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PHD : Parasites, Hosts and Diseases

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Original Article

Proteomic Analysis of Haptoglobin and Amyloid A Protein Levels in Patients with Vivax Malaria

The Korean Journal of Parasitology 2010;48(3):203-211.
Published online: September 16, 2010

1Department of Integrated OMICS for Biomedical Sciences, Graduate School, Yonsei University, Seoul 120-749, Korea.

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• Received: July 1, 2010   • Revised: August 31, 2010   • Accepted: August 31, 2010

Copyright © 2010 by The Korean Society for Parasitology

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Proteomic Analysis of Haptoglobin and Amyloid A Protein Levels in Patients with Vivax Malaria
Korean J Parasitol. 2010;48(3):203-211.   Published online September 16, 2010
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Proteomic Analysis of Haptoglobin and Amyloid A Protein Levels in Patients with Vivax Malaria
Korean J Parasitol. 2010;48(3):203-211.   Published online September 16, 2010
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Proteomic Analysis of Haptoglobin and Amyloid A Protein Levels in Patients with Vivax Malaria
Image Image Image Image Image Image
Fig. 1 Comparison of 2-DE maps of whole plasma from normal healthy donors in different experimental conditions. Plasma samples obtained from healthy normal individuals were analyzed by 2-DE as described in Materials and Methods. For these maps, 100 µg (pH range of 3-10), 150 µg (4-7), 200 µg (4.5-5.5) and 200 µg (5.5-6.7) of whole plasma proteins were applied by in-gel rehydration and to different IPG strips, pH ranges of 3-10 (nonlinear), 4-7, 4.5-5.5, and 5.5-6.7. For separation in the second dimension, 9-12% gradient SDS-PAGE was used. Three or more independent runs of each plasma sample were analyzed for each condition. The gels were visualized by silver nitrate staining.
Fig. 2 Comparison of 2-DE maps of plasma proteins from a normal healthy donor after depleting abundant plasma proteins. For these maps, 100 µg (pH range 3-10), 150 µg (4-7), 200 µg (4.5-5.5) and 200 µg (5.5-6.7) of plasma proteins were applied by in-gel rehydration to IPG strips after depleting 2, 6, or 20 abundant proteins in plasma using the ProteoExtract™ Albumin/IgG Removal kit, the multiple affinity removal column system (MARS®), or the ProteoPrep™ 20 column, respectively. For separation in the second dimension, 9-12% gradient SDS-PAGE was used. A, crude plasma sample; B, plasma sample after depleting 2 abundant proteins; C, plasma sample after depleting 6 abundant proteins; D, plasma sample after depleting 20 abundant proteins. The gels were visualized by silver staining and analyzed by the Melanie II program.
Fig. 3 Comparison of the 2-DE maps of the plasma proteins from a healthy donor and a patient with vivax malaria. One hundred micrograms of whole plasma from a normal healthy individual (A) or a patient with vivax malaria (B) were separated on 2-DE gel electrophoresis with IPG strip on the pH range of 3-10 (nonlinear) and by 9-12% SDS-PAGE in the second dimension, respectively. The gels were stained by silver nitrate. Regions 1, 2, and 3 indicate β-chain, α-chain, and truncated α-chain proteins of haptoglobin, respectively, which were found to be significantly and consistently different between the plasma from patients with vivax malaria and normal healthy individuals.
Fig. 4 Magnified regions of the differentially-expressed haptoglobin in plasma from the normal healthy individuals and patients with vivax malaria. Each set shows gel regions 2 and 1 representing the α-chain and β-chain of haptoglobin, respectively. Normal regions 1 to 4 are show the magnified regions on each 2-DE gel with the plasmas from 4 healthy donors and 4 patients with vivax malaria. Arrows indicate the differentially expressed haptoglobin spots (A, α-chain of haptoglobin; B, β-chain of haptoglobin).
Fig. 5 Magnified regions of the differentially expressed SAA protein spots on each 2-DE gel. Circled spots were identified as SAA proteins analyzed with 2-DE, SDS-PAGE and MALDI-TOF MS followed by identification with the search engine programs ProFound and Mascot. Normal denotes the plasma from a healthy donor and patients 1-5 denotes the plasma from 5 patients with vivax malaria.
Fig. 6 SAA protein in the plasma of vivax malaria patients detected by chemiluminescence. Lane 1-44, vivax patients; N1-4, normal healthy group. For immunoblot analysis, equal amounts (30 µg) of whole plasmas from individuals were analyzed with a commercially available anti-SAA polyclonal antibody followed by a goat antirabbit secondary antibody coupled to horseradish peroxidase. The immunoreactive proteins on the membrane were detected by chemilluminescence using the West-Save™ substrate onto X-ray film.
Proteomic Analysis of Haptoglobin and Amyloid A Protein Levels in Patients with Vivax Malaria