Table 1.
Primer sequences and PCR conditions for isolation of poctrp, pocsp and pomsp1 genes.
Fig 1.
(A) Schematic representation of the domain structure of Plasmodium ctrp gene. The Plasmodium CTRP composes of N-terminal signal peptide, six vWA domain, seven tandemly arrayed TSP 1- like domains, and the C-terminal transmembrane domain. Based on P. falciparum CTRP domain structure analysis, the PoCTRP domains could be drawn from multiple sequence alignment. Amino acid sequence signature for each Plasmodium species were observed between vWA 1–2 domains and between vWA 2–3 domains as indicated by red arrows. (B) Amino acid alignment of the transmembrane (TM) domain with the box representing the conserved tyrosine-based motif involved in cellular trafficking. (C) Amino acid alignment of the cytoplasmic region. The conserved tryptophan residue that interacts with motility actomyosin machinery was marked with the box.
Fig 2.
Distribution of the major tandem repeat units in PoCTRP and PoCSP.
Fig 3.
Sliding window plot of nucleotide diversity.
Sliding plot with a window length of 100 bp and 25 bp step size using DnaSP v5 revealed nucleotide diversity between P. ovale wallikeri (Pi 1) and and P. ovale cursiti (Pi 2). The nucleotide diversity is calculated from ctrp (A), csp (B), and partial msp1 gene (C).
Table 2.
Nucleotide diversity and natural selection in P. ovale spp.
Table 3.
Sequence polymorphism in the conserved regions of P. ovale CSP.
Fig 4.
Phylogenetic analysis of P. ovale spp.
Phylogenetic tree inferred using the Neighbor-Joining method based on concatenated CTRP, CSP, and MSP1 proteins. The percentage of replicate trees in which the associated taxa clustered together in the bootstrap test (1,000 replicates) are shown next to the branches. The evolutionary distances were computed using the JTT matrix-based method and are in the units of the number of amino acid substitutions per site. Accession numbers of CTRP-CSP-MSP1 of each sample is shown in the bracket.