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

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

Autor Jimenez, Maria Carolina S. Google Scholar
Ramos, Carlos Henrique I. Google Scholar
Barbosa, Joao Alexandre R. G. Google Scholar
Galinski, Mary R. Google Scholar
Barnwell, John W. Google Scholar
Rodrigues, Mauricio M. Autor UNIFESP Google Scholar
Soares, Irene S. Google Scholar
Instituição Universidade de São Paulo (USP)
Ctr Struct Mol Biol CeBiME
Universidade Estadual de Campinas (UNICAMP)
Emory Univ
Ctr Dis Control & Prevent
Universidade Federal de São Paulo (UNIFESP)
Resumo Plasmodium vivax Merozoite Surface Protein-3 alpha and 3 beta 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 alpha-helical secondary and coiled-coil tertiary structures. Seven recombinant proteins representing different regions of MSP-3 alpha and MSP-3 beta of P. vivax were generated to investigate their structure. Circular dichroism spectra analysis revealed that some proteins are folded with a high degree of alpha-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-3 alpha, 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. (C) 2008 Elsevier B.V. All rights reserved.
Assunto malaria
plasmodium vivax
merozoite surface protein-3
Idioma Inglês
Data 2008-07-01
Publicado em Biochimica Et Biophysica Acta-general Subjects. Amsterdam: Elsevier B.V., v. 1780, n. 7-8, p. 983-988, 2008.
ISSN 0304-4165 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 983-988
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000257309000006

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