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Targeting Human Cancer by a Glycosaminoglycan Binding Malaria Protein

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

DOI

  1. Molecular Evolution of Early-Onset Prostate Cancer Identifies Molecular Risk Markers and Clinical Trajectories

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  2. Targeting transcriptional addictions in small cell lung cancer with a covalent CDK7 inhibitor

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  3. Integrative Genomic Analyses Reveal an Androgen-Driven Somatic Alteration Landscape in Early-Onset Prostate Cancer

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  1. Capture and Detection of Circulating Glioma Cells Using the Recombinant VAR2CSA Malaria Protein

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  2. A proof-of-concept study for the design of a VLP-based combinatorial HPV and placental malaria vaccine

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  3. Fighting Cancer Using an Oncofetal Glycosaminoglycan-Binding Protein from Malaria Parasites

    Publikation: Bidrag til tidsskriftReviewForskningpeer review

Vis graf over relationer

Plasmodium falciparum engineer infected erythrocytes to present the malarial protein, VAR2CSA, which binds a distinct type chondroitin sulfate (CS) exclusively expressed in the placenta. Here, we show that the same CS modification is present on a high proportion of malignant cells and that it can be specifically targeted by recombinant VAR2CSA (rVAR2). In tumors, placental-like CS chains are linked to a limited repertoire of cancer-associated proteoglycans including CD44 and CSPG4. The rVAR2 protein localizes to tumors in vivo and rVAR2 fused to diphtheria toxin or conjugated to hemiasterlin compounds strongly inhibits in vivo tumor cell growth and metastasis. Our data demonstrate how an evolutionarily refined parasite-derived protein can be exploited to target a common, but complex, malignancy-associated glycosaminoglycan modification.

OriginalsprogEngelsk
TidsskriftCancer Cell
Vol/bind28
Udgave nummer4
Sider (fra-til)500-14
Antal sider15
ISSN1535-6108
DOI
StatusUdgivet - 12 okt. 2015

ID: 45788504