Evidence map›Paper›PMID 27550523›Full record

ArticleJournal of proteome research2017

Identification and Characterization of Complex Glycosylated Peptides Presented by the MHC Class II Processing Pathway in Melanoma.

Stacy A Malaker, Michael J Ferracane, Florence R Depontieu, Angela L Zarling, Jeffrey Shabanowitz, Dina L Bai, Suzanne L Topalian, Victor H Engelhard, Donald F Hunt

Abstract read
In one paragraph

Article in Journal of proteome research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Immunoproteomics: The Evolution from Classical Methods to Emerging Techniques.Methods in molecular biology (Clifton, N.J.) · 2026
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  9. ProfoundFrontiers in immunology · 2023
    Article
  10. Revealing the human mucinome.Nature communications · 2022
    Article
  11. Article
  12. Review
  13. Review
  14. Engineering neoantigen vaccines to improve cancer personalized immunotherapy.International journal of biological sciences · 2022
    Review
  15. Article
  16. Article
  17. Optimal Dissociation Methods Differ forJournal of proteome research · 2020
    Article
  18. Article
  19. Review
  20. 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

9 authors at 2 institutions in 1 country.

Stacy A Malaker
Michael J FerracaneDepartment of Medicinal Chemistry, University of Florida , Gainesville, Florida 32610, United States.
Florence R DepontieuDepartment of Surgery, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Angela L Zarling
Jeffrey Shabanowitz
Dina L Bai
Suzanne L TopalianDepartment of Surgery, Johns Hopkins University School of Medicine , Baltimore, Maryland 21205, United States.
Victor H Engelhard
Donald F Hunt
Johns Hopkins Medicine · USUniversity of Florida · US

Funding

Women's Oncology Program - WONP30CA044579 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Thomas P. Loughran · 1987 to 2026
$72.1M
INTERDISCIPLINARY TRAINING PROGRAM IN IMMUNOLOGYT32AI007496 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Michael G. Brown, Coleen A McNamara · 1995 to 2026
$10.2M
PROCESSED ANTIGEN CHARACTERIZATION BY MASS SPECTROMETRYR37AI033993 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1999 to 2008
$5.6M
PROCESSED ANTIGEN CHARACTERIZATION BY MASS SPECTROMETRYR01AI033993 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI HUNT, DONALD F · 1994 to 2017
$4.9M
Antigenic Determinants on HLA-B7 and -A2R01CA134060 · NCI · UNIVERSITY OF VIRGINIA · PI ENGELHARD, VICTOR H · 2008 to 2012
$2.4M
NCI NIH HHS P30 CA044579NCI NIH HHS R01 CA134060NIAID NIH HHS R01 AI033993NIAID NIH HHS R37 AI033993NIAID NIH HHS T32 AI007496
6 · The paper itself

Abstract

The MHC class II (MHCII) processing pathway presents peptides derived from exogenous or membrane-bound proteins to CD4+ T cells. Several studies have shown that glycopeptides are necessary to modulate CD4+ T cell recognition, though glycopeptide structures in these cases are generally unknown. Here, we present a total of 93 glycopeptides from three melanoma cell lines and one matched EBV-transformed line with most found only in the melanoma cell lines. The glycosylation we detected was diverse and comprised 17 different glycoforms. We then used molecular modeling to demonstrate that complex glycopeptides are capable of binding the MHC and may interact with complementarity determining regions. Finally, we present the first evidence of disulfide-bonded peptides presented by MHCII. This is the first large scale study to sequence glyco- and disulfide bonded MHCII peptides from the surface of cancer cells and could represent a novel avenue of tumor activation and/or immunoevasion.

Indexed as

Amino Acid SequenceBinding SitesCarbohydrate SequenceCell Line, TumorComplementarity Determining RegionsCrystallography, X-RayDisulfidesGlycopeptidesGlycosylationHLA-DR AntigensHumansMelanocytesModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandComplementarity Determining RegionsDisulfidesGlycopeptidesHLA-DR Antigensglycopeptide analysisimmunologymass spectrometryMHC class II

Identifiers

PMID27550523
PMCPMC5218890
OpenAlexW2508250503

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.