Evidence map›Paper›PMID 23297227›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Sortase-mediated modification of αDEC205 affords optimization of antigen presentation and immunization against a set of viral epitopes.

Lee Kim Swee, Carla P Guimaraes, Sharvan Sehrawat, Eric Spooner, M Inmaculada Barrasa, Hidde L Ploegh

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Article
  3. Site-directed antibody conjugation via ubiquitination.Nature biomedical engineering · 2025
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  7. Article
  8. Review
  9. Article
  10. Precision Modification of Native Antibodies.Bioconjugate chemistry · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Biomaterials for vaccine-based cancer immunotherapy.Journal of controlled release : official journal of the Controlled Release Society · 2018
    Review
  17. Article
  18. Article
  19. Review
  20. Review
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

6 authors at 2 institutions in 1 country.

Lee Kim SweeWhitehead Institute for Biomedical Research and Massachusetts Institute of Technology, Cambridge, MA 02142, USA.
Carla P Guimaraes
Sharvan Sehrawat
Eric Spooner
M Inmaculada Barrasa
Hidde L Ploegh
Whitehead Institute for Biomedical Research · USMassachusetts Institute of Technology · US

Funding

Sortase-mediated protein engineering for the study of host-pathogen interactionsR01AI087879 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2010 to 2019
$4.5M
Endosomal TLRs and their accessory proteins: cell biology and biochemistryR01GM100518 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2012 to 2015
$1.5M
Enzymatic modification of anti-DEC205 to manipulate its immunogenic propertiesR21AI098159 · NIAID · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PLOEGH, HIDDE L. · 2012 to 2013
$522k
NIAID NIH HHS AI098159NIAID NIH HHS R01 AI087879NIAID NIH HHS R21 AI098159NIGMS NIH HHS R01 GM100518
6 · The paper itself

Abstract

A monoclonal antibody against the C-type lectin DEC205 (αDEC205) is an effective vehicle for delivery of antigens to dendritic cells through creation of covalent αDEC205-antigen adducts. These adducts can induce antigen-specific T-cell immune responses or tolerance. We exploit the transpeptidase activity of sortase to install modified peptides and protein-sized antigens onto the heavy chain of αDEC205, including linkers that contain nonnatural amino acids. We demonstrate stoichiometric site-specific labeling on a scale not easily achievable by genetic fusions (49 distinct fusions in this report). We conjugated a biotinylated version of a class I MHC-restricted epitope to unlabeled αDEC205 and monitored epitope generation upon binding of the adduct to dendritic cells. Our results show transfer of αDEC205 heavy chain to the cytoplasm, followed by proteasomal degradation. Introduction of a labile dipeptide linker at the N terminus of a T-cell epitope improves proteasome-dependent class I MHC-restricted peptide cross-presentation when delivered by αDEC205 in vitro and in vivo. We also conjugated αDEC205 with a linker-optimized peptide library of known CD8 T-cell epitopes from the mouse γ-herpes virus 68. Animals immunized with such conjugates displayed a 10-fold reduction in viral load.

Indexed as

Amino Acid SequenceAminoacyltransferasesAnimalsAntigen PresentationAntigens, CDAntigens, ViralBacterial ProteinsCD8-Positive T-LymphocytesCysteine EndopeptidasesEpitopes, T-LymphocyteHerpesviridae InfectionsHistocompatibility Antigens Class IImmunizationImmunoconjugatesLectins, C-TypeMiceAminoacyltransferasesAntigens, CDAntigens, ViralBacterial ProteinsCysteine EndopeptidasesDEC-205 receptorEpitopes, T-LymphocyteHistocompatibility Antigens Class IImmunoconjugatesLectins, C-TypeMinor Histocompatibility AntigensProteasome Endopeptidase ComplexReceptors, Cell Surfacesortase AVaccines, SubunitViral Vaccines

Identifiers

PMID23297227
PMCPMC3557095
OpenAlexW2096848916

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.