Literature DB >> 25355939

High-throughput screening platform identifies small molecules that prevent sequestration of Plasmodium falciparum-infected erythrocytes.

Justin Gullingsrud1, Neta Milman1, Tracy Saveria1, Olga Chesnokov2, Kathryn Williamson1, Anand Srivastava3, Benoit Gamain3, Patrick E Duffy4, Andrew V Oleinikov5.   

Abstract

BACKGROUND: We developed a 2-step approach to screen molecules that prevent and/or reverse Plasmodium falciparum-infected erythrocyte (IE) binding to host receptors. IE adhesion and sequestration in vasculature causes severe malaria, and therefore antiadhesion therapy might be useful as adjunctive treatment. IE adhesion is mediated by the polymorphic family (approximately 60 members) of P. falciparum EMP1 (PfEMP1) multidomain proteins.
METHODS: We constructed sets of PfEMP1 domains that bind ICAM-1, CSA, or CD36, receptors that commonly support IE binding. Combinations of domain-coated beads were assayed by Bio-Plex technology as a high-throughput molecular platform to screen antiadhesion molecules (antibodies and small molecules). Molecules identified as so-called hits in the screen (first step) then could be assayed individually for inhibition of binding of live IE to receptors (second step).
RESULTS: In proof-of-principle studies, the antiadhesion activity of several antibodies was concordant in Bio-Plex and live IE assays. Using this 2-step approach, we identified several molecules in a small molecule library of 10 000 compounds that could inhibit and reverse binding of IEs to ICAM-1 and CSA receptors.
CONCLUSION: This 2-step screening approach should be efficient for identification of antiadhesion drug candidates for falciparum malaria. Published by Oxford University Press on behalf of the Infectious Diseases Society of America 2014. This work is written by (a) US Government employee(s) and is in the public domain in the US.

Entities:  

Keywords:  CD36; CSA; ICAM-1; PfEMP1 proteins; Plasmodium falciparum; antiadhesion therapy; high-throughput screening; host receptors; malaria; sequestration of parasites; small molecules

Mesh:

Substances:

Year:  2014        PMID: 25355939      PMCID: PMC4366606          DOI: 10.1093/infdis/jiu589

Source DB:  PubMed          Journal:  J Infect Dis        ISSN: 0022-1899            Impact factor:   5.226


  31 in total

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2.  Induction of adhesion-inhibitory antibodies against placental Plasmodium falciparum parasites by using single domains of VAR2CSA.

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3.  Clinical significance of sequestration in adults with severe malaria.

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9.  Human monoclonal IgG selection of Plasmodium falciparum for the expression of placental malaria-specific variant surface antigens.

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4.  Plasmodium falciparum infected erythrocytes can bind to host receptors integrins αVβ3 and αVβ6 through DBLδ1_D4 domain of PFL2665c PfEMP1 protein.

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Review 6.  Malaria Parasite Plasmodium falciparum Proteins on the Surface of Infected Erythrocytes as Targets for Novel Drug Discovery.

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