ArticleVirology2011
Glycosylation modulates arenavirus glycoprotein expression and function.
Article in Virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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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
22 citing papers in PubMed, 37 citations in OpenAlex.
- Infusion of neutralization into Lassa vaccine design.Trends in immunology · 2025Review
- Polyclonal B cells acquire LCMV antigens in a GP1-dependent manner.PLoS pathogens · 2025Article
- Development and characterization of a reverse genetics system for the lineage II Chicava strain of Machupo virus in a guinea pig model.PLoS neglected tropical diseases · 2025Article
- Strategies of rational and structure-driven vaccine design for Arenaviruses.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2024Review
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- Machupo Virus with Mutations in the Transmembrane Domain and Glycosylation Sites of the Glycoprotein Is Attenuated and Immunogenic in Animal Models of Bolivian Hemorrhagic Fever.Journal of virology · 2022Article
- Article
- Glycoprotein N-linked glycans play a critical role in arenavirus pathogenicity.PLoS pathogens · 2021Article
- Article
- The Janus Face of Follicular T Helper Cells in Chronic Viral Infections.Frontiers in immunology · 2018Review
- Mutational Analysis of Lassa Virus Glycoprotein Highlights Regions Required for Alpha-Dystroglycan Utilization.Journal of virology · 2017Article
- 25-Hydroxycholesterol Inhibition of Lassa Virus Infection through Aberrant GP1 Glycosylation.mBio · 2016Article
- Structure-function relationship of the mammarenavirus envelope glycoprotein.Virologica Sinica · 2016Review
- Arenavirus Glycan Shield Promotes Neutralizing Antibody Evasion and Protracted Infection.PLoS pathogens · 2015Article
- Arenavirus stable signal peptide is the keystone subunit for glycoprotein complex organization.mBio · 2014Article
- Crystal structure of Venezuelan hemorrhagic fever virus fusion glycoprotein reveals a class 1 postfusion architecture with extensive glycosylation.Journal of virology · 2013Article
- Watching every step of the way: junín virus attenuation markers in the vaccine lineage.Current genomics · 2013Article
- Targeting virulence mechanisms for the prevention and therapy of arenaviral hemorrhagic fever.Antiviral research · 2013Review
- LCMV glycosylation modulates viral fitness and cell tropism.PloS one · 2013Article
- Envelope glycoprotein of arenaviruses.Viruses · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The glycoprotein of lymphocytic choriomeningitis virus (LCMV) contains nine potential N-linked glycosylation sites. We investigated the function of these N-glycosylations by using alanine-scanning mutagenesis. All the available sites were occupied on GP1 and two of three on GP2. N-linked glycan mutations at positions 87 and 97 on GP1 resulted in reduction of expression and absence of cleavage and were necessary for downstream functions, as confirmed by the loss of GP-mediated fusion activity with T87A and S97A mutants. In contrast, T234A and E379N/A381T mutants impaired GP-mediated cell fusion without altered expression or processing. Infectivity via virus-like particles required glycans and a cleaved glycoprotein. Glycosylation at the first site within GP2, not normally utilized by LCMV, exhibited increased VLP infectivity. We also confirmed the role of the N-linked glycan at position 173 in the masking of the neutralizing epitope GP-1D. Taken together, our results indicated a strong relationship between fusion and infectivity.
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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.