Evidence map›Paper›PMID 33620037›Full record

ArticleActa crystallographica. Section F, Structural biology communications2021

Structural insights into the intermolecular interaction of the adhesin SdrC in the pathogenicity of Staphylococcus aureus.

Junchao Wang, Min Zhang, Mingzhu Wang, Jianye Zang, Xuan Zhang, Tianrong Hang

Open access · greenAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Inoculation withFrontiers in microbiology · 2023
    Article
  5. Functional Mapping of Phenotypic Plasticity ofFrontiers in microbiology · 2021
    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

6 authors at 3 institutions in 1 country.

Junchao WangSchool of Life Sciences, Anhui University, 111 Jiulong Road, Hefei, Anhui 230601, People's Republic of China.
Min ZhangSchool of Life Sciences, Anhui University, 111 Jiulong Road, Hefei, Anhui 230601, People's Republic of China.
Mingzhu WangInstitute of Health Sciences and Technology, Anhui University, 111 Jiulong Road, Hefei, Anhui 230601, People's Republic of China.
Jianye ZangHefei National Laboratory for Physical Sciences at Microscale, CAS Center for Excellence in Biomacromolecules, Collaborative Innovation Center of Chemistry for Life Sciences and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
Xuan ZhangHefei National Laboratory for Physical Sciences at Microscale, CAS Center for Excellence in Biomacromolecules, Collaborative Innovation Center of Chemistry for Life Sciences and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
Tianrong HangSchool of Life Sciences, Anhui University, 111 Jiulong Road, Hefei, Anhui 230601, People's Republic of China.
Anhui University · CNChinese Academy of Sciences · CNHefei Institutes of Physical Science · CN

Funding

Anhui Department of Education KJ2019ZD02Natural Science Foundation of Anhui Province 2008085QC161
6 · The paper itself

Abstract

Staphylococcus aureus is an opportunistic disease-causing pathogen that is widely found in the community and on medical equipment. A series of virulence factors secreted by S. aureus can trigger severe diseases such as sepsis, endocarditis and toxic shock, and thus have a great impact on human health. The transformation of S. aureus from a colonization state to a pathogenic state during its life cycle is intimately associated with the initiation of bacterial aggregation and biofilm accumulation. SdrC, an S. aureus surface protein, can act as an adhesin to promote cell attachment and aggregation by an unknown mechanism. Here, structural studies demonstrate that SdrC forms a unique dimer through intermolecular interaction. It is proposed that the dimerization of SdrC enhances the efficiency of bacteria-host attachment and therefore contributes to the pathogenicity of S. aureus.

Indexed as

Bacterial ProteinsCrystallography, X-RayProtein DomainsProtein MultimerizationStaphylococcus aureusBacterial ProteinsSdrC protein, Staphylococcus aureusadhesiondimerhomophilic interactionSdrCStaphylococcus aureus

Identifiers

PMID33620037
PMCPMC7900927
OpenAlexW3126899922

What OpenQuestion holds

Textmetadata
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.