Evidence map›Paper›PMID 19755422›Full record

ArticleThe Journal of biological chemistry2009

Different strategies adopted by K(b) and L(d) to generate T cell specificity directed against their respective bound peptides.

Natalie A Bowerman, Leremy A Colf, K Christopher Garcia, David M Kranz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Natalie A BowermanDepartment of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Leremy A Colf
K Christopher Garcia
David M Kranz
Stanford University · USUniversity of Illinois Urbana-Champaign · US

Funding

Molecular Principles of TCR Recognition and Activation by peptide-MHCR01AI048540 · NIAID · STANFORD UNIVERSITY · PI GARCIA, KENAN CHRISTOPHER · 2001 to 2010
$2.9M
Structure, Function &Engineering of Tau Cell ReceptorsR01GM055767 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI KRANZ, DAVID M. · 1997 to 2009
$2.4M
Molecular Principles of TCR Recognition and Activation by Peptide MHCR56AI048540 · NIAID · STANFORD UNIVERSITY · PI GARCIA, KENAN CHRISTOPHER · 2011 to 2011
$395k
NIAID NIH HHS AI048540NIAID NIH HHS R01 AI048540NIAID NIH HHS R56 AI048540NIGMS NIH HHS GM55767NIGMS NIH HHS R01 GM055767
6 · The paper itself

Abstract

Mouse T cell clone 2C recognizes two different major histocompatibility (MHC) ligands, the self MHC K(b) and the allogeneic MHC L(d). Two distinct peptides, SIY (SIYRYYGL) and QL9 (QLSPFPFDL), act as strong and specific agonists when bound to K(b) and L(d), respectively. To explore further the mechanisms involved in peptide potency and specificity, here we examined a collection of single amino acid peptide variants of SIY and QL9 for 1) T cell activity, 2) binding to their respective MHC, and 3) binding to the 2C T cell receptor (TCR) and high affinity TCR mutants. Characterization of SIY binding to MHC K(b) revealed significant effects of three SIY residues that were clearly embedded within the K(b) molecule. In contrast, QL9 binding to MHC L(d) was influenced by the majority of peptide side chains, distributed across the entire length of the peptide. Binding of the SIY-K(b) complex to the TCR involved three SIY residues that were pointed toward the TCR, whereas again the majority of QL9 residues influenced binding of TCRs, and thus the QL9 residues had impacts on both L(d) and TCR binding. In general, the magnitude of T cell activity mediated by a peptide variant was influenced more by peptide binding to MHC than by binding the TCR, especially for higher affinity TCRs. Findings with both systems, but QL9-L(d) in particular, suggest that many single-residue substitutions, introduced into peptides to improve their binding to MHC and thus their vaccine potential, could impair T cell reactivity due to their dual impact on TCR binding.

Indexed as

Major Histocompatibility ComplexAnimalsBinding SitesCell MembraneDose-Response Relationship, DrugLymphocyte ActivationMiceMolecular ConformationOligopeptidesPeptidesProtein BindingProtein Structure, TertiaryReceptors, Antigen, T-CellT-LymphocytesOligopeptidesPeptidesQL9 peptideReceptors, Antigen, T-Cellsuperagonist SIYR

Identifiers

PMID19755422
PMCPMC2781669
OpenAlexW2018133767

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.