Evidence map›Paper›PMID 27156860›Full record

ArticleScientific reports2016

N-hypermannose glycosylation disruption enhances recombinant protein production by regulating secretory pathway and cell wall integrity in Saccharomyces cerevisiae.

Hongting Tang, Shenghuan Wang, Jiajing Wang, Meihui Song, Mengyang Xu, Mengying Zhang, Yu Shen, Jin Hou, Xiaoming Bao

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

40 citing papers in PubMed, 83 citations in OpenAlex.

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  13. EngineeringEngineering microbiology · 2024
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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

9 authors at 2 institutions in 1 country.

Hongting TangState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Shenghuan WangState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Jiajing WangState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Meihui SongState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Mengyang XuState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Mengying ZhangState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Yu ShenState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Jin HouState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Xiaoming BaoState Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, China.
Shandong University · CNState Key Laboratory of Microbial Technology

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Saccharomyces cerevisiae is a robust host for heterologous protein expression. The efficient expression of cellulases in S. cerevisiae is important for the consolidated bioprocess that directly converts lignocellulose into valuable products. However, heterologous proteins are often N-hyperglycosylated in S. cerevisiae, which may affect protein activity. In this study, the expression of three heterologous proteins, β-glucosidase, endoglucanase and cellobiohydrolase, was found to be N-hyperglycosylated in S. cerevisiae. To block the formation of hypermannose glycan, these proteins were expressed in strains with deletions in key Golgi mannosyltransferases (Och1p, Mnn9p and Mnn1p), respectively. Their extracellular activities improved markedly in the OCH1 and MNN9 deletion strains. Interestingly, truncation of the N-hypermannose glycan did not increase the specific activity of these proteins, but improved the secretion yield. Further analysis showed OCH1 and MNN9 deletion up-regulated genes in the secretory pathway, such as protein folding and vesicular trafficking, but did not induce the unfolded protein response. The cell wall integrity was also affected by OCH1 and MNN9 deletion, which contributed to the release of secretory protein extracellularly. This study demonstrated that mannosyltransferases disruption improved protein secretion through up-regulating secretory pathway and affecting cell wall integrity and provided new insights into glycosylation engineering for protein secretion.

Indexed as

Secretory Pathwaybeta-FructofuranosidaseCell WallExtracellular SpaceGene DeletionGlycosylationMannosyltransferasesMolecular WeightPorosityRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription, GeneticUnfolded Protein Responsebeta-FructofuranosidaseMannosyltransferasesRecombinant ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID27156860
PMCPMC4860636
OpenAlexW2345464968

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Registered trials

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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.