Analysis of polymorphic regions of Plasmodium vivax Duffy binding protein of Korean isolates

Abstract

The present study was designed to investigate polymorphism in Duffy binding protein (DBP) gene of Plasmodium vivax isolates of Korea. Thirty samples were obtained from P. vivax patients in Yonchon-gun, Kyonggi-do in 1998. The PCR products of the samples were subjected to sequencing and hybridization analyses of the regions II and IV of P. vivax DBP gene. Two genotypes, SK-1 and SK-2, were identified on the basis of amino acid substitution and deletion. The genotype of 10 isolates was SK-1 and that of 20 isolates was SK-2. Most of the predicted amino acids in the region II of DBP gene were conserved between the Korean isolates and Belem strain except for 4-5 amino acid substitutions. In the region IV of DBP, a 6-bp insert that was shown in the Sal-1 allele type was found in SK-1, and a 27-bp insert that was shown in the Papua New Guinea allele type was found in SK-2. In conclusion, the present findings suggest that two genotypes of P. vivax coexist in the endemic area of Korea.

Antibody Responses and Avidity of Naturally Acquired Anti-Plasmodium vivax Duffy Binding Protein (PvDBP) Antibodies in Individuals from an Area with Unstable Malaria Transmission

“…However, the presence of a highly polymorphic sequence [38][39][40] in this antigen interferes with its use in vaccine development. Therefore, understanding the nature of this polymorphism present in PvDBP-II among P. vivax isolates as well as an immunoepidemiological study on various populations with a different genetic background are key features for vaccine development.…”

Rapid Dissemination of Newly Introduced Plasmodium vivax Genotypes in South Korea

“…Our aim was to determine genetic diversity, which can show whether P. vivax malaria in Korea has become heterogeneous. Genetic studies of P. vivax malaria in Korea have been performed by using several parasitic proteins, including CSP, 17 Duffy-binding protein, 18 apical membrane antigen-1, 19 18S ribosomal RNA, 20 and MSP-1. 9 However, these studies focused on simple polymorphism analysis for each gene over a short period.…”

The crystal structure of P. knowlesi DBPα DBL domain and its implications for immune evasion

“…The space filling models show the dimorphic residues as green, polymorphic residues as yellow, residues of the predicted binding pocket for the receptor recognition as white, and residues known to change antigenic character and sensitivity to antibody inhibition in red (K171, W191). Dimorphic and polymorphic residues were determined as those that were dimorphic or polymorphic from Sal I DBP in at least two other strains [16][17][18][20][21][22]. The worm model depicts the amino acid backbone and highlights the alpha helices of the second and third domains.…”

“…Supporting evidence depicted selected polymorphic residues identified from P. vivax field isolates mapped onto the P. knowlesi DBPα DBL structure localized to knobby protrusions on the face of the molecule opposite from the proposed DARC recognition site. However, P. vivax DBL polymorphisms [16][17][18][20][21][22] are more extensive than those depicted in the Singh et al paper (Fig. 2), and are widely dispersed over the DBL domain.…”