Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/348847
Type: Artigo
Title: Biophysical characterization of the recombinant merozoite surface protein-3 of Plasmodium vivax
Author: Jimenez, Maria Carolina S.
Ramos, Carlos Henrique I.
Barbosa, Joao Alexandre R. G.
Galinski, Mary R.
Barnwell, John W.
Rodrigues, Mauricio M.
Soares, Irene S.
Abstract: 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
Subject: Malaria
Plasmodium vivax
Country: Países Baixos
Editor: Elsevier
Rights: Fechado
Identifier DOI: 10.1016/j.bbagen.2008.03.016
Address: https://www.sciencedirect.com/science/article/pii/S0304416508000822
Date Issue: 2008
Appears in Collections:IB - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
000257309000006.pdf856.45 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.