scholarly journals Structure of the merozoite surface protein 1 from Plasmodium falciparum

2021 ◽  
Vol 7 (23) ◽  
pp. eabg0465
Author(s):  
Patricia M. Dijkman ◽  
Tanja Marzluf ◽  
Yingyi Zhang ◽  
Shih-Ying Scott Chang ◽  
Dominic Helm ◽  
...  
Keyword(s):  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Coiled Coils ◽  
Dependent Manner ◽  
Concentration Dependent Manner ◽  
Merozoite Surface Protein 1 ◽  
Dimerization Interface ◽  
Structural Insights ◽  
Promising Vaccine Candidate

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.

scholarly journals Fabrication of Oil-in-Water Emulsions with Whey Protein Isolate–Puerarin Composites: Environmental Stability and Interfacial Behavior

Foods ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 705
Author(s):  
Yejun Zhong ◽  
Jincheng Zhao ◽  
Taotao Dai ◽  
Jiangping Ye ◽  
Jianyong Wu ◽  
...  
Keyword(s):  
Interfacial Tension ◽  
Whey Protein ◽  
Surface Protein ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Environmental Stability ◽  
Dependent Manner ◽  
Emulsifying Properties ◽  
Interfacial Behavior ◽  
Concentration Dependent Manner

Protein–polyphenol interactions influence emulsifying properties in both directions. Puerarin (PUE) is an isoflavone that can promote the formation of heat-set gels with whey protein isolate (WPI) through hydrogen bonding. We examined whether PUE improves the emulsifying properties of WPI and the stabilities of the emulsions. We found that forming composites with PUE improves the emulsifying properties of WPI in a concentration-dependent manner. The optimal concentration is 0.5%, which is the highest PUE concentration that can be solubilized in water. The PUE not only decreased the droplet size of the emulsions, but also increased the surface charge by forming composites with the WPI. A 21 day storage test also showed that the maximum PUE concentration improved the emulsion stability the most. A PUE concentration of 0.5% improved the stability of the WPI emulsions against environmental stress, especially thermal treatment. Surface protein loads indicated more protein was adsorbed to the oil droplets, resulting in less interfacial WPI concentration due to an increase in specific surface areas. The use of PUE also decreased the interfacial tension of WPI at the oil–water interface. To conclude, PUE improves the emulsifying activity, storage, and environmental stability of WPI emulsions. This result might be related to the decreased interfacial tension of WPI–PUE composites.

scholarly journals Mosaic organization and heterogeneity in frequency of allelic recombination of the Plasmodium vivax merozoite surface protein-1 locus

2002 ◽  
Vol 99 (25) ◽  
pp. 16348-16353 ◽  
Author(s):  
C. Putaporntip ◽  
S. Jongwutiwes ◽  
N. Sakihama ◽  
M. U. Ferreira ◽  
W.-G. Kho ◽  
...  
Keyword(s):  
Plasmodium Vivax ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Merozoite Surface Protein 1
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