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A broadly cross-reactive i-body to AMA1 potently inhibits blood and liver stages of Plasmodium parasites

Nat Commun. 2024-08; 
Dimuthu Angage, Jill Chmielewski, Janesha C Maddumage, Eva Hesping, Sabrina Caiazzo, Keng Heng Lai, Lee Ming Yeoh, Joseph Menassa, D Herbert Opi, Callum Cairns, Hamsa Puthalakath, James G Beeson, Marc Kvansakul, Justin A Boddey, Danny W Wilson, Robin F Anders, Michael Foley
Products/Services Used Details Operation
Gene Synthesis Codon-optimised full ectodomain (domain I, II and III) and domain I + II (for X-ray structure determination experiments) sequences of Pf3D7, W2mef, 7G8, FVO, HB3, D10 and PcAMA1 were cloned into pET-28a(+)-Tev vector (Genscript, Singapore). Sequences of Human IgG1 Fc region-tagged WD33 and WD34 were designed by cloning into a PcDNA3.1 vector (Genscript, Singapore) to express i-body Fc versions in Expi293 and ExpiCHO (Invitrogen, USA) expression systems. Get A Quote

摘要

Apical membrane antigen-1 (AMA1) is a conserved malarial vaccine candidate essential for the formation of tight junctions with the rhoptry neck protein (RON) complex, enabling Plasmodium parasites to invade human erythrocytes, hepatocytes, and mosquito salivary glands. Despite its critical role, extensive surface polymorphisms in AMA1 have led to strain-specific protection, limiting the success of AMA1-based interventions beyond initial clinical trials. Here, we identify an i-body, a humanised single-domain antibody-like molecule that recognises a conserved pan-species conformational epitope in AMA1 with low nanomolar affinity and inhibits the binding of the RON2 ligand to AMA1. Structural characterisation indi... More

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