Abstract
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Infection and Immunity |
| Vol/bind | 71 |
| Udgave nummer | 9 |
| Sider (fra-til) | 5245-53 |
| Antal sider | 8 |
| ISSN | 0019-9567 |
| DOI | |
| Status | Udgivet - 2003 |
Bibliografisk note
Keywords: Adolescent; Alleles; Amino Acid Sequence; Animals; Case-Control Studies; Child; Child, Preschool; Erythrocytes; Genotype; Ghana; Humans; Infant; Infant, Newborn; Ligands; Malaria, Falciparum; Mannose-Binding Lectin; Molecular Sequence Data; Opsonin Proteins; Plasmodium falciparum; Variation (Genetics)Adgang til dokumentet
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Mannose-binding lectin is a disease modifier in clinical malaria and may function as opsonin for Plasmodium falciparum-infected erythrocytes. / Garred, Peter; Nielsen, Morten A; Kurtzhals, Jørgen; Malhotra, Rajneesh; Madsen, Hans O; Goka, Bamenla Q; Akanmori, Bartholomew D; Sim, Robert B; Hviid, Lars.
I: Infection and Immunity, Bind 71, Nr. 9, 2003, s. 5245-53.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
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TY - JOUR
T1 - Mannose-binding lectin is a disease modifier in clinical malaria and may function as opsonin for Plasmodium falciparum-infected erythrocytes
AU - Garred, Peter
AU - Nielsen, Morten A
AU - Kurtzhals, Jørgen
AU - Malhotra, Rajneesh
AU - Madsen, Hans O
AU - Goka, Bamenla Q
AU - Akanmori, Bartholomew D
AU - Sim, Robert B
AU - Hviid, Lars
N1 - Keywords: Adolescent; Alleles; Amino Acid Sequence; Animals; Case-Control Studies; Child; Child, Preschool; Erythrocytes; Genotype; Ghana; Humans; Infant; Infant, Newborn; Ligands; Malaria, Falciparum; Mannose-Binding Lectin; Molecular Sequence Data; Opsonin Proteins; Plasmodium falciparum; Variation (Genetics)
PY - 2003
Y1 - 2003
N2 - Variant alleles in the mannose-binding lectin (MBL) gene (mbl2) causing low levels of functional MBL are associated with susceptibility to different infections and are common in areas where malaria is endemic. Therefore, we investigated whether MBL variant alleles in 551 children from Ghana were associated with the occurrence and outcome parameters of Plasmodium falciparum malaria and asked whether MBL may function as an opsonin for P. falciparum. No difference in MBL genotype frequency was observed between infected and noninfected children or between children with cerebral malaria and/or severe malarial anemia and children with uncomplicated malaria. However, patients with complicated malaria who were homozygous for MBL variant alleles had significantly higher parasite counts and lower blood glucose levels than their MBL-competent counterparts. Distinct calcium-dependent binding of MBL to the membrane of P. falciparum-infected erythrocytes, which could be inhibited by mannose, was observed. Further characterization revealed that MBL reacted with a P. falciparum glycoprotein identical to the 78-kDa glucose-regulated stress protein of P. falciparum. MBL seems to be a disease modifier in clinical malaria and to function as an opsonin for erythrocytes invaded by P. falciparum and may thus be involved in sequestration of the parasite, which in turn may explain the association between homozygosity for MBL variant alleles and high parasite counts.
AB - Variant alleles in the mannose-binding lectin (MBL) gene (mbl2) causing low levels of functional MBL are associated with susceptibility to different infections and are common in areas where malaria is endemic. Therefore, we investigated whether MBL variant alleles in 551 children from Ghana were associated with the occurrence and outcome parameters of Plasmodium falciparum malaria and asked whether MBL may function as an opsonin for P. falciparum. No difference in MBL genotype frequency was observed between infected and noninfected children or between children with cerebral malaria and/or severe malarial anemia and children with uncomplicated malaria. However, patients with complicated malaria who were homozygous for MBL variant alleles had significantly higher parasite counts and lower blood glucose levels than their MBL-competent counterparts. Distinct calcium-dependent binding of MBL to the membrane of P. falciparum-infected erythrocytes, which could be inhibited by mannose, was observed. Further characterization revealed that MBL reacted with a P. falciparum glycoprotein identical to the 78-kDa glucose-regulated stress protein of P. falciparum. MBL seems to be a disease modifier in clinical malaria and to function as an opsonin for erythrocytes invaded by P. falciparum and may thus be involved in sequestration of the parasite, which in turn may explain the association between homozygosity for MBL variant alleles and high parasite counts.
U2 - 10.1128/IAI.71.9.5245-5253.2003
DO - 10.1128/IAI.71.9.5245-5253.2003
M3 - Journal article
C2 - 12933871
VL - 71
SP - 5245
EP - 5253
JO - Infection and Immunity
JF - Infection and Immunity
SN - 0019-9567
IS - 9
ER -