Unusually low-sulfated chondroitin 4-sulfate of human placenta and its role in placental malaria

Channe Gowda, Rajeshwara Achur, Arivalagan Muthusamy, Keiichi Takagaki

Research output: Contribution to journalShort survey

5 Citations (Scopus)

Abstract

The residents in malaria endemic areas generally acquire protective immunity to malaria by their adulthood. Despite this previously acquired natural immunity, women are highly susceptible to malaria during pregnancy, especially in their first pregnancy. This is due to the sequestration of a phenotypically different Plasmodium falciparum in the placenta by the adherence of the infected red blood cells (IRBCs). Because, prior to first pregnancy, women were not exposed to the placental adherent parasite at significant levels, they lack the phenotype-specific immunity. Therefore, infection during pregnancy leads to placental malaria, which is associated with a number of clinical manifestations. The adherence of P. falciparum IRBCs in the placenta is mediated predominantly by an unusually low sulfated aggrecan family chondroitin sulfate proteoglycan localized in the intervillous space of the placenta. The IRBC binding requires the participation of both 4-sulfated and nonsulfated disaccharide repeats of the chondroitin sulfate chains. The minimal structural motif required for optimal binding is a dodecasaccharide with two 4-sulfated and four non-sulfated disaccharides. P. falciparum erythrocyte membrane protein 1, a product of the var gene family, expressed on the surface of IRBCs has been proposed as the ligand for the IRBC adherence. In this review, we summarize our current knowledge on the structure of the placental chondroitin sulfate proteoglycan receptor, the identity of the parasite ligand, and chondroitin sulfate structural requirements for IRBC adherence.

Original languageEnglish (US)
Pages (from-to)407-420
Number of pages14
JournalTrends in Glycoscience and Glycotechnology
Volume16
Issue number92
DOIs
StatePublished - Jan 1 2004

Fingerprint

Chondroitin Sulfates
Placenta
Malaria
Blood
Erythrocytes
Chondroitin Sulfate Proteoglycans
Pregnancy
Disaccharides
Plasmodium falciparum
Immunity
Parasites
Ligands
Aggrecans
Adaptive Immunity
Innate Immunity
Membrane Proteins
Genes
Cells
Phenotype
Infection

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Organic Chemistry

Cite this

Gowda, Channe ; Achur, Rajeshwara ; Muthusamy, Arivalagan ; Takagaki, Keiichi. / Unusually low-sulfated chondroitin 4-sulfate of human placenta and its role in placental malaria. In: Trends in Glycoscience and Glycotechnology. 2004 ; Vol. 16, No. 92. pp. 407-420.
@article{6f7d23e3bf4343568b123ddf0ad0f0a4,
title = "Unusually low-sulfated chondroitin 4-sulfate of human placenta and its role in placental malaria",
abstract = "The residents in malaria endemic areas generally acquire protective immunity to malaria by their adulthood. Despite this previously acquired natural immunity, women are highly susceptible to malaria during pregnancy, especially in their first pregnancy. This is due to the sequestration of a phenotypically different Plasmodium falciparum in the placenta by the adherence of the infected red blood cells (IRBCs). Because, prior to first pregnancy, women were not exposed to the placental adherent parasite at significant levels, they lack the phenotype-specific immunity. Therefore, infection during pregnancy leads to placental malaria, which is associated with a number of clinical manifestations. The adherence of P. falciparum IRBCs in the placenta is mediated predominantly by an unusually low sulfated aggrecan family chondroitin sulfate proteoglycan localized in the intervillous space of the placenta. The IRBC binding requires the participation of both 4-sulfated and nonsulfated disaccharide repeats of the chondroitin sulfate chains. The minimal structural motif required for optimal binding is a dodecasaccharide with two 4-sulfated and four non-sulfated disaccharides. P. falciparum erythrocyte membrane protein 1, a product of the var gene family, expressed on the surface of IRBCs has been proposed as the ligand for the IRBC adherence. In this review, we summarize our current knowledge on the structure of the placental chondroitin sulfate proteoglycan receptor, the identity of the parasite ligand, and chondroitin sulfate structural requirements for IRBC adherence.",
author = "Channe Gowda and Rajeshwara Achur and Arivalagan Muthusamy and Keiichi Takagaki",
year = "2004",
month = "1",
day = "1",
doi = "10.4052/tigg.16.407",
language = "English (US)",
volume = "16",
pages = "407--420",
journal = "Trends in Glycoscience and Glycotechnology",
issn = "0915-7352",
publisher = "Gakushin Publishing Company",
number = "92",

}

Unusually low-sulfated chondroitin 4-sulfate of human placenta and its role in placental malaria. / Gowda, Channe; Achur, Rajeshwara; Muthusamy, Arivalagan; Takagaki, Keiichi.

In: Trends in Glycoscience and Glycotechnology, Vol. 16, No. 92, 01.01.2004, p. 407-420.

Research output: Contribution to journalShort survey

TY - JOUR

T1 - Unusually low-sulfated chondroitin 4-sulfate of human placenta and its role in placental malaria

AU - Gowda, Channe

AU - Achur, Rajeshwara

AU - Muthusamy, Arivalagan

AU - Takagaki, Keiichi

PY - 2004/1/1

Y1 - 2004/1/1

N2 - The residents in malaria endemic areas generally acquire protective immunity to malaria by their adulthood. Despite this previously acquired natural immunity, women are highly susceptible to malaria during pregnancy, especially in their first pregnancy. This is due to the sequestration of a phenotypically different Plasmodium falciparum in the placenta by the adherence of the infected red blood cells (IRBCs). Because, prior to first pregnancy, women were not exposed to the placental adherent parasite at significant levels, they lack the phenotype-specific immunity. Therefore, infection during pregnancy leads to placental malaria, which is associated with a number of clinical manifestations. The adherence of P. falciparum IRBCs in the placenta is mediated predominantly by an unusually low sulfated aggrecan family chondroitin sulfate proteoglycan localized in the intervillous space of the placenta. The IRBC binding requires the participation of both 4-sulfated and nonsulfated disaccharide repeats of the chondroitin sulfate chains. The minimal structural motif required for optimal binding is a dodecasaccharide with two 4-sulfated and four non-sulfated disaccharides. P. falciparum erythrocyte membrane protein 1, a product of the var gene family, expressed on the surface of IRBCs has been proposed as the ligand for the IRBC adherence. In this review, we summarize our current knowledge on the structure of the placental chondroitin sulfate proteoglycan receptor, the identity of the parasite ligand, and chondroitin sulfate structural requirements for IRBC adherence.

AB - The residents in malaria endemic areas generally acquire protective immunity to malaria by their adulthood. Despite this previously acquired natural immunity, women are highly susceptible to malaria during pregnancy, especially in their first pregnancy. This is due to the sequestration of a phenotypically different Plasmodium falciparum in the placenta by the adherence of the infected red blood cells (IRBCs). Because, prior to first pregnancy, women were not exposed to the placental adherent parasite at significant levels, they lack the phenotype-specific immunity. Therefore, infection during pregnancy leads to placental malaria, which is associated with a number of clinical manifestations. The adherence of P. falciparum IRBCs in the placenta is mediated predominantly by an unusually low sulfated aggrecan family chondroitin sulfate proteoglycan localized in the intervillous space of the placenta. The IRBC binding requires the participation of both 4-sulfated and nonsulfated disaccharide repeats of the chondroitin sulfate chains. The minimal structural motif required for optimal binding is a dodecasaccharide with two 4-sulfated and four non-sulfated disaccharides. P. falciparum erythrocyte membrane protein 1, a product of the var gene family, expressed on the surface of IRBCs has been proposed as the ligand for the IRBC adherence. In this review, we summarize our current knowledge on the structure of the placental chondroitin sulfate proteoglycan receptor, the identity of the parasite ligand, and chondroitin sulfate structural requirements for IRBC adherence.

UR - http://www.scopus.com/inward/record.url?scp=12344280843&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=12344280843&partnerID=8YFLogxK

U2 - 10.4052/tigg.16.407

DO - 10.4052/tigg.16.407

M3 - Short survey

VL - 16

SP - 407

EP - 420

JO - Trends in Glycoscience and Glycotechnology

JF - Trends in Glycoscience and Glycotechnology

SN - 0915-7352

IS - 92

ER -