Plasmodium falciparum field isolates use complement receptor 1 (CR1) as a receptor for invasion of erythrocytes

Gordon A. Awandare, Carmenza Spadafora, J. Kathleen Moch, Sheetij Dutta, J. David Haynes, Jose Stoute

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

A majority of Plasmodium falciparum strains invade erythrocytes through interactions with sialic acid (SA) on glycophorins. However, we recently reported that complement receptor 1 (CR1) is a SA-independent invasion receptor of many laboratory strains of P. falciparum. To determine the role of CR1 in erythrocyte invasion among P. falciparum field isolates, we tested eight isolates obtained from children in Kenya. All the parasites examined were capable of invading in a SA-independent manner, and invasion of neuraminidase-treated erythrocytes was nearly completely blocked by anti-CR1 and soluble CR1 (sCR1). In addition, anti-CR1 and sCR1 partially inhibited invasion of intact erythrocytes in a majority of isolates tested. Sequencing of the hypervariable region of P. falciparum AMA-1 showed considerable diversity among all the isolates. These data demonstrate that CR1 mediates SA-independent erythrocyte invasion in P. falciparum field isolates.

Original languageEnglish (US)
Pages (from-to)57-60
Number of pages4
JournalMolecular and biochemical parasitology
Volume177
Issue number1
DOIs
StatePublished - Jan 1 2011

Fingerprint

Complement C1
Complement Receptors
Plasmodium falciparum
Erythrocytes
N-Acetylneuraminic Acid
Glycophorin
Kenya
Neuraminidase
Parasites

All Science Journal Classification (ASJC) codes

  • Parasitology
  • Molecular Biology

Cite this

Awandare, Gordon A. ; Spadafora, Carmenza ; Moch, J. Kathleen ; Dutta, Sheetij ; Haynes, J. David ; Stoute, Jose. / Plasmodium falciparum field isolates use complement receptor 1 (CR1) as a receptor for invasion of erythrocytes. In: Molecular and biochemical parasitology. 2011 ; Vol. 177, No. 1. pp. 57-60.
@article{8bc360ae52ce451d99432a77792b1ecd,
title = "Plasmodium falciparum field isolates use complement receptor 1 (CR1) as a receptor for invasion of erythrocytes",
abstract = "A majority of Plasmodium falciparum strains invade erythrocytes through interactions with sialic acid (SA) on glycophorins. However, we recently reported that complement receptor 1 (CR1) is a SA-independent invasion receptor of many laboratory strains of P. falciparum. To determine the role of CR1 in erythrocyte invasion among P. falciparum field isolates, we tested eight isolates obtained from children in Kenya. All the parasites examined were capable of invading in a SA-independent manner, and invasion of neuraminidase-treated erythrocytes was nearly completely blocked by anti-CR1 and soluble CR1 (sCR1). In addition, anti-CR1 and sCR1 partially inhibited invasion of intact erythrocytes in a majority of isolates tested. Sequencing of the hypervariable region of P. falciparum AMA-1 showed considerable diversity among all the isolates. These data demonstrate that CR1 mediates SA-independent erythrocyte invasion in P. falciparum field isolates.",
author = "Awandare, {Gordon A.} and Carmenza Spadafora and Moch, {J. Kathleen} and Sheetij Dutta and Haynes, {J. David} and Jose Stoute",
year = "2011",
month = "1",
day = "1",
doi = "10.1016/j.molbiopara.2011.01.005",
language = "English (US)",
volume = "177",
pages = "57--60",
journal = "Molecular and Biochemical Parasitology",
issn = "0166-6851",
publisher = "Elsevier",
number = "1",

}

Plasmodium falciparum field isolates use complement receptor 1 (CR1) as a receptor for invasion of erythrocytes. / Awandare, Gordon A.; Spadafora, Carmenza; Moch, J. Kathleen; Dutta, Sheetij; Haynes, J. David; Stoute, Jose.

In: Molecular and biochemical parasitology, Vol. 177, No. 1, 01.01.2011, p. 57-60.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Plasmodium falciparum field isolates use complement receptor 1 (CR1) as a receptor for invasion of erythrocytes

AU - Awandare, Gordon A.

AU - Spadafora, Carmenza

AU - Moch, J. Kathleen

AU - Dutta, Sheetij

AU - Haynes, J. David

AU - Stoute, Jose

PY - 2011/1/1

Y1 - 2011/1/1

N2 - A majority of Plasmodium falciparum strains invade erythrocytes through interactions with sialic acid (SA) on glycophorins. However, we recently reported that complement receptor 1 (CR1) is a SA-independent invasion receptor of many laboratory strains of P. falciparum. To determine the role of CR1 in erythrocyte invasion among P. falciparum field isolates, we tested eight isolates obtained from children in Kenya. All the parasites examined were capable of invading in a SA-independent manner, and invasion of neuraminidase-treated erythrocytes was nearly completely blocked by anti-CR1 and soluble CR1 (sCR1). In addition, anti-CR1 and sCR1 partially inhibited invasion of intact erythrocytes in a majority of isolates tested. Sequencing of the hypervariable region of P. falciparum AMA-1 showed considerable diversity among all the isolates. These data demonstrate that CR1 mediates SA-independent erythrocyte invasion in P. falciparum field isolates.

AB - A majority of Plasmodium falciparum strains invade erythrocytes through interactions with sialic acid (SA) on glycophorins. However, we recently reported that complement receptor 1 (CR1) is a SA-independent invasion receptor of many laboratory strains of P. falciparum. To determine the role of CR1 in erythrocyte invasion among P. falciparum field isolates, we tested eight isolates obtained from children in Kenya. All the parasites examined were capable of invading in a SA-independent manner, and invasion of neuraminidase-treated erythrocytes was nearly completely blocked by anti-CR1 and soluble CR1 (sCR1). In addition, anti-CR1 and sCR1 partially inhibited invasion of intact erythrocytes in a majority of isolates tested. Sequencing of the hypervariable region of P. falciparum AMA-1 showed considerable diversity among all the isolates. These data demonstrate that CR1 mediates SA-independent erythrocyte invasion in P. falciparum field isolates.

UR - http://www.scopus.com/inward/record.url?scp=79952453853&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79952453853&partnerID=8YFLogxK

U2 - 10.1016/j.molbiopara.2011.01.005

DO - 10.1016/j.molbiopara.2011.01.005

M3 - Article

VL - 177

SP - 57

EP - 60

JO - Molecular and Biochemical Parasitology

JF - Molecular and Biochemical Parasitology

SN - 0166-6851

IS - 1

ER -