<i>Plasmodium falciparum</i>
            domain mediating adhesion to chondroitin sulfate A: A receptor for human placental infection

Buffet, Pierre; Gamain, B; Scheidig, Christine; Baruch, Dror I.; Smith, Joseph D.; Hernández‐Rivas, Rosaura; Pouvelle, Bruno; Oishi, Shinya; Fujii, Nobutaka; Fusaı̈, Thierry; Parzy, Daniel; Miller, Louis H.; Gysin, Jürg; Scherf, Artur

doi:10.1073/pnas.96.22.12743

Cited by 223 publications

(231 citation statements)

References 23 publications

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“…As an example, pregnant women develop strain-independent anti-CSA adhesion antibodies that correlate with protection against placental malaria (32). Although the epitope(s) recognized by antiadhesion antibodies are not known, CSA-binding PfEMP1 (24,25) may possess conserved features that are targets of strain-independent protection. In terms of the general population, it has been reported (33) that variants isolated from individuals with severe disease are more commonly recognized by serum from children in the community than those from cases of mild disease.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Plasmodium falciparum intercellular adhesion molecule-1 binding domain: A parasite adhesion trait implicated in cerebral malaria

Smith

Craig

Kriek

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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Binding of infected erythrocytes to brain venules is a central pathogenic event in the lethal malaria disease complication, cerebral malaria. The only parasite adhesion trait linked to cerebral sequestration is binding to intercellular adhesion molecule-1 (ICAM-1). In this report, we show that Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) binds ICAM-1. We have cloned and expressed PfEMP1 recombinant proteins from the A4tres parasite. Using heterologous expression in mammalian cells, the minimal ICAM-1 binding domain was a complex domain consisting of the second Duffy binding-like (DBL) domain and the C2 domain. Constructs that contained either domain alone did not bind ICAM-1. Based on phylogenetic criteria, there are five distinct PfEMP1 DBL types designated α, β, γ, δ, and ɛ. The DBL domain from the A4tres that binds ICAM-1 is DBLβ type. A PfEMP1 cloned from a distinct ICAM-1 binding variant, the A4 parasite, contains a DBLβ domain and a C2 domain in tandem arrangement similar to the A4tres PfEMP1. Anti-PfEMP1 antisera implicate the DBLβ domain from A4var PfEMP1 in ICAM-1 adhesion. The identification of a P. falciparum ICAM-1 binding domain may clarify mechanisms responsible for the pathogenesis of cerebral malaria and lead to interventions or vaccines that reduce malarial disease.

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Section: Discussionmentioning

confidence: 99%

Identification of a Plasmodium falciparum intercellular adhesion molecule-1 binding domain: A parasite adhesion trait implicated in cerebral malaria

Smith

Craig

Kriek

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

218

190

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“…Although VAR2CSA appears to be the only PfEMP1 associated with the VSA PAM phenotype, 16,17 many other PfEMP1 variants contain domains with affinity for CSA. 20,21 Furthermore, CSA is present in nonplacental tissues such as brain endothelium 22 (which has even been used by some to select for pregnancy-type parasites), and yet there is no pre-existing immunity to VSA PAM at first pregnancy. In addition, very recently, Gowda's group 23 has published evidence to suggest that the parasite molecule directly responsible for IE adhesion to CSA is a low-molecular weight protein rather than high-molecular weight molecules such as VAR2CSA.…”

Section: Discussionmentioning

confidence: 99%

Adhesion Specificities of Plasmodium falciparum-Infected Erythrocytes Involved in the Pathogenesis of Pregnancy-Associated Malaria

Hviid

2007

The American Journal of Pathology

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“…It appears that the primary function of PfEMP1 is to prevent IRBCs from being readily recognized by the host immune system (23,24). In 1999, two groups reported that two distinct PfEMP1 variants, one termed FCR3var1CSA (from FCR-3 parasite strain) and the other termed CS2var1CSA (from CS2 parasite strain), mediate IRBC binding to C4S in a strain-dependent manner (25,26). In both cases, a specific domain called DBL-3␥ was reported to be involved in the IRBC binding.…”

mentioning

confidence: 99%

Structural Basis for the Adherence of Plasmodium falciparum-infected Erythrocytes to Chondroitin 4-Sulfate and Design of Novel Photoactivable Reagents for the Identification of Parasite Adhesive Proteins

Gowda¹,

Madhunapantula²,

Achur

et al. 2007

Journal of Biological Chemistry

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A dodecasaccharide motif of the low-sulfated chondroitin 4-sulfate (C4S) mediate the binding of Plasmodium falciparuminfected red blood cells (IRBCs) in human placenta. Here we studied the detailed C4S structural requirements by assessing the ability of chemically modified C4S to inhibit IRBC binding to the placental chondroitin sulfate proteoglycan. Replacement of the N-acetyl groups with bulky N-acyl or N-benzoyl substituents had no effect on the inhibitory activity of C4S, whereas reduction of the carboxyl groups abrogated the activity. Dermatan sulfates showed ϳ50% inhibitory activity when compared with C4Ss with similar sulfate contents. These data demonstrate that the C4S carboxyl groups and their equatorial orientation but not the N-acetyl groups are critical for IRBC binding. Conjugation of bulky substituents to the reducing end N-acetylgalactosamine residues of C4S dodecasaccharide had no effect on its inhibitory activity. Based on these results, we prepared photoaffinity reagents for the identification of the parasite proteins involved in C4S binding. Cross-linking of the IRBCs with a radioiodinated photoactivable C4S dodecasaccharide labeled a ϳ22-kDa novel parasite protein, suggesting strongly for the first time that a low molecular weight IRBC surface protein rather than a 200 -400-kDa PfEMP1 is involved in C4S binding. Conjugation of biotin to the C4S dodecasaccharide photoaffinity probe afforded a strategy for the isolation of the labeled protein by avidin affinity precipitation, facilitating efforts to identify the C4S-adherent IRBC protein(s). Our results also have broader implications for designing oligosaccharide-based photoaffinity probes for the identification of proteins involved in glycosaminoglycan-dependent attachment of microbes to hosts.An unusual feature of Plasmodium falciparum infection compared with the three other human malarial parasites, Plasmodium vivax, Plasmodium ovale, and Plasmodium malariae, is that only the former parasite is able to sequester in the microvascular capillaries of various organs (1, 2). In P. falciparuminfected individuals, the infected red blood cells (IRBCs) 5 adhere to the vascular endothelial surface by binding to the cell adhesion molecules. This adherence property is believed to play an important role in the development of cerebral and other severe malaria syndromes (2-4). Several host molecules have been implicated in the IRBC adherence, including thrombospondin, CD36, intercellular adhesion molecule 1, vascular cell adhesion molecule 1, E-selectin, P-selectin, platelet endothelial cell adhesion molecule/CD31, and chondroitin 4-sulfate (1-6). In response to the development of adherent phenotypespecific immunity by hosts, parasites with different adherent receptor specificity evolve to efficiently survive in the host. However, eventually, when immunity to various adhesive parasite phenotypes is developed, the host effectively controls infection and avoids pathogenesis. This is generally true for malaria-immune people regardless of gender. However, in ...

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Plasmodium falciparum domain mediating adhesion to chondroitin sulfate A: A receptor for human placental infection

Cited by 223 publications

References 23 publications

Identification of a Plasmodium falciparum intercellular adhesion molecule-1 binding domain: A parasite adhesion trait implicated in cerebral malaria

Identification of a Plasmodium falciparum intercellular adhesion molecule-1 binding domain: A parasite adhesion trait implicated in cerebral malaria

Adhesion Specificities of Plasmodium falciparum-Infected Erythrocytes Involved in the Pathogenesis of Pregnancy-Associated Malaria

Structural Basis for the Adherence of Plasmodium falciparum-infected Erythrocytes to Chondroitin 4-Sulfate and Design of Novel Photoactivable Reagents for the Identification of Parasite Adhesive Proteins

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