Biophysical characterization of the recombinant merozoite surface protein-3 of Plasmodium vivax

• Published in: Biochimica et biophysica acta 2008-07, Vol.1780 (7), p.983-988
• Main Authors: Jimenez, Maria Carolina S., Ramos, Carlos Henrique I., Barbosa, João Alexandre R.G., Galinski, Mary R., Barnwell, John W., Rodrigues, Mauricio M., Soares, Irene S.
• Format: Article
• Language: English
• Subjects: Alanine - chemistry; Animals; Antigens, Protozoan - chemistry; Antigens, Protozoan - genetics; Antigens, Protozoan - immunology; Antigens, Protozoan - metabolism; Biophysics - methods; Circular Dichroism; Malaria; Merozoite surface protein-3; Plasmids; Plasmodium vivax; Plasmodium vivax - chemistry; Plasmodium vivax - genetics; Protein Structure, Secondary; Protein Structure, Tertiary; Protozoan Proteins - chemistry; Protozoan Proteins - genetics; Protozoan Proteins - immunology; Protozoan Proteins - metabolism; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - isolation & purification; Recombinant Fusion Proteins - metabolism
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2008.03.016

Plasmodium vivax Merozoite Surface Protein-3α and 3β are members of a family of related merozoite surface proteins that contain a central alanine-rich domain with heptad repeats that is predicted to form α-helical secondary and coiled-coil tertiary structures. Seven recombinant proteins representing different regions of MSP-3α and MSP-3β of P. vivax were generated to investigate their structure . Circular dichroism spectra analysis revealed that some proteins are folded with a high degree of α-helices as secondary structure, whereas other products contain a high content of random coil. Using size exclusion chromatography, we found that the two smaller fragments of the MSP-3α, named CC4 and CC5, predicted to form coiled-coil (CC) structures, eluted at volumes corresponding to molecular weights larger than their monomeric masses. This result suggests that both proteins are oligomeric molecules. Analytical ultracentrifugation experiments showed that the CC5 oligomers are elongated molecules. Together, these data may help to understand important aspects of P. vivax biology.