Evidence map›Paper›PMID 30367053›Full record

ArticleNature communications2018

Mycoplasma genitalium adhesin P110 binds sialic-acid human receptors.

David Aparicio, Sergi Torres-Puig, Mercè Ratera, Enrique Querol, Jaume Piñol, Oscar Q Pich, Ignacio Fita

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Genotyping ofFrontiers in microbiology · 2023
    Article
  11. Frontiers in microbiology · 2023
    Review
  12. Review
  13. Virulence · 2022
    Article
  14. Article
  15. Review
  16. Review
  17. Pathogens (Basel, Switzerland) · 2021
    Article
  18. Review
  19. Article
  20. Alternative conformation of the C-domain of the P140 protein from Mycoplasma genitalium.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

David AparicioInstituto de Biología Molecular de Barcelona (IBMB-CSIC) and Maria de Maeztu Unit of Excellence, Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain.
Sergi Torres-PuigInstitut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.ORCID http://orcid.org/0000-0002-8976-6488
Mercè RateraInstituto de Biología Molecular de Barcelona (IBMB-CSIC) and Maria de Maeztu Unit of Excellence, Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain.ORCID http://orcid.org/0000-0001-5224-9172
Enrique QuerolInstitut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
Jaume PiñolInstitut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain.
Oscar Q PichInstitut de Biotecnologia i Biomedicina and Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193, Bellaterra, Barcelona, Spain. oscar.quijada@uab.cat.ORCID http://orcid.org/0000-0003-3561-630X
Ignacio FitaInstituto de Biología Molecular de Barcelona (IBMB-CSIC) and Maria de Maeztu Unit of Excellence, Parc Científic de Barcelona, Baldiri Reixac 10, 08028, Barcelona, Spain. ifrcri@ibmb.csic.es.
Universitat Autònoma de Barcelona · ESInstitut de Biologia Molecular de Barcelona · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adhesion of pathogenic bacteria to target cells is a prerequisite for colonization and further infection. The main adhesins of the emerging sexually transmitted pathogen Mycoplasma genitalium, P140 and P110, interact to form a Nap complex anchored to the cell membrane. Herein, we present the crystal structures of the extracellular region of the virulence factor P110 (916 residues) unliganded and in complex with sialic acid oligosaccharides. P110 interacts only with the neuraminic acid moiety of the oligosaccharides and experiments with human cells demonstrate that these interactions are essential for mycoplasma cytadherence. Additionally, structural information provides a deep insight of the P110 antigenic regions undergoing programmed variation to evade the host immune response. These results enlighten the interplay of M. genitalium with human target cells, offering new strategies to control mycoplasma infections.

Indexed as

Adhesins, BacterialBinding SitesCell MembraneErythrocytesHemadsorptionHumansModels, MolecularMutationMycoplasma genitaliumMycoplasma InfectionsPotassiumProtein BindingProtein ConformationReceptors, Cell SurfaceVirulence Factorsadhesin, Mycoplasma genitaliumAdhesins, BacterialPotassiumReceptors, Cell Surfacesialic acid receptorVirulence Factors

Identifiers

PMID30367053
PMCPMC6203739
OpenAlexW2896002418

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.