ArticleAIDS (London, England)2017
Serum glycan-binding IgG antibodies in HIV-1 infection and during the development of broadly neutralizing responses.
Article in AIDS (London, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 13 citations in OpenAlex.
- Serum antibody screening using glycan arrays.Chemical Society reviews · 2024Review
- Article
- Virus Evolution and Neutralization Sensitivity in an HIV-1 Subtype B' Infected Plasma Donor with Broadly Neutralizing Activity.Vaccines · 2021Article
- Abnormal antibodies to self-carbohydrates in SARS-CoV-2 infected patients.bioRxiv : the preprint server for biology · 2020Article
- Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins.Frontiers in chemistry · 2019Review
- Anti-glycan IgM repertoires in newborn human cord blood.PloS one · 2019Article
- Development of a Multiplex Glycan Microarray Assay and Comparative Analysis of Human Serum Anti-Glycan IgA, IgG, and IgM Repertoires.ACS omega · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundThe HIV-1 envelope is covered with glycans that provide structural integrity and protect conserved regions from host antibody responses. However, these glycans are often the target of broadly neutralizing antibodies (bNAbs) that emerge in some HIV-infected individuals. We aimed to determine whether antiglycan IgG antibodies are a general response to HIV-1 infection or specific to individuals who develop bNAbs.
methodsIgG binding to glycans was assessed using arrays that contained 245 unique components including N-linked carbohydrates, glycolipids, and Tn-peptides. Sera from 20 HIV-negative and 27 HIV-positive women (including 12 individuals who developed bNAbs) were profiled longitudinally. HIV-1 gp120 proteins were used to compete for binding to the array.
resultsAntiglycan IgG antibodies fluctuated over a 3-year period, irrespective of HIV infection. However, HIV-positive individuals had elevated binding to 40 components on the array that included Man8, Man9, Tn-peptides, heat shock protein, and glycolipids. Competition experiments confirmed that a proportion of these glycan-binding IgG antibodies were HIV-1-specific, some of which were higher in individuals who developed bNAbs.
conclusionsHIV-1 infection is associated with elevated levels of IgG antibodies to specific glycans. Furthermore, some antiglycan IgG antibodies were more abundant in individuals with bNAbs, suggesting a unique phenotype that may be informative for HIV vaccine design.
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Registered trials
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