Evidence map›Paper›PMID 36564474›Full record

ArticleScientific reports2022

Proline-rich protein from S. mutans can perform a competitive mineralization function to enhance bacterial adhesion to teeth.

Kun Tian, Chengwei Xiao, Yue Chen, Min Zhou, Jun Guo, Xiaohua Ren, Qin Du

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Differential susceptibility of Streptococcus dentisani to dental surfaces: An atomic force microscopy study.International microbiology : the official journal of the Spanish Society for Microbiology · 2025
    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.

Kun Tian *Department of Stomatology, Sichuan Provincial People's Hospital, University of Electronic Science and Technology of China, No. 32#, Section 2, the First Ring Road West, Chengdu, 610072, Sichuan, China.
Chengwei Xiao *Department of Osteology, Sichuan Provincial People's Hospital, University of Electronic Science and Technology of China, Chengdu, 610072, Sichuan, China.
Yue ChenSchool of Stomatology, Southwest Medical University, Luzhou, 646000, China.
Min ZhouDepartment of Stomatology, Sichuan Provincial People's Hospital, University of Electronic Science and Technology of China, No. 32#, Section 2, the First Ring Road West, Chengdu, 610072, Sichuan, China.
Jun GuoDepartment of Stomatology, Sichuan Provincial People's Hospital, University of Electronic Science and Technology of China, No. 32#, Section 2, the First Ring Road West, Chengdu, 610072, Sichuan, China.
Xiaohua RenDepartment of Stomatology, Sichuan Provincial People's Hospital, University of Electronic Science and Technology of China, No. 32#, Section 2, the First Ring Road West, Chengdu, 610072, Sichuan, China.
Qin DuDepartment of Stomatology, Sichuan Provincial People's Hospital, University of Electronic Science and Technology of China, No. 32#, Section 2, the First Ring Road West, Chengdu, 610072, Sichuan, China. dududicn@163.com.
University of Electronic Science and Technology of China · CNSouthwest Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A proline-rich region was found in Streptococcus mutans (S. mutans) surface antigen I/II (Ag I/II). The functions of this region were explored to determine its role in the cariogenic abilities of S. mutans; specifically, the proline-rich region was compared with human amelogenin. The full-length amelogenin genes were cloned from human (AmH) and surface antigen I/II genes from S. mutans. Then, the genes expressed and purified. We analyzed the structure and self-assembly ability of AmH and Ag I/II, compared their capacities to induce mineralization, and assessed the adhesion ability of S. mutans to AmH- and Ag I/II-coated tooth slices. AmH formed ordered chains and net frames in the early stage of protein self-assembly, while Ag I/II formed irregular and overlapping structures. AmH induced mineralization possessed a parallel rosary structure, while Ag I/II-induced mineralization is rougher and more irregular. The S. mutans adhesion assay indicated that the adhesion ability S. mutans on the Ag I/II-induced crystal layer was significantly higher than that on the AmH-induced crystal layer. S. mutans' Ag I/II may have evolved to resemble human amelogenin and form a rougher crystal layer on teeth, which play a competitive mineralization role and promotes better bacterial adhesion and colonization. Thus, the cariogenic ability of S. mutans Ag I/II is increased.

Indexed as

Bacterial AdhesionStreptococcus mutansAmelogeninAntibodiesAntigens, SurfaceHumansProlineAmelogeninAntibodiesAntigens, SurfaceProline

Identifiers

PMID36564474
PMCPMC9789152
OpenAlexW4312180716

What OpenQuestion holds

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LicenceCC BY
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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.