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Plasmodium vivax Duffy binding protein: a modular evolutionary proposal

Published online by Cambridge University Press:  16 April 2004

P. MARTINEZ
Affiliation:
Molecular Biology Department, Fundacion Instituto de Inmunologia de Colombia, Carrera 50#26-00, Bogota, Colombia Faculty of Science, Chemistry Department, Universidad Nacional de Colombia, Carrera 30, Calle 45, Bogota, Colombia
C. F. SUAREZ
Affiliation:
Molecular Biology Department, Fundacion Instituto de Inmunologia de Colombia, Carrera 50#26-00, Bogota, Colombia
P. P. CARDENAS
Affiliation:
Molecular Biology Department, Fundacion Instituto de Inmunologia de Colombia, Carrera 50#26-00, Bogota, Colombia Faculty of Science, Chemistry Department, Universidad Nacional de Colombia, Carrera 30, Calle 45, Bogota, Colombia
M. A. PATARROYO
Affiliation:
Molecular Biology Department, Fundacion Instituto de Inmunologia de Colombia, Carrera 50#26-00, Bogota, Colombia Faculty of Science, Chemistry Department, Universidad Nacional de Colombia, Carrera 30, Calle 45, Bogota, Colombia
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Abstract

The population of malaria-causing parasites is characterized by great genetic diversity. Knowledge of the polymorphism generation mechanism is a central issue for developing effective vaccines against malaria and understanding the parasite population structure. Plasmodium vivax genetic diversity has been explained in terms of two major factors: natural selection and intragenic recombination. A modular organization was found within P. vivax Duffy binding protein in the present work. Four Colombian isolates have identical sequences to Salvador-1 strain amongst dpb regions III–VI analysed, suggesting a high identity between Central and South American isolates. Geographically clustered sectors, corresponding to cysteine-rich regions (II and VI), show a high sequence diversity that could reflect a possible immune response evasion mechanism; both positive and negative selection were detected in these regions. In contrast, other dbp gene regions display a non-geographical clustering pattern, lower sequence diversity and predominant negative selective pressure. Recombination was homogeneously detected all along the molecule. These findings suggest that diversification vs. homogenizing forces, drive dbp gene evolution and determine its mosaic region organization.

Information

Type
Research Article
Copyright
© 2004 Cambridge University Press
Figure 0

Fig. 1. (A) Map of Colombia for studied locations. Shaded parts of the map represent the areas from which patients came who donated the infected blood samples; the black squares represent sample reception centres; stippled areas represent mountain ranges. (B) Plasmodium vivax dbp region structure. Grey represents cysteine-rich regions; numbers represent amino acid location, according to Fang's subdivision of regions (Fang et al. 1991).

Figure 1

Fig. 2. Colombian isolate DBP region III–VI amino acid alignment. Grey shading indicates specific high binding affinity peptides (1640 and 1642); bold represents co-variant residues with Korean and Papua New Guinean sequences; italics show insertion in COLns08 sample. Dots indicate conserved residues and dashes represent gaps introduced for alignment.

Figure 2

Fig. 3. Neighbour-Joining tree of amino acid sequences from Plasmodium vivax DBP regions (I–VI) from endemic populations based on pair-wise differences using P distance. The significance of the nodes was proved by Bootstrap calculated with 1000 replicates. The scale indicates 0·01 substitutions per site. (A) Tree for region I. (B) Region II. (C) Region III. (D) Region IV. (E) Region V. (F) Region VI. Colombia, COL; Norte de Santander, ns; Llanos Orientales, lla; Korea, KOR; Papua Nueva Guinea, PNG; Wosera, W; Madang, m.

Figure 3

Table 1. Diversity analysis of dbp gene

Figure 4

Table 2. Nei–Gojobori's and Tajimas's tests for dpb gene

Figure 5

Fig. 4. Conserved carboxyl cysteine-rich alignment of the erythrocyte binding proteins. The shading indicates levels of identity among sequences. White letters on a black background represent amino acid residues that were 100% identical; white letters on a grey background represent amino acid residues that were 80% identical; and black letters on a grey background represent amino acid residues that were 60% identical. Bold letters represent conserved physicochemical properties: Small, S; Polar, P; Hydrophobicity, H; Charged, C; Aromatic, A; P. vivax Duffy Binding Protein, PVDBP; Madang Papua New Guinea, PNGm; Colombia, COL; Norte de Santander, ns; Llanos Orientales, lla; erythrocyte binding protein, EBP; erythrocyte binding antigen, EBA; erythrocyte binding like, EBL; P. cynomolgy, Pc; P. knowlesi, Pk; P. vivax, Pv; P. falciparum, Pf; P. yoelii, Py; P. reichenowi, Pr; P. berghei, Pb; P. chabaudi, Pch; P. vinckei, Pvin. Dashes represent gaps introduced to maintain alignment.

Figure 6

Fig. 5. Kyte–Doolitle Hydropathy Plot of region VI (3 cys) for variant sequences from Papua New Guinea and Colombia. Score corresponds to normalized (to 1) values used in the computation. Position corresponds to amino acid numeration according to Sal-1 sequence (Fang et al. 1991).