Evidence map›Paper›PMID 31103030›Full record

ArticleMicrobial cell factories2019

Development of novel surface display platforms for anchoring heterologous proteins in Saccharomyces cerevisiae.

Xiaoyu Yang, Hongting Tang, Meihui Song, Yu Shen, Jin Hou, Xiaoming Bao

Abstract read
In one paragraph

Article in Microbial cell factories, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

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  11. Construction of L-type lectin displaying Saccharomyces cerevisiae for Vibrio parahaemolyticus agglutination.International microbiology : the official journal of the Spanish Society for Microbiology · 2025
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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

6 authors.

Xiaoyu YangState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Hongting TangState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Meihui SongState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Yu ShenState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China.
Jin HouState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China. houjin@sdu.edu.cn.
Xiaoming BaoState Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, People's Republic of China. bxm@sdu.edu.cn.

Funding

National Natural Science Foundation of China 31470219National Natural Science Foundation of China 31711530155National Natural Science Foundation of China 31770101Natural Science Foundation of Shandong Province ZR2017ZB0210the Key R and D Program of Shandong Province 2017GSF21110
6 · The paper itself

Abstract

backgroundCell surface display of recombinant proteins has become a powerful tool for biotechnology and biomedical applications. As a model eukaryotic microorganism, Saccharomyces cerevisiae is an ideal candidate for surface display of heterologous proteins. However, the frequently used commercial yeast surface display system, the a-agglutinin anchor system, often results in low display efficiency.

resultsWe initially reconstructed the a-agglutinin system by replacing two anchor proteins with one anchor protein. By directly fusing the target protein to the N-terminus of Aga1p and inserting a flexible linker, the display efficiency almost doubled, and the activity of reporter protein α-galactosidase increased by 39%. We also developed new surface display systems. Six glycosylphosphatidylinositol (GPI) anchored cell wall proteins were selected to construct the display systems. Among them, Dan4p and Sed1p showed higher display efficiency than the a-agglutinin anchor system. Linkers were also inserted to eliminate the effects of GPI fusion on the activity of the target protein. We further used the newly developed Aga1p, Dan4p systems and Sed1p system to display exoglucanase and a relatively large protein β-glucosidase, and found that Aga1p and Dan4p were more suitable for immobilizing large proteins.

conclusionOur study developed novel efficient yeast surface display systems, that will be attractive tools for biotechnological and biomedical applications.

Indexed as

Cell Surface Display TechniquesCell Adhesion MoleculesCell WallGlycosylphosphatidylinositolsMembrane GlycoproteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsa-agglutinin protein, S cerevisiaeAGA1 protein, S cerevisiaeCell Adhesion MoleculesGlycosylphosphatidylinositolsMembrane GlycoproteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSED1 protein, S cerevisiaea-AgglutininAga1Dan4Glycosylphosphatidylinositol (GPI)Sed1Yeast surface display

Identifiers

PMID31103030
PMCPMC6525377

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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.