Evidence map›Paper›PMID 25332379›Full record

ArticleMicrobiology (Reading, England)2015

Functional regions of Candida albicans hyphal cell wall protein Als3 that determine interaction with the oral bacterium Streptococcus gordonii.

Caroline V Bamford, Angela H Nobbs, Michele E Barbour, Richard J Lamont, Howard F Jenkinson

Open access · greenAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing 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

41 citing papers in PubMed, 60 citations in OpenAlex.

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  10. Host's Immunity andMicroorganisms · 2022
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  12. Interactions betweenFrontiers in microbiology · 2022
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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

5 authors at 3 institutions in 2 countries.

Caroline V BamfordSchool of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, UK.
Angela H NobbsSchool of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, UK.
Michele E BarbourSchool of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, UK.
Richard J LamontSchool of Dentistry, University of Louisville, Louisville, Kentucky, USA.
Howard F JenkinsonSchool of Oral and Dental Sciences, University of Bristol, Lower Maudlin Street, Bristol BS1 2LY, UK.
University of Bristol · GBUniversity Of Bristol Dental Hospital · GBUniversity of Louisville · US

Funding

Streptococcus-Candida Communication in Oral BiofilmsR01DE016690 · NIDCR · UNIVERSITY OF BRISTOL · PI JENKINSON, HOWARD F, LAMONT, RICHARD J · 2006 to 2016
$3.8M
NIDCR NIH HHS R01 DE016690NIDCR NIH HHS R01DE016690
6 · The paper itself

Abstract

The opportunistic pathogen Candida albicans colonizes the oral cavity and gastrointestinal tract. Adherence to host cells, extracellular matrix and salivary glycoproteins that coat oral surfaces, including prostheses, is an important prerequisite for colonization. In addition, interactions of C. albicans with commensal oral streptococci are suggested to promote retention and persistence of fungal cells in mixed-species communities. The hyphal filament specific cell wall protein Als3, a member of the Als protein family, is a major determinant in C. albicans adherence. Here, we utilized site-specific in-frame deletions within Als3 expressed on the surface of heterologous Saccharomyces cerevisiae to determine regions involved in interactions of Als3 with Streptococcus gordonii. N-terminal region amino acid residue deletions Δ166-225, Δ218-285, Δ270-305 and Δ277-286 were each effective in inhibiting binding of Strep. gordonii to Als3. In addition, these deletions differentially affected biofilm formation, hydrophobicity, and adherence to silicone and human tissue proteins. Deletion of the central repeat domain (Δ434-830) did not significantly affect interaction of Als3 with Strep. gordonii SspB protein, but affected other adherence properties and biofilm formation. Deletion of the amyloid-forming region (Δ325-331) did not affect interaction of Als3 with Strep. gordonii SspB adhesin, suggesting this interaction was amyloid-independent. These findings highlighted the essential function of the N-terminal domain of Als3 in mediating the interaction of C. albicans with S. gordonii, and suggested that amyloid formation is not essential for the inter-kingdom interaction.

Indexed as

Adhesins, BacterialBiofilmsCandida albicansCell MembraneCell WallExtracellular Matrix ProteinsFungal ProteinsGene DeletionGene ExpressionHumansMouthProtein BindingSaccharomyces cerevisiaeStreptococcus gordoniiAdhesins, BacterialALS3 protein, Candida albicansExtracellular Matrix ProteinsFungal Proteinssalivary agglutinin receptor, Streptocococcus

Identifiers

PMID25332379
PMCPMC4274786
OpenAlexW2127207315

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.