The Plasmodium vivax homolog of the ookinete adhesive micronemal protein, CTRP

• DOI: 10.1016/j.parint.2006.04.003
• Publication Date: 2006-07-07T14:43:11Z
• Authors: Osamu Kaneko; Thomas J. Templeton; Hideyuki Iriko; Mayumi Tachibana; Hitoshi Otsuki; Satoru Takeo; Jetsumon Sattabon...; Motomi Torii; Takafumi Tsuboi
• Keywords: Life Cycle Stages; Base Sequence; Amino Acid Motifs; Molecular Sequence Data; Protozoan Proteins; Plasmodium gallinaceum; Receptors, Cell Surface; Plasmodium yoelii; Protein Structure, Tertiary; 3. Good health; 03 medical and health sciences; 0302 clinical medicine; Animals; Amino Acid Sequence; Plasmodium vivax; Sequence Alignment

The Plasmodium circumsporozoite protein/thrombospondin-related anonymous protein-related protein (CTRP) is expressed at the mosquito midgut ookinete stage and is considered to be a transmission-blocking vaccine candidate. CTRP is composed of multiple von Willebrand factor A (vWA) and thrombospondin type 1 domains in the extracellular portion of the molecule, and a short acidic cytoplasmic domain that interacts with the actomyosin machinery. As a means to predict functionally relevant domains within CTRP we determined the nucleotide sequences of CTRP from the Plasmodium vivax Sall and the Plasmodium yoelii 17XL strains and characterized the conservation of domain architectures and motifs across Plasmodium genera. Sequence alignments indicate that the CTRP 1st to 4th vWA domains exhibit greater conservation, and thereby are perhaps functionally more important than the 5th and 6th domains. This point should be considered for the development of a transmission-blocking vaccine that includes CTRP recombinant subunit. To complement previous cellular studies on CTRP, we further determined the expression and cellular localization of CTRP protein in P. vivax and P. yoelii.