scholarly journals Can growth inhibition assays (GIA) predict blood-stage malaria vaccine efficacy?

2012 ◽  
Vol 8 (6) ◽  
pp. 706-714 ◽  
Author(s):  
Christopher J.A. Duncan ◽  
Adrian V.S. Hill ◽  
Ruth D. Ellis
Keyword(s):  
Growth Inhibition ◽  
Vaccine Efficacy ◽  
Malaria Vaccine ◽  
Blood Stage ◽  
Blood Stage Malaria

scholarly journals Strain-specific Plasmodium falciparum growth inhibition among Malian children immunized with a blood-stage malaria vaccine

PLoS ONE ◽  
2017 ◽  
Vol 12 (3) ◽  
pp. e0173294 ◽  
Author(s):  
Matthew B. Laurens ◽  
Bourema Kouriba ◽  
Elke Bergmann-Leitner ◽  
Evelina Angov ◽  
Drissa Coulibaly ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Growth Inhibition ◽  
Malaria Vaccine ◽  
Blood Stage ◽  
Blood Stage Malaria

scholarly journals A Phase 1 study of the blood-stage malaria vaccine candidate AMA1-C1/Alhydrogel® with CPG 7909, using two different formulations and dosing intervals

Vaccine ◽  
2009 ◽  
Vol 27 (31) ◽  
pp. 4104-4109 ◽  
Author(s):  
Ruth D. Ellis ◽  
Gregory E.D. Mullen ◽  
Mark Pierce ◽  
Laura B. Martin ◽  
Kazutoyo Miura ◽  
...  
Keyword(s):  
Malaria Vaccine ◽  
Vaccine Candidate ◽  
Phase 1 ◽  
Blood Stage ◽  
Phase 1 Study ◽  
Malaria Vaccine Candidate ◽  
Dosing Intervals ◽  
Blood Stage Malaria

scholarly journals Bacterially Expressed Full-Length Recombinant Plasmodium falciparum RH5 Protein Binds Erythrocytes and Elicits Potent Strain-Transcending Parasite-Neutralizing Antibodies

2013 ◽  
Vol 82 (1) ◽  
pp. 152-164 ◽  
Author(s):  
K. Sony Reddy ◽  
Alok K. Pandey ◽  
Hina Singh ◽  
Tajali Sahar ◽  
Amlabu Emmanuel ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Neutralizing Antibodies ◽  
Malaria Vaccine ◽  
Expression System ◽  
Full Length ◽  
Blood Stage ◽  
Parasite Protein ◽  
Content Type ◽  
Erythrocyte Binding ◽  
Blood Stage Malaria

ABSTRACTPlasmodium falciparumreticulocyte binding-like homologous protein 5 (PfRH5) is an essential merozoite ligand that binds with its erythrocyte receptor, basigin. PfRH5 is an attractive malaria vaccine candidate, as it is expressed by a wide number ofP. falciparumstrains, cannot be genetically disrupted, and exhibits limited sequence polymorphisms. Viral vector-induced PfRH5 antibodies potently inhibited erythrocyte invasion. However, it has been a challenge to generate full-length recombinant PfRH5 in a bacterial-cell-based expression system. In this study, we have produced full-length recombinant PfRH5 inEscherichia colithat exhibits specific erythrocyte binding similar to that of the native PfRH5 parasite protein and also, importantly, elicits potent invasion-inhibitory antibodies against a number ofP. falciparumstrains. Antibasigin antibodies blocked the erythrocyte binding of both native and recombinant PfRH5, further confirming that they bind with basigin. We have thus successfully produced full-length PfRH5 as a functionally active erythrocyte binding recombinant protein with a conformational integrity that mimics that of the native parasite protein and elicits potent strain-transcending parasite-neutralizing antibodies.P. falciparumhas the capability to develop immune escape mechanisms, and thus, blood-stage malaria vaccines that target multiple antigens or pathways may prove to be highly efficacious. In this regard, antibody combinations targeting PfRH5 and other key merozoite antigens produced potent additive inhibition against multiple worldwideP. falciparumstrains. PfRH5 was immunogenic when immunized with other antigens, eliciting potent invasion-inhibitory antibody responses with no immune interference. Our results strongly support the development of PfRH5 as a component of a combination blood-stage malaria vaccine.

scholarly journals Blood Stage Malaria Vaccine Eliciting High Antigen-Specific Antibody Concentrations Confers No Protection to Young Children in Western Kenya

PLoS ONE ◽  
2009 ◽  
Vol 4 (3) ◽  
pp. e4708 ◽  
Author(s):  
Bernhards R. Ogutu ◽  
Odika J. Apollo ◽  
Denise McKinney ◽  
Willis Okoth ◽  
Joram Siangla ◽  
...  
Keyword(s):  
Young Children ◽  
Specific Antibody ◽  
Malaria Vaccine ◽  
Blood Stage ◽  
Western Kenya ◽  
Blood Stage Malaria

Evaluation of simian adenoviral vector AdCh63 expressing MSP-1 as a candidate blood-stage malaria vaccine

2009 ◽  
Vol 59 (6) ◽  
pp. S427-S428
Author(s):  
Anna Goodman ◽  
Sarah Gilbert ◽  
Stefano Colloca ◽  
Matthew Dicks ◽  
Adrian Hill ◽  
...  
Keyword(s):  
Adenoviral Vector ◽  
Malaria Vaccine ◽  
Blood Stage ◽  
Blood Stage Malaria

Blood-stage Challenge for Malaria Vaccine Efficacy Trials: A Pilot Study with Discussion of Safety and Potential Value

2008 ◽  
Vol 78 (6) ◽  
pp. 878-883 ◽  
Author(s):  
Frances Sanderson ◽  
Angela Hunt-Cooke ◽  
Philip Bejon ◽  
Laura Andrews ◽  
Alexander D. Douglas ◽  
...  
Keyword(s):  
Pilot Study ◽  
Vaccine Efficacy ◽  
Malaria Vaccine ◽  
Blood Stage ◽  
Potential Value ◽  
Efficacy Trials

scholarly journals Identification of a Potent Combination of Key Plasmodium falciparum Merozoite Antigens That Elicit Strain-Transcending Parasite-Neutralizing Antibodies

2012 ◽  
Vol 81 (2) ◽  
pp. 441-451 ◽  
Author(s):  
Alok K. Pandey ◽  
K. Sony Reddy ◽  
Tajali Sahar ◽  
Sonal Gupta ◽  
Hina Singh ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Neutralizing Antibodies ◽  
Malaria Vaccine ◽  
Vaccine Development ◽  
Blood Stage ◽  
Content Type ◽  
Receptor Blocking ◽  
Erythrocyte Invasion ◽  
Invasion Inhibition ◽  
Blood Stage Malaria

ABSTRACTBlood-stage malaria vaccines that target singlePlasmodium falciparumantigens involved in erythrocyte invasion have not induced optimal protection in field trials. Blood-stage malaria vaccine development has faced two major hurdles, antigenic polymorphisms and molecular redundancy, which have led to an inability to demonstrate potent, strain-transcending, invasion-inhibitory antibodies. Vaccines that target multiple invasion-related parasite proteins may inhibit erythrocyte invasion more efficiently. Our approach is to develop a receptor-blocking blood-stage vaccine againstP. falciparumthat targets the erythrocyte binding domains of multiple parasite adhesins, blocking their interaction with their receptors and thus inhibiting erythrocyte invasion. However, with numerous invasion ligands, the challenge is to identify combinations that elicit potent strain-transcending invasion inhibition. We evaluated the invasion-inhibitory activities of 20 different triple combinations of antibodies mixedin vitroagainst a diverse set of six key merozoite ligands, including the novel ligandsP. falciparumapical asparagine-rich protein (PfAARP), EBA-175 (PfF2),P. falciparumreticulocyte binding-like homologous protein 1 (PfRH1), PfRH2, PfRH4, andPlasmodiumthrombospondin apical merozoite protein (PTRAMP), which are localized in different apical organelles and are translocated to the merozoite surface at different time points during invasion. They bind erythrocytes with different specificities and are thus involved in distinct invasion pathways. The antibody combination of EBA-175 (PfF2), PfRH2, and PfAARP produced the most efficacious strain-transcending inhibition of erythrocyte invasion against diverseP. falciparumclones. This potent antigen combination was selected for coimmunization as a mixture that induced balanced antibody responses against each antigen and inhibited erythrocyte invasion efficiently. We have thus demonstrated a novel two-step screening approach to identify a potent antigen combination that elicits strong strain-transcending invasion inhibition, supporting its development as a receptor-blocking malaria vaccine.

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