Jamaree Bhisutthibhan

University of Michigan–Ann Arbor

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Steven R. Meshnick

University of North Carolina at Chapel Hill

Daniel J. Walker

University of Tennessee at Knoxville

Chariya R. Brockelman

Bangkok University

Paul A. Hossler

University of Michigan–Ann Arbor

John B. Dame

University of Florida

Madalitso Tembo

University of Zambia

Charles A. Yowell

University of Florida

Steven R. Meshnick

University of North Carolina at Chapel Hill

Jane M. Carlton

New York University

Masanori Aikawa

Brigham and Women's Hospital

Cooperative Institutions

University of Michigan–Ann Arbor

Johns Hopkins University

University of Melbourne

Queen Elizabeth Central Hospital

University of North Carolina at Chapel Hill

Malawi-Liverpool-Wellcome Trust Clinical Research Programme

University of Liverpool

University of Malawi

Johns Hopkins Medicine

Mahidol University

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Immune mimicry in malaria:Plasmodium falciparumsecretes a functional histamine-releasing factor homologin vitroandin vivo

Proceedings of the National Academy of Sciences (2001)

Susan M. MacDonald Jamaree Bhisutthibhan Theresa A. Shapiro Stephen J. Rogerson Terrie E. Taylor

The Plasmodium falciparum translationally controlled tumor protein (TCTP) is a homolog of the mammalian histamine-releasing factor (HRF), which causes histamine release from human basophils and IL-8 secretion from eosinophils. Histamine, IL-8, and eosinophils have been reported to be elevated in patients with malaria. This study was undertaken to determine whether malarial TCTP is found in the plasma of malaria-infected patients and to determine whether it has HRF biologic activity. Malarial TCTP was found in lightly infected human volunteers and in heavily infected Malawian children, but not in uninfected patients. Recombinant malarial TCTP, like HRF, stimulated histamine release from basophils and IL-8 secretion from eosinophils in vitro . Whereas malarial TCTP was less active than HRF, the concentrations that were effective in vitro could be achievable in vivo . These data suggest that malarial TCTP, present in human plasma during a malarial illness, may affect host immune responses in vivo .

10.1073/pnas.201191498

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Citations (131)

Effects of thalassaemic serum on the in vitro development of the malarial parasitePlasmodium falciparum

Zeitschrift für Parasitenkunde Parasitology Research (1989)

Benjamas Thanomsub Suthat Fucharoen Chariya R. Brockelman Jamaree Bhisutthibhan

10.1007/bf00931278

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Citations (2)

The Plasmodium falciparum Translationally Controlled Tumor Protein Homolog and Its Reaction with the Antimalarial Drug Artemisinin

Journal of Biological Chemistry (1998)

Jamaree Bhisutthibhan Xing-Qing Pan Paul A. Hossler Daniel J. Walker Charles A. Yowell

Artemisinin and its derivatives are important new antimalarial drugs. When Plasmodium falciparum-infected erythrocytes are incubated with [10-³H]dihydroartemisinin, several malaria-specific proteins become labeled. One of these proteins is the P. falciparum translationally controlled tumor protein (TCTP) homolog. In vitro, dihydroartemisinin reacts covalently with recombinant TCTP in the presence of hemin. The association between drug and protein increases with increasing drug concentration, plateauing at approximately 1 drug/TCTP molecule. By Scatchard analysis, there appear to be 2 hemin binding sites on TCTP with dissociation constants of ∼18 μm. When the single cysteine moiety is blocked by pretreatment with iodoacetamide, hemin binding is not affected, whereas drug binding is reduced by two-thirds. Thus, TCTP reacts with artemisinin in situ and in vitro in the presence of hemin and appears to bind to hemin. The function of the malarial TCTP and the role of this reaction in the mechanism of action of artemisinin await elucidation.

Hemin

Dihydroartemisinin

10.1074/jbc.273.26.16192

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Citations (255)

Functional studies of the Plasmodium falciparum translationally controlled tumor protein.

Jamaree Bhisutthibhan

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The Plasmodium falciparum translationally controlled tumor protein: subcellular localization and calcium binding

European Journal of Cell Biology (1999)

Jamaree Bhisutthibhan Martin A. Philbert Hisashi Fujioka Masanori Aikawa Steven R. Meshnick

Immunoelectron microscopy

10.1016/s0171-9335(99)80052-1

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Citations (41)

Functional studies of the Plasmodium falciparum translationally controlled tumor protein.

Deep Blue (University of Michigan) (2000)

Jamaree Bhisutthibhan

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Immunoprecipitation of [ ³ H]Dihydroartemisinin Translationally Controlled Tumor Protein (TCTP) Adducts from Plasmodium falciparum -Infected Erythrocytes by Using Anti-TCTP Antibodies

Antimicrobial Agents and Chemotherapy (2001)

Jamaree Bhisutthibhan Steven R. Meshnick

ABSTRACT Artemisinin and its derivatives are endoperoxide-containing antimalarial drugs that appear to form adducts in situ with the Plasmodium falciparum translationally controlled tumor protein (TCTP) homolog. Immunoprecipitation with antibody to recombinant TCTP suggests that adducts may form with both monomeric and dimeric TCTP.

Immunoprecipitation

Dihydroartemisinin

10.1128/aac.45.8.2397-2399.2001

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Mechanisms of Artemisinin Resistance in the Rodent Malaria Pathogen Plasmodium yoelii

Antimicrobial Agents and Chemotherapy (2000)

Daniel J. Walker Jessica L. Pitsch Michael Peng B. L. Robinson Wallace Peters

ABSTRACT Artemisinin and its derivatives are important new antimalarials which are now used widely in Southeast Asia. Clinically relevant artemisinin resistance has not yet been reported but is likely to occur. In order to understand how the malaria parasite might become resistant to this drug, we studied artemisinin resistance in the murine malaria parasite Plasmodium yoelii . The artemisinin-resistant strain (ART), which is approximately fourfold less sensitive to artemisinin than the sensitive NS strain, accumulated 43% less radiolabeled drug in vitro ( P < 0.01). Within the parasite, the drug appeared to react with the same parasite proteins in both strains. The translationally controlled tumor protein, one of the artemisinin target proteins, did not differ between the strains. No DNA sequence difference was found, but the resistant strain was found to express 2.5-fold-more protein than the sensitive strain ( P < 0.01). Thus, the phenotype of artemisinin resistance in P. yoelii appears to be multifactorial.

Plasmodium yoelii

Strain (injury)

Plasmodium (life cycle)

10.1128/aac.44.2.344-347.2000

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Citations (75)