Evidence map›Paper›PMID 18669916›Full record

ArticleGlycobiology2008

Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease.

Vered Padler-Karavani, Hai Yu, Hongzhi Cao, Harshal Chokhawala, Felix Karp, Nissi Varki, Xi Chen, Ajit Varki

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers.

0numbers the graph read from it
0cells of the map it votes in
138citing papers in PubMed
6.1field-weighted citation impact, top 3% of its field
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

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.

3 · Its place in the literature

Who cites it

138 citing papers in PubMed, 319 citations in OpenAlex.

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  15. Serum antibody screening using glycan arrays.Chemical Society reviews · 2024
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78 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Vered Padler-KaravaniGlycobiology Research and Training Center and Department of Medicine, University of California, San Diego, La Jolla, CA 92093, USA.
Hai Yu
Hongzhi Cao
Harshal Chokhawala
Felix Karp
Nissi Varki
Xi Chen
Ajit Varki
University of California, Davis · USUniversity of California, San Diego · US

Funding

BIOSYNTHESIS AND REGULATION OF SUBSTITUTED SIALIC ACIDSR01GM032373 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VARKI, AJIT P · 1985 to 2022
$6.9M
SULFATED OLIGOSACCHARIDES OF NORMAL AND MALIGNANT CELLSR01CA038701 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VARKI, AJIT P · 1985 to 2015
$5.5M
Neu5Gc and anti-Neu5Gc antibodies for detection of cancer and cancer riskU01CA128442 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VARKI, AJIT P · 2007 to 2011
$2.1M
Studies of Naturally Occurring Structurally Modified CarbohydratesR01GM076360 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2006 to 2010
$1.9M
NCI NIH HHS R01CA38701NCI NIH HHS U01 CA128442NIGMS NIH HHS R01 GM076360NIGMS NIH HHS R01GM076360NIGMS NIH HHS R01GM32373
6 · The paper itself

Abstract

Human heterophile antibodies that agglutinate animal erythrocytes are known to detect the nonhuman sialic acid N-glycolylneuraminic acid (Neu5Gc). This monosaccharide cannot by itself fill the binding site (paratope) of an antibody and can also be modified and presented in various linkages, on diverse underlying glycans. Thus, we hypothesized that the human anti-Neu5Gc antibody response is diverse and polyclonal. Here, we use a novel set of natural and chemoenzymatically synthesized glycans to show that normal humans have an abundant and diverse spectrum of such anti-Neu5Gc antibodies, directed against a variety of Neu5Gc-containing epitopes. High sensitivity and specificity assays were achieved by using N-acetylneuraminic acid (Neu5Ac)-containing probes (differing from Neu5Gc by one less oxygen atom) as optimal background controls. The commonest anti-Neu5Gc antibodies are of the IgG class. Moreover, the range of reactivity and Ig classes of antibodies vary greatly amongst normal humans, with some individuals having remarkably large amounts, even surpassing levels of some well-known natural blood group and xenoreactive antibodies. We purified these anti-Neu5Gc antibodies from individual human sera using a newly developed affinity method and showed that they bind to wild-type but not Neu5Gc-deficient mouse tissues. Moreover, they bind back to human carcinomas that have accumulated Neu5Gc in vivo. As dietary Neu5Gc is primarily found in red meat and milk products, we suggest that this ongoing antigen-antibody reaction may generate chronic inflammation, possibly contributing to the high frequency of diet-related carcinomas and other diseases in humans.

Indexed as

AnimalsAntibodiesAntibody SpecificityAntigensDiseaseEnzyme-Linked Immunosorbent AssayEpitopesHealthHumansImmunohistochemistryMiceNeoplasmsNeuraminic AcidsAntibodiesAntigensEpitopesNeuraminic AcidsN-glycolylneuraminic acid

Identifiers

PMID18669916
PMCPMC2586336
OpenAlexW2153180588

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.