Evidence map›Paper›PMID 20212169›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Constraints within major histocompatibility complex class I restricted peptides: presentation and consequences for T-cell recognition.

Alex Theodossis, Carole Guillonneau, Andrew Welland, Lauren K Ely, Craig S Clements, Nicholas A Williamson, Andrew I Webb, Jacqueline A Wilce, Roger J Mulder, Michelle A Dunstone and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 64 citations in OpenAlex.

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  18. The cellular redox environment alters antigen presentation.The Journal of biological chemistry · 2014
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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

15 authors at 3 institutions in 1 country.

Alex TheodossisThe Protein Crystallography Unit, Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Victoria 3800, Australia.
Carole Guillonneau
Andrew Welland
Lauren K Ely
Craig S Clements
Nicholas A Williamson
Andrew I Webb
Jacqueline A Wilce
Roger J Mulder
Michelle A Dunstone
Peter C Doherty
James McCluskey
Anthony W Purcell
Stephen J Turner
Jamie Rossjohn
Monash University · AUUniversity of Melbourne · AUCommonwealth Scientific and Industrial Research Organisation · AU

Funding

Protective Cell-Mediated Immunity Against Lethal H5N1 Influenza A VirusesR01AI070251 · NIAID · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI DOHERTY, PETER C · 2006 to 2010
$2.0M
NIAID NIH HHS R01 AI070251
6 · The paper itself

Abstract

Residues within processed protein fragments bound to major histocompatibility complex class I (MHC-I) glycoproteins have been considered to function as a series of "independent pegs" that either anchor the peptide (p) to the MHC-I and/or interact with the spectrum of alphabeta-T-cell receptors (TCRs) specific for the pMHC-I epitope in question. Mining of the extensive pMHC-I structural database established that many self- and viral peptides show extensive and direct interresidue interactions, an unexpected finding that has led us to the idea of "constrained" peptides. Mutational analysis of two constrained peptides (the HLA B44 restricted self-peptide (B44DPalpha-EEFGRAFSF) and an H2-D(b) restricted influenza peptide (D(b)PA, SSLENFRAYV) demonstrated that the conformation of the prominently exposed arginine in both peptides was governed by interactions with MHC-I-orientated flanking residues from the peptide itself. Using reverse genetics in a murine influenza model, we revealed that mutation of an MHC-I-orientated residue (SSLENFRAYV --> SSLENARAYV) within the constrained PA peptide resulted in a diminished cytotoxic T lymphocyte (CTL) response and the recruitment of a limited pMHC-I specific TCR repertoire. Interactions between individual peptide positions can thus impose fine control on the conformation of pMHC-I epitopes, whereas the perturbation of such constraints can lead to a previously unappreciated mechanism of viral escape.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsAntigen PresentationEpitopesFemaleH-2 AntigensHistocompatibility Antigen H-2DHistocompatibility Antigens Class IHLA-B44 AntigenHLA-B AntigensHumansLigandsMiceMice, Inbred C57BLModels, MolecularEpitopesH-2 AntigensHistocompatibility Antigen H-2DHistocompatibility Antigens Class IHLA-B44 AntigenHLA-B AntigensLigandsPeptide FragmentsViral Proteins

Identifiers

PMID20212169
PMCPMC2851776
OpenAlexW2031951044

What OpenQuestion holds

Textmetadata
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.