Evidence map›Paper›PMID 27551071›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Precision glycocalyx editing as a strategy for cancer immunotherapy.

Han Xiao, Elliot C Woods, Petar Vukojicic, Carolyn R Bertozzi

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 246 papers.

0numbers the graph read from it
0cells of the map it votes in
246citing papers in PubMed
14.3field-weighted citation impact, top 1% 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

246 citing papers in PubMed, 430 citations in OpenAlex.

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186 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Han XiaoDepartment of Chemistry, Stanford University, Stanford, CA 94305-4404; Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305-4404.
Elliot C WoodsDepartment of Chemistry, Stanford University, Stanford, CA 94305-4404; Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305-4404.
Petar VukojicicDepartment of Chemistry, Stanford University, Stanford, CA 94305-4404; Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305-4404.
Carolyn R BertozziDepartment of Chemistry, Stanford University, Stanford, CA 94305-4404; Howard Hughes Medical Institute, Stanford University, Stanford, CA 94305-4404 bertozzi@stanford.edu.
Stanford University · USHoward Hughes Medical Institute · US

Funding

Investigations of Golgi EnzymesR01GM059907 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERTOZZI, CAROLYN · 1999 to 2016
$5.9M
Development of Mucin-mimetics to Study the Role of the Glycocalyx in OncogenesisF31CA200544 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI WOODS, ELLIOT CARTER · 2015 to 2016
$74k
NCI NIH HHS F31 CA200544NIGMS NIH HHS R01 GM059907
6 · The paper itself

Abstract

Cell surface sialosides constitute a central axis of immune modulation that is exploited by tumors to evade both innate and adaptive immune destruction. Therapeutic strategies that target tumor-associated sialosides may therefore potentiate antitumor immunity. Here, we report the development of antibody-sialidase conjugates that enhance tumor cell susceptibility to antibody-dependent cell-mediated cytotoxicity (ADCC) by selective desialylation of the tumor cell glycocalyx. We chemically fused a recombinant sialidase to the human epidermal growth factor receptor 2 (HER2)-specific antibody trastuzumab through a C-terminal aldehyde tag. The antibody-sialidase conjugate desialylated tumor cells in a HER2-dependent manner, reduced binding by natural killer (NK) cell inhibitory sialic acid-binding Ig-like lectin (Siglec) receptors, and enhanced binding to the NK-activating receptor natural killer group 2D (NKG2D). Sialidase conjugation to trastuzumab enhanced ADCC against tumor cells expressing moderate levels of HER2, suggesting a therapeutic strategy for cancer patients with lower HER2 levels or inherent trastuzumab resistance. Precision glycocalyx editing with antibody-enzyme conjugates is therefore a promising avenue for cancer immune therapy.

Indexed as

ImmunotherapyAntibody-Dependent Cell CytotoxicityCell Line, TumorDrug Resistance, NeoplasmErb-b2 Receptor Tyrosine KinasesGlycocalyxHumansKiller Cells, NaturalNeoplasmsNeuraminidaseNK Cell Lectin-Like Receptor Subfamily KSialic Acid Binding Ig-like Lectin 1TrastuzumabERBB2 protein, humanErb-b2 Receptor Tyrosine KinasesNeuraminidaseNK Cell Lectin-Like Receptor Subfamily KSialic Acid Binding Ig-like Lectin 1SIGLEC1 protein, humanTrastuzumabADCCcancer immune therapysialic acidSiglectrastuzumab

Identifiers

PMID27551071
PMCPMC5027407
OpenAlexW2508974650

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.