Abstract
Vaccination trails have shown that a purified, 74 kDa glycoprotein, GP74, isolated from the host cell membrane of Plasmodium knowlesi-infected rhesus erythrocytes, can provide protective immunity against P. knowlesi malaria. We have extended this work by a tryptic peptide analysis of the disposition of GP74 in the host cell membrane. Of the 18 peptides characterized by high-performance liquid chromatography only four were accessible to lactoperoxidase-catalyzed radioiodination of non-leaky, schizont-infected host cells from the extracellular space. Metabolic labeling with radioactive glucosamine indicates that two of the surface exposed peptides are glycopeptides, and one of these, peptide 12, appears to carry a dominant antigenic site, according to its reactivity with immunoglobulin from sera of monkeys protected against P. knowlesis malaria.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
