Evidence map›Paper›PMID 26748477›Full record

ArticleArthritis & rheumatology (Hoboken, N.J.)2016

Increased Conformational Flexibility of HLA-B*27 Subtypes Associated With Ankylosing Spondylitis.

Bernhard Loll, Heinz Fabian, Hans Huser, Chee-Seng Hee, Alexander Ziegler, Barbara Uchanska-Ziegler, Andreas Ziegler

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In one paragraph

Article in Arthritis & rheumatology (Hoboken, N.J.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

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

20 citing papers in PubMed.

  1. Trial
  2. Review
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  4. Uncovering the Underworld of Axial Spondyloarthritis.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. The molecular basis of how buried human leukocyte antigen polymorphism modulates natural killer cell function.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
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  16. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Bernhard LollFreie Universität Berlin, Berlin, Germany.ORCID 0000-0001-7928-4488
Heinz Fabian
Hans HuserCharité-Universitätsmedizin Berlin and Freie Universität Berlin, Berlin, Germany.
Chee-Seng HeeUniversität Basel, Basel, Switzerland.
Alexander ZieglerUniversität Bonn, Bonn, Germany.
Barbara Uchanska-ZieglerCharité-Universitätsmedizin Berlin and Freie Universität Berlin, Berlin, Germany.
Andreas ZieglerZiegler Biosolutions, Waldshut-Tiengen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveDissimilarities in antigen processing and presentation are known to contribute to the differential association of HLA-B*27 subtypes with the inflammatory rheumatic disease ankylosing spondylitis (AS). In support of this notion, previous x-ray crystallographic data showed that peptides can be displayed by almost identical HLA-B*27 molecules in a subtype-dependent manner, allowing cytotoxic T lymphocytes to distinguish between these subtypes. For example, a human self-peptide derived from vasoactive intestinal peptide receptor type 1 (pVIPR; sequence RRKWRRWHL) is displayed in a single conformation by B*27:09 (which is not associated with AS), while B*27:05 (which is associated with AS) presents the peptide in a dual binding mode. In addition, differences in conformational flexibility between these subtypes might affect their stability or antigen presentation capability. This study was undertaken to investigate B*27:04 and B*27:06, another pair of minimally distinct HLA-B*27 subtypes, to assess whether dual peptide conformations or structural dynamics play a role in the initiation of AS.

methodsUsing x-ray crystallography, we determined the structures of the pVIPR-B*27:04 and pVIPR-B*27:06 complexes and used isotope-edited infrared (IR) spectroscopy to probe the dynamics of these HLA-B*27 subtypes.

resultsAs opposed to B*27:05 and B*27:09, B*27:04 (which is associated with AS) displays pVIPR conventionally and B*27:06 (which is not associated with AS) presents the peptide in a dual conformation. Comparison of the 4 HLA-B*27 subtypes using IR spectroscopy revealed that B*27:04 and B*27:05 possess elevated molecular dynamics compared to the nonassociated subtypes B*27:06 and B*27:09.

conclusionOur results demonstrate that an increase in conformational flexibility characterizes the disease-associated subtypes B*27:04 and B*27:05.

Indexed as

Crystallography, X-RayHLA-B27 AntigenHumansMolecular ConformationMolecular Docking SimulationProtein BindingProtein ConformationReceptors, Vasoactive Intestinal Polypeptide, Type ISpectroscopy, Fourier Transform InfraredSpondylitis, AnkylosingT-Lymphocytes, CytotoxicHLA-B*27:04 antigenHLA-B*27:06 antigenHLA-B27 AntigenReceptors, Vasoactive Intestinal Polypeptide, Type IVIPR1 protein, human

Identifiers

PMID26748477

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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.