Proteolysis of Plasmodium falciparum surface antigen, Pfs230, during gametogenesis.

By S. Brooks, K. Williamson. 2000

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Structural and Immunological Characterization of Recombinant 6-Cysteine Domains of the Plasmodium falciparum Sexual Stage Protein Pfs230* (2016, background): “Pfs230 is initially a 360-kDa gametocyte surface protein that is proteolytically processed during development at the amino terminus (18).”
Analysis of the Plasmodium falciparum proteome by high-accuracy mass spectrometry (2002, methodology): “For the production of gametes, purified gametocytes were pelleted and incubated in G m buffer containing 100 µM xanthurenic acid for a period of 3 h at 21 °C (ref”
Worldwide sequence conservation of transmission-blocking vaccine candidate Pvs230 in Plasmodium vivax (2011, background): “The boundary of IVP and ICP does not coincide with the putative cleavage sites proposed for Pfs230 [56], which reside in a C-terminal part of IVP.”
The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle (2016, background): “…P230 undergoes two independent proteolytic cleavage events at the N-terminus, at sites N-terminal to the first s48/45 domain, resulting in two processed versions of the protein (300 and 307 kDa) that remain associated with the gamete (Williamson et al., 1996; Brooks and Williamson, 2000).”