ArticleEBioMedicine2020
Interferon-α alters host glycosylation machinery during treated HIV infection.
Article in EBioMedicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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The trial behind it
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Expression of type I interferon-associated genes at antiretroviral therapy interruption predicts HIV virological rebound.Scientific reports · 2022Trial
- Persistent CD8Frontiers in immunology · 2026Article
- Glycosylated IgG antibodies contribute to the recovery of haemorrhagic fever with renal syndrome patients.eLife · 2025Article
- Discovery and characterization of vertebrate sialoglycan-binding proteins.Seminars in immunology · 2025Review
- Post-translational modification of NK cell receptors offers clues to antigenic specificity riddle.Frontiers in immunology · 2025Review
- Interferons in HIV-1 infection: mechanisms, antiviral potentials, and therapeutic challenges.Frontiers in immunology · 2025Review
- Clinical glycoproteomics: methods and diseases.MedComm · 2024Review
- Immunoglobulin G N-glycan markers of accelerated biological aging during chronic HIV infection.Nature communications · 2024Article
- Plasma Glycomic Markers of Accelerated Biological Aging During Chronic HIV Infection.bioRxiv : the preprint server for biology · 2023Article
- Differences in Immunoglobulin G Glycosylation Between Influenza and COVID-19 Patients.Engineering (Beijing, China) · 2022Article
- Article
- Glycosylation as a key parameter in the design of nucleic acid vaccines.Current opinion in structural biology · 2022Review
- N-Glycosylation and Inflammation; the Not-So-Sweet Relation.Frontiers in immunology · 2022Review
- Glycosylation tips the scales: Novel insights into the dual role of type-I interferons in treated HIV infection.EBioMedicine · 2020Article
Corrections and comments
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Authors and funding
17 authors at 4 institutions in 2 countries.
Funding
Abstract
backgroundA comprehensive understanding of host factors modulated by the antiviral cytokine interferon-α (IFNα) is imperative for harnessing its beneficial effects while avoiding its detrimental side-effects during HIV infection. Cytokines modulate host glycosylation which plays a critical role in mediating immunological functions. However, the impact of IFNα on host glycosylation has never been characterized.
methodsWe assessed the impact of pegylated IFNα2a on IgG glycome, as well as CD8
findingsWe identified significant interactions that support a model in which a) IFNα increases the proportion of pro-inflammatory, bisecting GlcNAc glycans (known to enhance FcγR binding) within the IgG glycome, which in turn b) increases inflammation, which c) leads to poor CD8
interpretationIFNα causes host glycomic alterations that are known to modulate immunological responses. These alterations are associated with both detrimental and beneficial consequences of IFNα. Manipulating host glycomic interactions may represent a strategy for enhancing the positive effects of IFNα while avoiding its detrimental side-effects.
fundingNIH grants R21AI143385, U01AI110434.
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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.