| Autor: |
Planson AG; Unité de RMN des Biomolécules, Institut Pasteur, Paris, France., Guijarro JI, Chaffotte AF |
| Jazyk: |
angličtina |
| Zdroj: |
PloS one [PLoS One] 2013; Vol. 8 (2), pp. e57086. Date of Electronic Publication: 2013 Feb 22. |
| DOI: |
10.1371/journal.pone.0057086 |
| Abstrakt: |
Malaria represents a major public health problem and an important cause of mortality and morbidity. The malaria parasites are becoming resistant to drugs used to treat the disease and still no efficient vaccine has been developed. One promising vaccine candidate is the merozoite surface protein 1 (MSP1), which has been extensively investigated as a vaccine target. The surface protein MSP1 plays an essential role in the erythrocyte invasion process and is an accessible target for the immune system. Antibodies to the carboxy-terminal region of the protein, named MSP119, can inhibit erythrocyte invasion and parasite growth. In order to develop an effective MSP119- based vaccine against malaria, production of an antigen that is recognized by protective antibodies is mandatory. To this aim, we propose a method to produce the disulfide-rich MSP119 in its native conformation based on its in vitro oxidative refolding. The native conformation of the renatured MSP119 is carefully established by immunochemical reactivity experiments, circular dichroism and NMR. MSP119 can successfully be refolded in vitro as an isolated protein or as a fusion with the maltose binding protein. The possibility to properly fold MSP119in vitro paves the way to new approaches for high titer production of native MSP119 using Escherichia coli as a host. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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