Identification of a novel antigenic domain of Plasmodium falciparum merozoite surface protein-1 that specifically binds to human erythrocytes and inhibits parasite invasion, in vitro

2000 ◽  
Vol 108 (1) ◽  
pp. 79-91 ◽  
Author(s):  
David-P Nikodem ◽  
Eugene-A Davidson
Keyword(s):  
Plasmodium Falciparum ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Human Erythrocytes ◽  
Parasite Invasion ◽  
Merozoite Surface Protein 1 ◽  
Falciparum Merozoite ◽  
Antigenic Domain

Protein–protein interaction studies reveal the Plasmodium falciparum merozoite surface protein-1 region involved in a complex formation that binds to human erythrocytes

2018 ◽  
Vol 475 (6) ◽  
pp. 1197-1209 ◽  
Author(s):  
Gourab Paul ◽  
Arunaditya Deshmukh ◽  
Bishwanath Kumar Chourasia ◽  
Md Kalamuddin ◽  
Ashutosh Panda ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Recombinant Proteins ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Human Erythrocytes ◽  
Proteolytic Processing ◽  
Protein Protein Interaction ◽  
Falciparum Merozoite ◽  
Vaccine Candidate Antigen ◽  
Serological Studies

Plasmodium falciparum merozoite surface protein (PfMSP) 1 has been studied extensively as a vaccine candidate antigen. PfMSP-1 undergoes proteolytic processing into four major products, such as p83, p30, p38, and p42, that are associated in the form of non-covalent complex(s) with other MSPs. To delineate MSP1 regions involved in the interaction with other MSPs, here we expressed recombinant proteins (PfMSP-165) encompassing part of p38 and p42 regions and PfMSP-119. PfMSP-165 interacted strongly with PfMSP-3, PfMSP-6, PfMSP-7, and PfMSP-9, whereas PfMSP-119 did not interact with any of these proteins. Since MSP-1 complex binds human erythrocytes, we examined the ability of these proteins to bind human erythrocyte. Among the proteins of MSP-1 complex, PfMSP-6 and PfMSP-9 bound to human erythrocytes. Serological studies showed that PfMSP-165 was frequently recognized by sera from malaria endemic regions, whereas this was not the case for PfMSP-119. In contrast, antibodies against PfMSP-119 showed much higher inhibition of merozoite invasion compared with antibodies against the larger PfMSP-165 fragment. Importantly, anti-PfMSP-119 antibodies recognized both recombinant proteins, PfMSP-119 and PfMSP-165; however, anti-PfMSP-165 antibody failed to recognize the PfMSP-119 protein. Taken together, these results demonstrate that PfMSP-1 sequences upstream of the 19 kDa C-terminal region are involved in molecular interactions with other MSPs, and these sequences may probably serve as a smoke screen to evade antibody response to the membrane-bound C-terminal 19 kDa region.

Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1 1 1Edited by P. E. Wright

1999 ◽  
Vol 289 (1) ◽  
pp. 113-122 ◽  
Author(s):  
William D. Morgan ◽  
Berry Birdsall ◽  
Thomas A. Frenkiel ◽  
Michael G. Gradwell ◽  
Petra A. Burghaus ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Solution Structure ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Merozoite Surface Protein 1 ◽  
Falciparum Merozoite
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