ArticlePLoS pathogens2026
N-linked glycosylation of NS1 protein modulates progeny virion assembly in orthoflaviviruses.
Article in PLoS pathogens, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
22 authors.
Funding
Abstract
Tembusu virus (TMUV) is a mosquito-borne avian virus belonging to the genus Orthoflavivirus within the family Flaviviridae. The nonstructural protein 1 (NS1) of TMUV is a secretory protein containing three N-linked glycosylation sites at residues N130, N175, and N207. Using a reverse genetics system and site-directed mutagenesis, we revealed that NS1 deglycosylation impairs the proliferation of recombinant TMUV (rTMUV) in multiple cell types. By performing subcellular fractionation assay, we observed that NS1 deglycosylation significantly impairs viral assembly. Besides, NS1 deglycosylation impairs the thermostability of NS1 dimers but not their formation. Tunicamycin treatment and enzyme-linked immunosorbent assays demonstrated that deglycosylated NS1 significantly induces the endoplasmic reticulum (ER) stress, which in turn reduces the secretion of NS1. Immunofluorescence and coimmunoprecipitation assays further demonstrated that deglycosylated NS1 is largely retained in the ER and enhances its interaction with the E protein. Retention using selective hooks (RUSH)-based live-cell imaging assay revealed that NS1 deglycosylation disrupts the trafficking of E protein from the ER to the Golgi apparatus. In addition, cycloheximide chase analysis showed that NS1 deglycosylation impairs its solubilization and then causes rapid degradation of NS1 and E protein by the host proteasomal pathway. Notably, the efficient viral assembly through NS1 glycosylation is a common feature among flaviviruses (West Nile virus and Yellow Fever virus). Our results consistently demonstrated that the glycosylation modification process of NS1 is highly synchronized with the maturation and assembly of viral particles during their trafficking from the ER to the Golgi apparatus. Collectively, our study confirms that NS1 glycosylation of orthoflavivirus species regulates progeny virion assembly by modulating the NS1-E interaction.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.