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The merozoite surface protein 1 complex Is a platform for binding to human erythrocytes by plasmodium falciparum

Plasmodium falciparum is the causative agent of the most severe form of malaria in humans. The merozoite, an extracellular stage of the parasite lifecycle, invades erythrocytes in which they develop. The most abundant protein on the surface of merozoites is merozoite surface protein 1 (MSP1), which...

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Main Authors: Lin, Clara S. (Author) , Uboldi, Alessandro D. (Author) , Marapana, Danushka (Author) , Czabotar, Peter E. (Author) , Epp, Christian (Author) , Bujard, Hermann (Author) , Taylor, Nicole L. (Author) , Perugini, Matthew A. (Author) , Hodder, Anthony N. (Author) , Cowman, Alan F. (Author)
Format: Article (Journal)
Language:English
Published: [September 12, 2014]
In: The journal of biological chemistry
Year: 2014, Volume: 289, Issue: 37, Pages: 25655-25669
ISSN:1083-351X
DOI:10.1074/jbc.M114.586495
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M114.586495
Verlag, lizenzpflichtig, Volltext: http://www.jbc.org/content/289/37/25655
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Author Notes:Clara S. Lin, Alessandro D. Uboldi, Danushka Marapana, Peter E. Czabotar, Christian Epp, Hermann Bujard, Nicole L. Taylor, Matthew A. Perugini, Anthony N. Hodder, and Alan F. Cowman
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Summary:Plasmodium falciparum is the causative agent of the most severe form of malaria in humans. The merozoite, an extracellular stage of the parasite lifecycle, invades erythrocytes in which they develop. The most abundant protein on the surface of merozoites is merozoite surface protein 1 (MSP1), which consists of four processed fragments. Studies indicate that MSP1 interacts with other peripheral merozoite surface proteins to form a large complex. Successful invasion of merozoites into host erythrocytes is dependent on this protein complex; however, the identity of all components and its function remain largely unknown. We have shown that the peripheral merozoite surface proteins MSPDBL1 and MSPDBL2 are part of the large MSP1 complex. Using surface plasmon resonance, we determined the binding affinities of MSPDBL1 and MSPDBL2 to MSP1 to be in the range of 2-4 × 10−7 m. Both proteins bound to three of the four proteolytically cleaved fragments of MSP1 (p42, p38, and p83). In addition, MSPDBL1 and MSPDBL2, but not MSP1, bound directly to human erythrocytes. This demonstrates that the MSP1 complex acts as a platform for display of MSPDBL1 and MSPDBL2 on the merozoite surface for binding to receptors on the erythrocyte and invasion.
Item Description:Gesehen am 03.09.2020
Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.M114.586495

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