lipoprotein in Mycoplasma penetrans adhesion to human urothelial cells.BMC microbiology · 2025Article
- Unraveling the role of distinct cytoskeletal motility structures in Mycoplasma pneumoniae relatives.BMC microbiology · 2025Review
- Systematic analysis of structural disorder in the minimal proteome ofMicrobiology spectrum · 2025Article
- Development of an epitope-based vaccine fromToxicology research · 2025Article
- JMM Profile:Journal of medical microbiology · 2025Review
- Assembly Formation of P65 Protein, Featured by an Intrinsically Disordered Region Involved in Gliding Machinery ofBiomolecules · 2025Article
- Dynamics of the adhesion complex of the human pathogens Mycoplasma pneumoniae and Mycoplasma genitalium.PLoS pathogens · 2025Article
- Cryo-electron tomography reveals the binding and release states of the major adhesion complex from Mycoplasma genitalium.PLoS pathogens · 2023Article
- Maternal Infection and Preterm Birth: From Molecular Basis to Clinical Implications.Children (Basel, Switzerland) · 2023Review
- Review
- Genotyping ofFrontiers in microbiology · 2023Article
- ArtiaX: An electron tomography toolbox for the interactive handling of sub-tomograms in UCSF ChimeraX.Protein science : a publication of the Protein Society · 2022Article
- Pathogenicity and virulence ofVirulence · 2022Review
- How bacteria utilize sialic acid during interactions with the host: snip, snatch, dispatch, match and attach.Microbiology (Reading, England) · 2022Review
- Molecular Tools for TypingFrontiers in microbiology · 2022Review
- Article
- Molecular ruler of the attachment organelle in Mycoplasma pneumoniae.PLoS pathogens · 2021Article
- Force and Stepwise Movements of Gliding Motility in Human Pathogenic BacteriumFrontiers in microbiology · 2021Article
- Alternative conformation of the C-domain of the P140 protein from Mycoplasma genitalium.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Immunodominant proteins P1 and P40/P90 from human pathogen Mycoplasma pneumoniae.Nature communications · 2020Article
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma genitalium is a human pathogen adhering to host target epithelial cells and causing urethritis, cervicitis and pelvic inflammatory disease. Essential for infectivity is a transmembrane adhesion complex called Nap comprising proteins P110 and P140. Here we report the crystal structure of P140 both alone and in complex with the N-terminal domain of P110. By cryo-electron microscopy (cryo-EM) and tomography (cryo-ET) we find closed and open Nap conformations, determined at 9.8 and 15 Å, respectively. Both crystal structures and the cryo-EM structure are found in a closed conformation, where the sialic acid binding site in P110 is occluded. By contrast, the cryo-ET structure shows an open conformation, where the binding site is accessible. Structural information, in combination with functional studies, suggests a mechanism for attachment and release of M. genitalium to and from the host cell receptor, in which Nap conformations alternate to sustain motility and guarantee infectivity.
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