Faculty Opinions recommendation of Screening and hit evaluation of a chemical library against blood-stage Plasmodium falciparum.

2016 ◽  
Author(s):  
Audrey Odom John
Keyword(s):  
Plasmodium Falciparum ◽  
Blood Stage ◽  
Chemical Library

scholarly journals Screening and hit evaluation of a chemical library against blood-stage Plasmodium falciparum

2014 ◽  
Vol 13 (1) ◽  
pp. 190 ◽  
Author(s):  
Vicky M Avery ◽  
Sridevi Bashyam ◽  
Jeremy N Burrows ◽  
Sandra Duffy ◽  
George Papadatos ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Blood Stage ◽  
Chemical Library

scholarly journals The Structure of the Cysteine-Rich Domain of Plasmodium falciparum P113 Identifies the Location of the RH5 Binding Site

mBio ◽  
2020 ◽  
Vol 11 (5) ◽  
Author(s):  
Ivan Campeotto ◽  
Francis Galaway ◽  
Shahid Mehmood ◽  
Lea K. Barfod ◽  
Doris Quinkert ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Binding Site ◽  
Structural Information ◽  
Blood Stage ◽  
Site Directed Mutagenesis ◽  
Effective Vaccine ◽  
Binding Region ◽  
Fab Fragment ◽  
Content Type ◽  
Blood Stage Malaria

ABSTRACT Plasmodium falciparum RH5 is a secreted parasite ligand that is essential for erythrocyte invasion through direct interaction with the host erythrocyte receptor basigin. RH5 forms a tripartite complex with two other secreted parasite proteins, CyRPA and RIPR, and is tethered to the surface of the parasite through membrane-anchored P113. Antibodies against RH5, CyRPA, and RIPR can inhibit parasite invasion, suggesting that vaccines containing these three components have the potential to prevent blood-stage malaria. To further explore the role of the P113-RH5 interaction, we selected monoclonal antibodies against P113 that were either inhibitory or noninhibitory for RH5 binding. Using a Fab fragment as a crystallization chaperone, we determined the crystal structure of the RH5 binding region of P113 and showed that it is composed of two domains with structural similarities to rhamnose-binding lectins. We identified the RH5 binding site on P113 by using a combination of hydrogen-deuterium exchange mass spectrometry and site-directed mutagenesis. We found that a monoclonal antibody to P113 that bound to this interface and inhibited the RH5-P113 interaction did not inhibit parasite blood-stage growth. These findings provide further structural information on the protein interactions of RH5 and will be helpful in guiding the development of blood-stage malaria vaccines that target RH5. IMPORTANCE Malaria is a deadly infectious disease primarily caused by the parasite Plasmodium falciparum. It remains a major global health problem, and there is no highly effective vaccine. A parasite protein called RH5 is centrally involved in the invasion of host red blood cells, making it—and the other parasite proteins it interacts with—promising vaccine targets. We recently identified a protein called P113 that binds RH5, suggesting that it anchors RH5 to the parasite surface. In this paper, we use structural biology to locate and characterize the RH5 binding region on P113. These findings will be important to guide the development of new antimalarial vaccines to ultimately prevent this disease, which affects some of the poorest people on the planet.

Safety, tolerability, pharmacokinetics, and antimalarial efficacy of a novel Plasmodium falciparum ATP4 inhibitor SJ733: a first-in-human and induced blood-stage malaria phase 1a/b trial

2020 ◽  
Vol 20 (8) ◽  
pp. 964-975 ◽  
Author(s):  
Aditya H Gaur ◽  
James S McCarthy ◽  
John C Panetta ◽  
Ronald H Dallas ◽  
John Woodford ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Blood Stage ◽  
Blood Stage Malaria

scholarly journals Immunization of Aotus monkeys with Plasmodium falciparum blood-stage recombinant proteins.

1990 ◽  
Vol 87 (10) ◽  
pp. 4017-4021 ◽  
Author(s):  
S. Herrera ◽  
M. A. Herrera ◽  
B. L. Perlaza ◽  
Y. Burki ◽  
P. Caspers ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Recombinant Proteins ◽  
Blood Stage

The Blood-stage Dynamics of Mixed Plasmodium malariae–Plasmodium falciparum Infections

1999 ◽  
Vol 198 (4) ◽  
pp. 549-566 ◽  
Author(s):  
Daniel P Mason ◽  
F.Ellis McKenzie ◽  
William H Bossert
Keyword(s):  
Plasmodium Falciparum ◽  
Plasmodium Malariae ◽  
Blood Stage

A Plasmodium falciparum malaria vaccine candidate which contains epitopes from the circumsporozoite protein and a blood stage antigen, 5.1

1991 ◽  
Vol 47 (2) ◽  
pp. 143-150 ◽  
Author(s):  
Patrick Caspers ◽  
Howard Etlinger ◽  
Hugues Matile ◽  
J.Richard Pink ◽  
Dietrich Stüber ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Falciparum Malaria ◽  
Malaria Vaccine ◽  
Vaccine Candidate ◽  
Plasmodium Falciparum Malaria ◽  
Circumsporozoite Protein ◽  
Blood Stage ◽  
Malaria Vaccine Candidate

scholarly journals Serum factors inhibitory for in vitro development of Plasmodium falciparum blood-stage parasites

1994 ◽  
Vol 89 (suppl 2) ◽  
pp. 17-21
Author(s):  
Blanca L. Perlaza ◽  
Cecilia de Plata ◽  
Constanza Zapata ◽  
Jaime A. Ramírez ◽  
Socrates Herrera
Keyword(s):  
Plasmodium Falciparum ◽  
Blood Stage ◽  
Serum Factors ◽  
In Vitro Development ◽  
Vitro Development
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