Evidence map›Paper›PMID 7520419›Full record

ArticleInfection and immunity1994

Epitopes of the Onchocerca volvulus RAL1 antigen, a member of the calreticulin family of proteins, recognized by sera from patients with onchocerciasis.

L A Rokeach, P A Zimmerman, T R Unnasch

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Frontiers in cellular and infection microbiology · 2018
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Excreted/secreted proteins from trypanosome procyclic strains.Journal of biomedicine & biotechnology · 2010
    Article
  12. Article
  13. Article
  14. Article
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

3 authors at 1 institution in 1 country.

L A RokeachDépartement de Biochimie, Faculté de médecine, Université de Montréal, Québec, Canada.
P A Zimmerman
T R Unnasch
Université de Montréal · CA

Funding

NUCLEAR PROTEINS AND AUTOIMMUNITYR01AI021083 · NIAID · AGOURON INSTITUTE · PI HOCH, SALLIE O · 1985 to 1992
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IDENTIFICATION--ONCHOCERCA VOLVULUS PROTECTIVE EPITOPESR29AI029693 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI UNNASCH, THOMAS R · 1989 to 1993
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AUTOANTIGENS AND RHEUMATIC DISEASER29AR040159 · NIAMS · AGOURON INSTITUTE · PI ROKEACH, LUIS A · 1990 to 1992
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NIAID NIH HHS AI 21083NIAID NIH HHS NIAID AI 29693NIAMS NIH HHS AR 40159
6 · The paper itself

Abstract

RAL1 is an antigen (Ag) encoded by the filarial nematode Onchocerca volvulus, the parasite causing onchocerciasis (river blindness). RAL1 shares 64.4% identity with the autoantigen calreticulin. The striking similarity of the parasite Ag and the human autoantigen has led to the hypothesis that RAL1 may induce a cross-reactive immune response to calreticulin, which in turn may be involved in the pathogenesis of onchocerciasis. To test this hypothesis, we explored the immune response to RAL1 recombinant Ag (RAL1 rAg) and human calreticulin in patients with O. volvulus infection. A total of 86% of the O. volvulus-infected individuals produced antibodies recognizing RAL1 rAg. Antibody reactivity to RAL1 rAg in patient sera was confined primarily to the central and carboxyl-terminal parts of the molecule. No significant correlations were found to associate recognition of RAL1 rAg, or any particular portion thereof, with a particular disease state. Antibodies against RAL1 thus appear to be produced as a general immune reaction to O. volvulus infection and do not necessarily lead to a cross-reacting response with the host protein. In contrast, 33% of the patient sera tested bound recombinant human calreticulin. All of these sera also recognized a polypeptide encompassing the carboxyl-terminal portion of the RAL1 rAg. These results suggest that recognition of an epitope encoded in the carboxyl-terminal portion of RAL1 is at least in part responsible for inducing a cross-reacting immune response to the host protein.

Indexed as

Amino Acid SequenceAnimalsAntigens, HelminthBase SequenceCalciumCalcium-Binding ProteinsCalreticulinDNA, ComplementaryEpitopesHumansMolecular Sequence DataOnchocerca volvulusOnchocerciasisRibonucleoproteinsAntigens, HelminthCalciumCalcium-Binding ProteinsCalreticulinDNA, ComplementaryEpitopesRibonucleoproteins

Identifiers

PMID7520419
PMCPMC303020
OpenAlexW1944653209

What OpenQuestion holds

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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.