Evidence map›Paper›PMID 31492138›Full record

ArticleJournal of biomedical science2019

Most of anti-glycolipid IgG-antibodies associated to neurological disorders occur without their IgM counterpart.

Ricardo Dante Lardone, Fernando José Irazoqui, Gustavo Alejandro Nores

Abstract read
In one paragraph

Article in Journal of biomedical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

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3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

3 authors.

Ricardo Dante LardoneFacultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina. rlardone@fcq.unc.edu.ar.ORCID http://orcid.org/0000-0003-3569-8755
Fernando José IrazoquiFacultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.
Gustavo Alejandro NoresFacultad de Ciencias Químicas. Departamento de Química Biológica Ranwel Caputto, Universidad Nacional de Córdoba, Ciudad Universitaria, X5000HUA, Córdoba, Argentina.

Funding

Consejo Nacional de Investigaciones Científicas y Técnicas PIP 11220150100226, 2016-18Fondo para la Investigación Científica y Tecnológica PICT-0223-2017Ministerio de Ciencia y Tecnología, Gobierno de la Provincia de Córdoba Res 144/18, 2018-19Secretaria de Ciencia y Tecnología - Universidad Nacional de Córdoba PIP 20180101251
6 · The paper itself

Abstract

backgroundDifferent neurological disorders frequently display antibodies against several self-glycans. Increasing evidence supports their pathogenic role; however, far less is known about their origin. Meanwhile, antibodies recognizing non-self glycans appear in normal human serum during immune response to bacteria.

methodsUsing high performance thin layer chromatography-immunostaining, we comparatively evaluated humoral immune response (IgG and IgM immunoreactivity) against glycolipids carrying self-glycans (GM3/GM2/GM1/GD1a/GD1b/GD3/GT1b/GQ1b) and non-self glycans (Forssman/GA1/"A" blood group/Nt7) in sera from 383 patients with neurological disorders along with 87 healthy controls.

resultsIn contrast to no healthy controls having anti-self glycan IgG antibodies, one-fifth of patients' sera had anti-self glycan IgG antibodies: remarkably, 60% of these occurred without IgM antibodies of the same specificity. Contrary to this unusual fact (anti-self glycan IgG occurrence without simultaneous presence of IgM having the same specificity ~ IgG/IgM discordance), all IgG antibodies against non-self glycans occurred simultaneously with their IgM antibody counterpart (i.e. 0% discordance). When analyzed closer, the IgG/IgM discordance frequency for anti-self glycans exhibited a dual trend: below 40% for IgG antibodies against GM2, GM1 and GD1b, and greater than 53% for IgG antibodies against the remaining self glycans. Interestingly, this discordance behavior was common to several different neurological disorders.

conclusionsClassic immunology principles indicate this anti-self glycan IgG/IgM discordance should not occur in an antibody response; its unusual presence is discussed within the "binding site drift hypothesis" context, where anti-self glycan IgG antibodies could originate from pre-existing IgG recognizing structurally-related non-self glycans.

Indexed as

Antibodies, Anti-IdiotypicArgentinaGlycolipidsHumansImmunoglobulin MNervous System DiseasesAntibodies, Anti-Idiotypicanti-IgGGlycolipidsImmunoglobulin MAnti-ganglioside IgG-antibodiesAutoimmunityGlycanGlycolipidIgG/IgM discordanceNeurological disorder

Identifiers

PMID31492138
PMCPMC6729026

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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.