Sequence polymorphisms of Plasmodium vivax tryptophan and alanine rich antigen (PvTARAg55)

Jin Woo Jang, Seung Gyu Yun, Mi Kyung Woo, Eun Taek Han, Feng Lu, Qi Gao, Soo-Young Yoon, Seong Soo A An, Chae Seung Lim

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Since PvTARAg55 protein (. PvTARAg55) of Plasmodium vivax (. P. vivax) is expressed during the parasite's sporozoite stage, it was strongly suggested, as a potential candidate for the development of a vaccine against malaria. PvTARAg55 polymorphisms were examined among isolates from various locations in Asian countries mainly; thus the current study could set the valuable baseline data for the development of a vaccine and clinical trials. A total of 59 samples were collected from Asian countries and one isolate from Africa. PvTARAg55 gene from 59 isolates was amplified, sequenced, and analyzed. PvTARAg55 contained a highly conserved tryptophan-rich domain (TRD) and a variable alanine-rich domain (ARD). In comparison to the Sal-1 strain, 10 allelic types of PvTARAg55 were found among 59 isolates. The main observed variations were the insertions and deletions of repeated sequences in the Ala-rich domain. Four types of GGVAAAP repeats were found at codon 324. Interestingly, GGVAAAP was found to be majority of Sal-1 type in the world. Two repeats (x2) were found in isolates from Korea, China, and India. Type of total deletion of GGVAAAP and three repeat (x3) were found from Indonesia isolates. Furthermore, "second insertion repeats" - with one or two repeats - were found with AFGAPSGFAPRP amino acid sequences at codon 338. Two repeats (x2) of AFGAPSGFAPRP were found in Indonesia, and PNG isolates. Finally, a "third repeat" was present with TTVNPEA amino acid sequences at codon 429 (the Indonesian isolates had three TTVNPEA sequences at that position). Isolates from ROK revealed "conserved sequences" in tryptophan-rich domain of PvTARAg55 with single amino acid substitutions (M180I). Hence, the extensive antigenic diversity of PvTARAg55 should be taken in account during the vaccine development.

Original languageEnglish
Pages (from-to)122-126
Number of pages5
JournalActa Tropica
Volume142
DOIs
Publication statusPublished - 2015 Feb 1

Fingerprint

Plasmodium vivax
vaccine development
codons
Codon
Tryptophan
Alanine
tryptophan
alanine
Indonesia
genetic polymorphism
antigens
Antigens
Amino Acid Sequence
Vaccines
amino acid sequences
Malaria Vaccines
Antigenic Variation
antigenic variation
Sporozoites
conserved sequences

ASJC Scopus subject areas

  • Parasitology
  • Infectious Diseases

Cite this

Sequence polymorphisms of Plasmodium vivax tryptophan and alanine rich antigen (PvTARAg55). / Jang, Jin Woo; Yun, Seung Gyu; Woo, Mi Kyung; Han, Eun Taek; Lu, Feng; Gao, Qi; Yoon, Soo-Young; An, Seong Soo A; Lim, Chae Seung.

In: Acta Tropica, Vol. 142, 01.02.2015, p. 122-126.

Research output: Contribution to journalArticle

Jang, Jin Woo ; Yun, Seung Gyu ; Woo, Mi Kyung ; Han, Eun Taek ; Lu, Feng ; Gao, Qi ; Yoon, Soo-Young ; An, Seong Soo A ; Lim, Chae Seung. / Sequence polymorphisms of Plasmodium vivax tryptophan and alanine rich antigen (PvTARAg55). In: Acta Tropica. 2015 ; Vol. 142. pp. 122-126.
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AU - Jang, Jin Woo

AU - Yun, Seung Gyu

AU - Woo, Mi Kyung

AU - Han, Eun Taek

AU - Lu, Feng

AU - Gao, Qi

AU - Yoon, Soo-Young

AU - An, Seong Soo A

AU - Lim, Chae Seung

PY - 2015/2/1

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AB - Since PvTARAg55 protein (. PvTARAg55) of Plasmodium vivax (. P. vivax) is expressed during the parasite's sporozoite stage, it was strongly suggested, as a potential candidate for the development of a vaccine against malaria. PvTARAg55 polymorphisms were examined among isolates from various locations in Asian countries mainly; thus the current study could set the valuable baseline data for the development of a vaccine and clinical trials. A total of 59 samples were collected from Asian countries and one isolate from Africa. PvTARAg55 gene from 59 isolates was amplified, sequenced, and analyzed. PvTARAg55 contained a highly conserved tryptophan-rich domain (TRD) and a variable alanine-rich domain (ARD). In comparison to the Sal-1 strain, 10 allelic types of PvTARAg55 were found among 59 isolates. The main observed variations were the insertions and deletions of repeated sequences in the Ala-rich domain. Four types of GGVAAAP repeats were found at codon 324. Interestingly, GGVAAAP was found to be majority of Sal-1 type in the world. Two repeats (x2) were found in isolates from Korea, China, and India. Type of total deletion of GGVAAAP and three repeat (x3) were found from Indonesia isolates. Furthermore, "second insertion repeats" - with one or two repeats - were found with AFGAPSGFAPRP amino acid sequences at codon 338. Two repeats (x2) of AFGAPSGFAPRP were found in Indonesia, and PNG isolates. Finally, a "third repeat" was present with TTVNPEA amino acid sequences at codon 429 (the Indonesian isolates had three TTVNPEA sequences at that position). Isolates from ROK revealed "conserved sequences" in tryptophan-rich domain of PvTARAg55 with single amino acid substitutions (M180I). Hence, the extensive antigenic diversity of PvTARAg55 should be taken in account during the vaccine development.

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