Malaria during pregnancy: parasites, antibodies, and chondroitin sulfate A

1999 ◽  
Vol 27 (3) ◽  
pp. A84-A84
Author(s):  
Patrick E. Duffy ◽  
Michal Fried
Keyword(s):  
Chondroitin Sulfate ◽  
Malaria During Pregnancy ◽  
Chondroitin Sulfate A

scholarly journals The Chondroitin Sulfate A-binding Site of the VAR2CSA Protein Involves Multiple N-terminal Domains

2011 ◽  
Vol 286 (18) ◽  
pp. 15908-15917 ◽  
Author(s):  
Madeleine Dahlbäck ◽  
Lars M. Jørgensen ◽  
Morten A. Nielsen ◽  
Thomas M. Clausen ◽  
Sisse B. Ditlev ◽  
...  
Keyword(s):  
Chondroitin Sulfate ◽  
Binding Site ◽  
Placental Malaria ◽  
African Women ◽  
Major Health Problem ◽  
Major Health ◽  
Malaria During Pregnancy ◽  
High Parasite ◽  
Similar Affinity ◽  
Chondroitin Sulfate A

Malaria during pregnancy is a major health problem for African women. The disease is caused by Plasmodium falciparum malaria parasites, which accumulate in the placenta by adhering to chondroitin sulfate A (CSA). The interaction between infected erythrocytes and the placental receptor is mediated by a parasite expressed protein named VAR2CSA. A vaccine protecting pregnant women against placental malaria should induce antibodies inhibiting the interaction between VAR2CSA and CSA. Much effort has been put into defining the part of the 350 kDa VAR2CSA protein that is responsible for binding. It has been shown that full-length recombinant VAR2CSA binds specifically to CSA with high affinity, however to date no sub-fragment of VAR2CSA has been shown to interact with CSA with similar affinity or specificity. In this study, we used a biosensor technology to examine the binding properties of a panel of truncated VAR2CSA proteins. The experiments indicate that the core of the CSA-binding site is situated in three domains, DBL2X-CIDRPAM and a flanking domain, located in the N-terminal part of VAR2CSA. Furthermore, recombinant VAR2CSA subfragments containing this region elicit antibodies with high parasite adhesion blocking activity in animal immunization experiments.

scholarly journals Nonspecific Immunoglobulin M Binding and Chondroitin Sulfate A Binding Are Linked Phenotypes of Plasmodium falciparum Isolates Implicated in Malaria during Pregnancy

2003 ◽  
Vol 71 (8) ◽  
pp. 4767-4771 ◽  
Author(s):  
Alison M. Creasey ◽  
Trine Staalsoe ◽  
Ahmed Raza ◽  
David E. Arnot ◽  
J. Alexandra Rowe
Keyword(s):  
Plasmodium Falciparum ◽  
Chondroitin Sulfate ◽  
Blood Cells ◽  
Immunoglobulin M ◽  
Wide Range ◽  
Malaria During Pregnancy ◽  
Normal Human ◽  
Immunological Assays ◽  
Chondroitin Sulfate A ◽  
In Pregnancy

ABSTRACT Binding of immunoglobulin M (IgM) antibodies from normal human serum to the surface of Plasmodium falciparum-infected red blood cells (iRBC) has previously been demonstrated only in parasites that form rosettes with uninfected red cells. We show that natural, nonspecific IgM but not IgG, IgA, IgD, or IgE also binds to the surface of iRBC selected for adhesion to chondroitin sulfate A (CSA), a placental receptor for parasites associated with malaria in pregnancy. The protease sensitivity of IgM-binding appears to match that of CSA binding, suggesting that the two phenotypes may be mediated by the same parasite molecule. We also show that a wide range of mouse monoclonal antibodies of the IgM class bind nonspecifically to CSA-selected iRBC, an important consideration in the interpretation of immunological assays performed on these parasite lines.

scholarly journals Immunogenicity of Duffy Binding-Like Domains That Bind Chondroitin Sulfate A and Protection against Pregnancy-Associated Malaria

2006 ◽  
Vol 74 (10) ◽  
pp. 5955-5963 ◽  
Author(s):  
Nivedita Bir ◽  
Syed Shams Yazdani ◽  
Marion Avril ◽  
Corinne Layez ◽  
Jürg Gysin ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Chondroitin Sulfate ◽  
Protective Immunity ◽  
Binding Domains ◽  
Malaria During Pregnancy ◽  
Protective Antibodies ◽  
Chondroitin Sulfate A

ABSTRACTSequestration ofPlasmodium falciparum-infected erythrocytes in the placenta is implicated in pathological outcomes of pregnancy-associated malaria (PAM).P. falciparumisolates that sequester in the placenta primarily bind chondroitin sulfate A (CSA). Following exposure to malaria during pregnancy, women in areas of endemicity develop immunity, and so multigravid women are less susceptible to PAM than primigravidae. Protective immunity to PAM is associated with the development of antibodies that recognize diverse CSA-binding, placentalP. falciparumisolates. The epitopes recognized by such protective antibodies have not been identified but are likely to lie in conserved Duffy binding-like (DBL) domains, encoded byvargenes, that bind CSA. Immunization of mice with the CSA-binding DBL3γ domain encoded byvar1CSAelicits cross-reactive antibodies that recognize diverse CSA-bindingP. falciparumisolates and block their binding to placental cryosections under flow. However, CSA-binding isolates primarily expressvar2CSA, which does not encode any DBLγ domains. Here, we demonstrate that antibodies raised against DBL3γ encoded byvar1CSAcross-react with one of the CSA-binding domains, DBL3X, encoded byvar2CSA. This explains the paradoxical observation made here and earlier that anti-rDBL3γ sera recognize CSA-binding isolates and provides evidence for the presence of conserved, cross-reactive epitopes in diverse CSA-binding DBL domains. Such cross-reactive epitopes within CSA-binding DBL domains can form the basis for a vaccine that provides protection against PAM.

scholarly journals Immobilization of Chondroitin Sulfate A onto Monolithic Epoxy Silica Column as a New Chiral Stationary Phase for High-Performance Liquid Chromatographic Enantioseparation

2021 ◽  
Vol 14 (2) ◽  
pp. 98
Author(s):  
Ratih Ratih ◽  
Hermann Wätzig ◽  
Azminah Azminah ◽  
Mufarreh Asmari ◽  
Benjamin Peters ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Chondroitin Sulfate ◽  
High Performance ◽  
Chiral Stationary Phase ◽  
High Performance Liquid Chromatographic ◽  
Schiff Base Formation ◽  
The Individual ◽  
Liquid Chromatographic ◽  
Base Formation ◽  
Chondroitin Sulfate A

Chondroitin sulfate A was covalently immobilized onto a monolithic silica epoxy column involving a Schiff base formation in the presence of ethylenediamine as a spacer and evaluated in terms of its selectivity in enantioseparation. The obtained column was utilized as a chiral stationary phase in enantioseparation of amlodipine and verapamil using a mobile phase consisting of 50 mM phosphate buffer pH 3.5 and UV detection. Sample dilution by organic solvents (preferably 25% v/v acetonitrile-aqueous solution) was applied to achieve baseline enantioresolution (Rs > 3.0) of the individual drug models within 7 min, an excellent linearity (R2 = 0.999) and an interday repeatability of 1.1% to 1.8% RSD. The performance of the immobilized column for quantification of racemate in commercial tablets showed a recovery of 86–98% from tablet matrices. Computational modeling by molecular docking was employed to investigate the feasible complexes between enantiomers and the chiral selector.

scholarly journals Chondroitin Sulfate: A Critical Review of Generic and Specific Problems in Its Characterization and Determination—An Exemplar of a Material with an Unknown or Variable Composition (UVCB)

2018 ◽  
Vol 101 (1) ◽  
pp. 196-202 ◽  
Author(s):  
Duncan Thorburn Burns ◽  
Michael John Walker ◽  
Christopher Mussell
Keyword(s):  
Chondroitin Sulfate ◽  
Critical Review ◽  
Analytical Methods ◽  
Cetylpyridinium Chloride ◽  
Variable Composition ◽  
Reference Samples ◽  
Selection Of ◽  
Chondroitin Sulfate A

Abstract This review discusses the criteria for the selection of appropriate reference samples of chondroitin sulfate (CS) and the properties and specific problems of analytical methods for CS, namely titration with cetylpyridinium chloride; various separations; and UV-Vis, NMR, MS, and IR spectroscopies. Suggestions are put forward with regard to acceptable protocols for manufactures’ and for official/referee analysts for the analysis of CS in products.

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