Evidence map›Paper›PMID 28754944›Full record

ArticleNature chemistry2017

Cytosolic antibody delivery by lipid-sensitive endosomolytic peptide.

Misao Akishiba, Toshihide Takeuchi, Yoshimasa Kawaguchi, Kentarou Sakamoto, Hao-Hsin Yu, Ikuhiko Nakase, Tomoka Takatani-Nakase, Fatemeh Madani, Astrid Gräslund, Shiroh Futaki

Abstract read
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In one paragraph

Article in Nature chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 130 papers.

0numbers the graph read from it
0cells of the map it votes in
130citing papers in PubMed
–field-weighted citation impact
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

130 citing papers in PubMed.

  1. Review
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  13. Microcondensate-Mediated Intracellular Infusion of mRNA Across the Plasma Membrane.Angewandte Chemie (International ed. in English) · 2026
    Article
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  18. Hydrophilic α-Aryl-α-Diazoamides for Protein Esterification.Synlett : accounts and rapid communications in synthetic organic chemistry · 2025
    Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Misao AkishibaInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Toshihide TakeuchiInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Yoshimasa KawaguchiInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Kentarou SakamotoInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Hao-Hsin YuInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Ikuhiko NakaseInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Tomoka Takatani-NakaseSchool of Pharmacy and Pharmaceutical Sciences, Mukogawa Women's University, Nishinomiya, Hyogo 663-8179, Japan.
Fatemeh MadaniDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories, Stockholm University, 10691 Stockholm, Sweden.
Astrid GräslundDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories, Stockholm University, 10691 Stockholm, Sweden.
Shiroh FutakiInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One of the major obstacles in intracellular targeting using antibodies is their limited release from endosomes into the cytosol. Here we report an approach to deliver proteins, which include antibodies, into cells by using endosomolytic peptides derived from the cationic and membrane-lytic spider venom peptide M-lycotoxin. The delivery peptides were developed by introducing one or two glutamic acid residues into the hydrophobic face. One peptide with the substitution of leucine by glutamic acid (L17E) was shown to enable a marked cytosolic liberation of antibodies (immunoglobulins G (IgGs)) from endosomes. The predominant membrane-perturbation mechanism of this peptide is the preferential disruption of negatively charged membranes (endosomal membranes) over neutral membranes (plasma membranes), and the endosomolytic peptide promotes the uptake by inducing macropinocytosis. The fidelity of this approach was confirmed through the intracellular delivery of a ribosome-inactivation protein (saporin), Cre recombinase and IgG delivery, which resulted in a specific labelling of the cytosolic proteins and subsequent suppression of the glucocorticoid receptor-mediated transcription. We also demonstrate the L17E-mediated cytosolic delivery of exosome-encapsulated proteins.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionCell MembraneCytosolDrug CarriersDrug LiberationEndocytosisEndosomesHeLa CellsHumansImmunoglobulin GIntegrasesPinocytosisProtein EngineeringSaporinsSpider VenomsCre recombinaseDrug CarriersImmunoglobulin GIntegrasesSaporinsSpider Venoms

Identifiers

PMID28754944

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.