Literature DB >> 33430886

Isolation and light chain shuffling of a Plasmodium falciparum AMA1-specific human monoclonal antibody with growth inhibitory activity.

Melanie Seidel-Greven1, Otchere Addai-Mensah1,2, Holger Spiegel1, Gwladys Nina Chiegoua Dipah1, Stefan Schmitz1, Gudrun Breuer1, Margaret Frempong3, Andreas Reimann1, Torsten Klockenbring1, Rainer Fischer1,4,5, Stefan Barth1,6,7, Rolf Fendel8,9.   

Abstract

BACKGROUND: Plasmodium falciparum, the parasite causing malaria, affects populations in many endemic countries threatening mainly individuals with low malaria immunity, especially children. Despite the approval of the first malaria vaccine Mosquirix™ and very promising data using cryopreserved P. falciparum sporozoites (PfSPZ), further research is needed to elucidate the mechanisms of humoral immunity for the development of next-generation vaccines and alternative malaria therapies including antibody therapy. A high prevalence of antibodies against AMA1 in immune individuals has made this antigen one of the major blood-stage vaccine candidates.
MATERIAL AND METHODS: Using antibody phage display, an AMA1-specific growth inhibitory human monoclonal antibody from a malaria-immune Fab library using a set of three AMA1 diversity covering variants (DiCo 1-3), which represents a wide range of AMA1 antigen sequences, was selected. The functionality of the selected clone was tested in vitro using a growth inhibition assay with P. falciparum strain 3D7. To potentially improve affinity and functional activity of the isolated antibody, a phage display mediated light chain shuffling was employed. The parental light chain was replaced with a light chain repertoire derived from the same population of human V genes, these selected antibodies were tested in binding tests and in functionality assays.
RESULTS: The selected parental antibody achieved a 50% effective concentration (EC50) of 1.25 mg/mL. The subsequent light chain shuffling led to the generation of four derivatives of the parental clone with higher expression levels, similar or increased affinity and improved EC50 against 3D7 of 0.29 mg/mL. Pairwise epitope mapping gave evidence for binding to AMA1 domain II without competing with RON2.
CONCLUSION: We have thus shown that a compact immune human phage display library is sufficient for the isolation of potent inhibitory monoclonal antibodies and that minor sequence mutations dramatically increase expression levels in Nicotiana benthamiana. Interestingly, the antibody blocks parasite inhibition independently of binding to RON2, thus having a yet undescribed mode of action.

Entities:  

Keywords:  Apical membrane antigen 1; Chain shuffling; Human monoclonal antibodies; Malaria; Parasite growth inhibition; Phage display; Plant expression; Plasmodium falciparum

Mesh:

Substances:

Year:  2021        PMID: 33430886      PMCID: PMC7798374          DOI: 10.1186/s12936-020-03548-3

Source DB:  PubMed          Journal:  Malar J        ISSN: 1475-2875            Impact factor:   2.979


  76 in total

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Journal:  Infect Immun       Date:  2002-08       Impact factor: 3.441

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Authors:  Dominika J Maskus; Susanne Bethke; Melanie Seidel; Stephanie Kapelski; Otchere Addai-Mensah; Alexander Boes; Güven Edgü; Holger Spiegel; Andreas Reimann; Rainer Fischer; Stefan Barth; Torsten Klockenbring; Rolf Fendel
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Journal:  Nat Commun       Date:  2013       Impact factor: 14.919

9.  Characterization of a novel inhibitory human monoclonal antibody directed against Plasmodium falciparum Apical Membrane Antigen 1.

Authors:  Dominika J Maskus; Michał Królik; Susanne Bethke; Holger Spiegel; Stephanie Kapelski; Melanie Seidel; Otchere Addai-Mensah; Andreas Reimann; Torsten Klockenbring; Stefan Barth; Rainer Fischer; Rolf Fendel
Journal:  Sci Rep       Date:  2016-12-21       Impact factor: 4.379

10.  Reversion of advanced Ebola virus disease in nonhuman primates with ZMapp.

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Journal:  Nature       Date:  2014-08-29       Impact factor: 49.962

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