Evidence map›Paper›PMID 25359271›Full record

ArticleJournal of microbiology (Seoul, Korea)2014

The identification of six novel proteins with fibronectin or collagen type I binding activity from Streptococcus suis serotype 2.

Hui Zhang, Junxi Zheng, Li Yi, Yue Li, Zhe Ma, Hongjie Fan, Chengping Lu

Abstract read
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In one paragraph

Article in Journal of microbiology (Seoul, Korea), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

7 citing papers in PubMed, 29 citations in OpenAlex.

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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 1 institution in 1 country.

Hui ZhangCollege of Veterinary Medicine, Nanjing Agricultural University, Nanjing, P. R. China.
Junxi Zheng
Li Yi
Yue Li
Zhe Ma
Hongjie Fan
Chengping Lu
Nanjing Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptococcus suis, a major swine pathogen, is an emerging zoonotic agent that causes meningitis and septic shock. Bacterial cell wall and secreted proteins are often involved in interactions with extracellular matrix proteins (ECMs), which play important roles in the initial steps of pathogenesis. In this study, 2D SDS-PAGE, western blotting-based binding affinity measurements, and microtiter plate binding assays were used to identify cell wall and secreted proteins from S. suis that interact with fibronectin and collagen type I. We identified six proteins from S. suis, including three proteins (translation elongation factor G, oligopeptide-binding protein OppA precursor, and phosphoglycerate mutase) that show both fibronectin and collagen type I binding activity. To the best of our knowledge, these three newly identified proteins had no previously reported fibronectin or collagen type I binding activity. Overall, the aim in this study was to identify proteins with ECM binding activity from S. suis and it represents the first report of six new proteins from S. suis that interact with fibronectin or collagen type I.

Indexed as

Adhesins, BacterialAnimalsBacterial ProteinsCarrier ProteinsCollagen Type IExtracellular Matrix ProteinsFibronectinsLipoproteinsPeptide Elongation Factor GPhosphoglycerate MutaseStreptococcal InfectionsStreptococcus suisSwineAdhesins, BacterialBacterial ProteinsCarrier ProteinsCollagen Type IExtracellular Matrix Proteinsfibronectin-binding proteins, bacterialFibronectinsLipoproteinsoligopeptide-binding protein, bacteriaPeptide Elongation Factor GPhosphoglycerate Mutase

Identifiers

PMID25359271
OpenAlexW1983094284

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.