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Clinical and Vaccine Immunology, March 2007, p. 320-322, Vol. 14, No. 3
1071-412X/07/$08.00+0 doi:10.1128/CVI.00424-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
,
Jae-Won Park,2
Hyeong-Woo Lee,3
Klin Lin,4
Seon-Hee Kim,1
Young-An Bae,1
Woon-Mok Sohn,5
Tong-Soo Kim,3 and
Yoon Kong1*
Department of Molecular Parasitology and Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea,1 Department of Microbiology, Gachon Medical School, Inchon 405-760, Korea,2 Division of Malaria and Parasitic Diseases, National Institute of Health, Korea Centers for Disease Control and Prevention, Seoul 122-701, Korea,3 Department of Medical Research (Upper Myanmar), Pying Oo Lwin Township, Mandalay, Myanmar,4 Department of Parasitology and Institute of Health Sciences, Gyeongsang National University College of Medicine, Jinju 660-751, Korea5
Received 15 November 2006/ Returned for modification 18 December 2006/ Accepted 9 January 2007
We have characterized Plasmodium vivax heat shock protein 70 (PvHSP70) and evaluated serodiagnostic applicability of recombinant PvHSP70 (rPvHSP70). In enzyme-linked immunosorbent assays and immunoblot analyses, rPvHSP70 showed high sensitivity (88.8%; 203/228 cases). P. falciparum-infected sera revealed positive reactions (78.8%). The predominant immunoglobulin G (IgG) subclasses were segregated with IgG1 and IgG3.
Supplemental material for this article may be found at http://cvi.asm.org/.
Published ahead of print on 17 January 2007.
Present address: Department of Parasitology and Institute of Health Sciences, Gyeongsang National University College of Medicine, Jinju 660-751, Korea.
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