scholarly journals PS4 Gene gun-based co-immunization of merozoite surface protein-1 cDNA with IL-12 expression plasmid confers protection against lethal malaria infection(Role of cytokine networks in parasite-infected hosts)

2001 ◽  
Vol 52 (Supplement) ◽  
pp. 76
Author(s):  
Tohru SAKAI ◽  
Kunisuke HIMENO
2004 ◽  
Vol 72 (10) ◽  
pp. 6172-6175 ◽  
Author(s):  
Lina Wang ◽  
Matthew W. Goschnick ◽  
Ross L. Coppel

ABSTRACT Oral immunization of mice with Escherichia coli-expressed Plasmodium yoelii merozoite surface protein 4/5 or the C-terminal 19-kDa fragment of merozoite surface protein 1 induced systemic antibody responses and protected mice against lethal malaria infection. A combination of these two proteins administered orally conferred improved protection compared to that conferred by either protein administered alone.


2001 ◽  
Vol 69 (2) ◽  
pp. 1207-1211 ◽  
Author(s):  
David R. Cavanagh ◽  
Carlota Dobaño ◽  
Ibrahim M. Elhassan ◽  
Kevin Marsh ◽  
Ahmed Elhassan ◽  
...  

ABSTRACT Comparisons of immunoglobulin G (IgG) subclass responses to the major polymorphic region and to a conserved region of MSP-1 in three cohorts of African villagers exposed to Plasmodium falciparum revealed that responses to Block 2 are predominantly IgG3 whereas antibodies to MSP-119 are mainly IgG1. The striking dominance of IgG3 to Block 2 may explain the short duration of this response and also the requirement for continuous stimulation by malaria infection to maintain clinical immunity.


2021 ◽  
Vol 7 (23) ◽  
pp. eabg0465
Author(s):  
Patricia M. Dijkman ◽  
Tanja Marzluf ◽  
Yingyi Zhang ◽  
Shih-Ying Scott Chang ◽  
Dominic Helm ◽  
...  

The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading Plasmodium merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in Plasmodium infection and immunity.


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