Plasmodium falciparum: Adherence of the parasite-infected erythrocytes to chondroitin sulfate proteoglycans bearing structurally distinct chondroitin sulfate chains

Arivalagan Muthusamy, Rajeshwara N. Achur, Manojkumar Valiyaveettil, Channe Gowda

Research output: Contribution to journalArticle

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Abstract

Infection with Plasmodium falciparum during pregnancy leads to the selective adherence of infected red blood cells (IRBCs) in the placenta causing placental malaria. The IRBC adherence is mediated through the chondroitin 4-sulfate (C4S) chains of unusually low-sulfated chondroitin sulfate proteoglycans (CSPGs) in the placenta. To study the structural interactions involved in C4S-IRBC adherence, various investigators have used CSPGs from different sources. Since the structural characteristics of the polysaccharide chains in CSPGs from various sources differ substantially, the CSPGs are likely to differentially bind IRBCs. In this study, the CSPG purified from bovine trachea, a CSPG form of human recombinant thrombomodulin (TM-CSPG), two CSPG fractions from bovine cornea, and the CSPGs of human placenta, the natural receptor, were studied in parallel for their IRBC binding characteristics. The TM-CSPG and corneal CSPG fractions could bind IRBCs at significantly higher density compared to the placental CSPGs. However, the avidity of IRBC binding by TM-CSPG was considerably low compared to placental CSPGs. The corneal CSPGs have substantially higher binding strengths. The bovine tracheal CSPG bound IRBCs at much lower density and exhibited significantly lower avidity than the placental CSPGs. These data demonstrated that the bovine tracheal CSPG and TM-CSPG are not ideal for studying the fine structural interactions involved in the IRBC adherence to the placental C4S, whereas the bovine corneal CSPGs are better alternatives to the placental CSPGs for determining these interactions.

Original languageEnglish (US)
Pages (from-to)183-188
Number of pages6
JournalExperimental Parasitology
Volume107
Issue number3-4
DOIs
StatePublished - Jul 1 2004

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Chondroitin Sulfate Proteoglycans
Chondroitin Sulfates
Plasmodium falciparum
Parasites
Erythrocytes
Placenta

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Immunology
  • Infectious Diseases

Cite this

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title = "Plasmodium falciparum: Adherence of the parasite-infected erythrocytes to chondroitin sulfate proteoglycans bearing structurally distinct chondroitin sulfate chains",
abstract = "Infection with Plasmodium falciparum during pregnancy leads to the selective adherence of infected red blood cells (IRBCs) in the placenta causing placental malaria. The IRBC adherence is mediated through the chondroitin 4-sulfate (C4S) chains of unusually low-sulfated chondroitin sulfate proteoglycans (CSPGs) in the placenta. To study the structural interactions involved in C4S-IRBC adherence, various investigators have used CSPGs from different sources. Since the structural characteristics of the polysaccharide chains in CSPGs from various sources differ substantially, the CSPGs are likely to differentially bind IRBCs. In this study, the CSPG purified from bovine trachea, a CSPG form of human recombinant thrombomodulin (TM-CSPG), two CSPG fractions from bovine cornea, and the CSPGs of human placenta, the natural receptor, were studied in parallel for their IRBC binding characteristics. The TM-CSPG and corneal CSPG fractions could bind IRBCs at significantly higher density compared to the placental CSPGs. However, the avidity of IRBC binding by TM-CSPG was considerably low compared to placental CSPGs. The corneal CSPGs have substantially higher binding strengths. The bovine tracheal CSPG bound IRBCs at much lower density and exhibited significantly lower avidity than the placental CSPGs. These data demonstrated that the bovine tracheal CSPG and TM-CSPG are not ideal for studying the fine structural interactions involved in the IRBC adherence to the placental C4S, whereas the bovine corneal CSPGs are better alternatives to the placental CSPGs for determining these interactions.",
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Plasmodium falciparum : Adherence of the parasite-infected erythrocytes to chondroitin sulfate proteoglycans bearing structurally distinct chondroitin sulfate chains. / Muthusamy, Arivalagan; Achur, Rajeshwara N.; Valiyaveettil, Manojkumar; Gowda, Channe.

In: Experimental Parasitology, Vol. 107, No. 3-4, 01.07.2004, p. 183-188.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Plasmodium falciparum

T2 - Adherence of the parasite-infected erythrocytes to chondroitin sulfate proteoglycans bearing structurally distinct chondroitin sulfate chains

AU - Muthusamy, Arivalagan

AU - Achur, Rajeshwara N.

AU - Valiyaveettil, Manojkumar

AU - Gowda, Channe

PY - 2004/7/1

Y1 - 2004/7/1

N2 - Infection with Plasmodium falciparum during pregnancy leads to the selective adherence of infected red blood cells (IRBCs) in the placenta causing placental malaria. The IRBC adherence is mediated through the chondroitin 4-sulfate (C4S) chains of unusually low-sulfated chondroitin sulfate proteoglycans (CSPGs) in the placenta. To study the structural interactions involved in C4S-IRBC adherence, various investigators have used CSPGs from different sources. Since the structural characteristics of the polysaccharide chains in CSPGs from various sources differ substantially, the CSPGs are likely to differentially bind IRBCs. In this study, the CSPG purified from bovine trachea, a CSPG form of human recombinant thrombomodulin (TM-CSPG), two CSPG fractions from bovine cornea, and the CSPGs of human placenta, the natural receptor, were studied in parallel for their IRBC binding characteristics. The TM-CSPG and corneal CSPG fractions could bind IRBCs at significantly higher density compared to the placental CSPGs. However, the avidity of IRBC binding by TM-CSPG was considerably low compared to placental CSPGs. The corneal CSPGs have substantially higher binding strengths. The bovine tracheal CSPG bound IRBCs at much lower density and exhibited significantly lower avidity than the placental CSPGs. These data demonstrated that the bovine tracheal CSPG and TM-CSPG are not ideal for studying the fine structural interactions involved in the IRBC adherence to the placental C4S, whereas the bovine corneal CSPGs are better alternatives to the placental CSPGs for determining these interactions.

AB - Infection with Plasmodium falciparum during pregnancy leads to the selective adherence of infected red blood cells (IRBCs) in the placenta causing placental malaria. The IRBC adherence is mediated through the chondroitin 4-sulfate (C4S) chains of unusually low-sulfated chondroitin sulfate proteoglycans (CSPGs) in the placenta. To study the structural interactions involved in C4S-IRBC adherence, various investigators have used CSPGs from different sources. Since the structural characteristics of the polysaccharide chains in CSPGs from various sources differ substantially, the CSPGs are likely to differentially bind IRBCs. In this study, the CSPG purified from bovine trachea, a CSPG form of human recombinant thrombomodulin (TM-CSPG), two CSPG fractions from bovine cornea, and the CSPGs of human placenta, the natural receptor, were studied in parallel for their IRBC binding characteristics. The TM-CSPG and corneal CSPG fractions could bind IRBCs at significantly higher density compared to the placental CSPGs. However, the avidity of IRBC binding by TM-CSPG was considerably low compared to placental CSPGs. The corneal CSPGs have substantially higher binding strengths. The bovine tracheal CSPG bound IRBCs at much lower density and exhibited significantly lower avidity than the placental CSPGs. These data demonstrated that the bovine tracheal CSPG and TM-CSPG are not ideal for studying the fine structural interactions involved in the IRBC adherence to the placental C4S, whereas the bovine corneal CSPGs are better alternatives to the placental CSPGs for determining these interactions.

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