NMR Investigation of Unstructured Malaria Surface Protein MSP2, Isoform 3D7

M. Zachrdla¹, J. Nováček¹, L. Žídek¹, V. Sklenář¹, R. S. Norton²

¹NCBR, Faculty of Science and CEITEC, Masaryk University, Kamenice 5, 62500 Brno, Czech Republic

² The Walter and Eliza Hall, Institute of Medical Research, 1G Royal Parade, Parkville 3050, Australia

324489@mail.muni.cz

Malaria is one of the most important infectious diseases resulting in two million deaths worldwide. Merozoite surface protein 2 (MSP2) belongs to potential malaria vaccine candidates. In this study, we focused on the MSP2 isoform 3D7. The aggregation and fibril formation propensities of 3D7 are lower than those of the other isoform FC27. The goal of the study is to describe structural differences between the isoforms. This task is complicated by the fact that both proteins are intrinsically disordered. Nuclear magnetic resonance (NMR) has been chosen as a method well suited to describe structural features of molecules lacking a well-defined structure. The first step of the study was assignment of NMR frequencies to individual atoms of the protein. In order to overcome a severe peak overlap, 5D non-uniformly sampled NMR experiments were employed. Frequencies of backbone atoms of all 217 non-proline residues were successfully assigned. The obtained data was used to calculate secondary structure propensity of the protein.