ArticleOncotarget2017
Fungal lectin MpL enables entry of protein drugs into cancer cells and their subcellular targeting.
Article in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- The Entomotoxic Fungal LectinJournal of agricultural and food chemistry · 2026Article
- Unlocking the Power: New Insights into the Anti-Aging Properties of Mushrooms.Journal of fungi (Basel, Switzerland) · 2024Review
- Possibilities of UsingInternational journal of food science · 2022Review
- LectinOracle: A Generalizable Deep Learning Model for Lectin-Glycan Binding Prediction.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Antiproliferative and Antimicrobial Potentials of a Lectin fromMarine drugs · 2021Article
- Lectin-Mediated Binding of EngineeredMicroorganisms · 2021Article
- Overview of the role of kinetoplastid surface carbohydrates in infection and host cell invasion: prospects for therapeutic intervention.Parasitology · 2019Review
- CNL-Molecules (Basel, Switzerland) · 2019Review
- MytiLec-1 Shows Glycan-Dependent Toxicity against Brine ShrimpMarine drugs · 2019Article
- Antioxidant Versus Pro-Apoptotic Effects of Mushroom-Enriched Diets on Mitochondria in Liver Disease.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lectins have been recognized as promising carrier molecules for targeted drug delivery. They specifically bind carbohydrate moieties on cell membranes and trigger cell internalization. Fungal lectin MpL (Macrolepiota procera lectin) does not provoke cancer cell cytotoxicity but is able to bind aminopeptidase N (CD13) and integrin α3β1, two glycoproteins that are overexpressed on the membrane of tumor cells. Upon binding, MpL is endocytosed in a clathrin-dependent manner and accumulates initially in the Golgi apparatus and, finally, in the lysosomes. For effective binding and internalization a functional binding site on the α-repeat is needed. To test the potential of MpL as a carrier for delivering protein drugs to cancer cells we constructed fusion proteins consisting of MpL and the cysteine peptidase inhibitors cystatin C and clitocypin. The fused proteins followed the same endocytic route as the unlinked MpL. Peptidase inhibitor-MpL fusions impaired both the intracellular degradation of extracellular matrix and the invasiveness of cancer cells. MpL is thus shown in vitro to be a lectin that can enable protein drugs to enter cancer cells, enhance their internalization and sort them to lysosomes and the Golgi apparatus.
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Registered trials
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.