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Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain

Molecular processes that govern pathogenic features of erythrocyte invasion and cytoadherence in malaria are reliant on Plasmodium-specific Duffy-binding-like domains (DBLs). These cysteine-rich modules recognize diverse host cell-surface receptors during pathogenesis. DBLs of parasite erythrocyte-b... Full description

Journal Title: Nature 2006-02-09, Vol.439 (7077), p.741-744
Main Author: Sharma, Amit
Other Authors: Chitnis, Chetan E , Hora, Rachna , Singh, Saurabh Kumar , Belrhali, Hassan
Format: Electronic Article Electronic Article
Language: English
Subjects:
Publisher: London: Nature Publishing
ID: ISSN: 0028-0836
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recordid: cdi_proquest_miscellaneous_743486333
title: Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain
format: Article
creator:
  • Sharma, Amit
  • Chitnis, Chetan E
  • Hora, Rachna
  • Singh, Saurabh Kumar
  • Belrhali, Hassan
subjects:
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Biological and medical sciences
  • Crystallography, X-Ray
  • Disulfides - metabolism
  • Duffy Blood-Group System - chemistry
  • Duffy Blood-Group System - metabolism
  • Erythrocytes - chemistry
  • Erythrocytes - metabolism
  • Human protozoal diseases
  • Humans
  • Infectious diseases
  • Malaria
  • Medical sciences
  • Models, Molecular
  • Molecular Sequence Data
  • Parasitic diseases
  • Plasmodium falciparum - chemistry
  • Plasmodium knowlesi - chemistry
  • Plasmodium knowlesi - metabolism
  • Plasmodium knowlesi - pathogenicity
  • Protein Binding
  • Protein Folding
  • Protein Structure, Tertiary
  • Protozoal diseases
  • Structure-Activity Relationship
ispartof: Nature, 2006-02-09, Vol.439 (7077), p.741-744
description: Molecular processes that govern pathogenic features of erythrocyte invasion and cytoadherence in malaria are reliant on Plasmodium-specific Duffy-binding-like domains (DBLs). These cysteine-rich modules recognize diverse host cell-surface receptors during pathogenesis. DBLs of parasite erythrocyte-binding proteins mediate invasion, and those from the antigenically variant P. falciparum erythrocyte membrane protein 1 (PfEMP1) have been implicated in cytoadherence. The simian and human malarial parasites, P. knowlesi and P. vivax, invade human erythrocytes exclusively through the host DARC receptor (Duffy antigen receptor for chemokines). Here we present the crystal structure of the P. knowlesi DBL domain (Pkα-DBL), which binds to DARC during invasion of human erythrocytes. Pkα-DBL retains the overall fold observed in DBLs from P. falciparum erythrocyte-binding antigen (EBA)-175 (ref. 4). Mapping the residues that have previously been implicated in binding highlights a fairly flat but exposed site for DARC recognition in subdomain 2 of Pkα-DBL; this is in sharp contrast to receptor recognition by EBA-175 (ref. 4). In Pkα-DBL, the residues that contact DARC and the clusters of residues under immune pressure map to opposite surfaces of the DBL, and suggest a possible mechanism for immune evasion by P. vivax. Our comparative structural analysis of Pkα-DBL and P. falciparum EBA-175 provides a framework for the understanding of malaria parasite DBLs, and may affect the development of new prophylactic and therapeutic strategies.
language: eng
source:
identifier: ISSN: 0028-0836
fulltext: no_fulltext
issn:
  • 0028-0836
  • 1476-4687
  • 1476-4679
url: Link


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titleStructural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain
creatorSharma, Amit ; Chitnis, Chetan E ; Hora, Rachna ; Singh, Saurabh Kumar ; Belrhali, Hassan
creatorcontribSharma, Amit ; Chitnis, Chetan E ; Hora, Rachna ; Singh, Saurabh Kumar ; Belrhali, Hassan
descriptionMolecular processes that govern pathogenic features of erythrocyte invasion and cytoadherence in malaria are reliant on Plasmodium-specific Duffy-binding-like domains (DBLs). These cysteine-rich modules recognize diverse host cell-surface receptors during pathogenesis. DBLs of parasite erythrocyte-binding proteins mediate invasion, and those from the antigenically variant P. falciparum erythrocyte membrane protein 1 (PfEMP1) have been implicated in cytoadherence. The simian and human malarial parasites, P. knowlesi and P. vivax, invade human erythrocytes exclusively through the host DARC receptor (Duffy antigen receptor for chemokines). Here we present the crystal structure of the P. knowlesi DBL domain (Pkα-DBL), which binds to DARC during invasion of human erythrocytes. Pkα-DBL retains the overall fold observed in DBLs from P. falciparum erythrocyte-binding antigen (EBA)-175 (ref. 4). Mapping the residues that have previously been implicated in binding highlights a fairly flat but exposed site for DARC recognition in subdomain 2 of Pkα-DBL; this is in sharp contrast to receptor recognition by EBA-175 (ref. 4). In Pkα-DBL, the residues that contact DARC and the clusters of residues under immune pressure map to opposite surfaces of the DBL, and suggest a possible mechanism for immune evasion by P. vivax. Our comparative structural analysis of Pkα-DBL and P. falciparum EBA-175 provides a framework for the understanding of malaria parasite DBLs, and may affect the development of new prophylactic and therapeutic strategies.
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subjectAmino Acid Sequence ; Animals ; Binding Sites ; Biological and medical sciences ; Crystallography, X-Ray ; Disulfides - metabolism ; Duffy Blood-Group System - chemistry ; Duffy Blood-Group System - metabolism ; Erythrocytes - chemistry ; Erythrocytes - metabolism ; Human protozoal diseases ; Humans ; Infectious diseases ; Malaria ; Medical sciences ; Models, Molecular ; Molecular Sequence Data ; Parasitic diseases ; Plasmodium falciparum - chemistry ; Plasmodium knowlesi - chemistry ; Plasmodium knowlesi - metabolism ; Plasmodium knowlesi - pathogenicity ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; Protozoal diseases ; Structure-Activity Relationship
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descriptionMolecular processes that govern pathogenic features of erythrocyte invasion and cytoadherence in malaria are reliant on Plasmodium-specific Duffy-binding-like domains (DBLs). These cysteine-rich modules recognize diverse host cell-surface receptors during pathogenesis. DBLs of parasite erythrocyte-binding proteins mediate invasion, and those from the antigenically variant P. falciparum erythrocyte membrane protein 1 (PfEMP1) have been implicated in cytoadherence. The simian and human malarial parasites, P. knowlesi and P. vivax, invade human erythrocytes exclusively through the host DARC receptor (Duffy antigen receptor for chemokines). Here we present the crystal structure of the P. knowlesi DBL domain (Pkα-DBL), which binds to DARC during invasion of human erythrocytes. Pkα-DBL retains the overall fold observed in DBLs from P. falciparum erythrocyte-binding antigen (EBA)-175 (ref. 4). Mapping the residues that have previously been implicated in binding highlights a fairly flat but exposed site for DARC recognition in subdomain 2 of Pkα-DBL; this is in sharp contrast to receptor recognition by EBA-175 (ref. 4). In Pkα-DBL, the residues that contact DARC and the clusters of residues under immune pressure map to opposite surfaces of the DBL, and suggest a possible mechanism for immune evasion by P. vivax. Our comparative structural analysis of Pkα-DBL and P. falciparum EBA-175 provides a framework for the understanding of malaria parasite DBLs, and may affect the development of new prophylactic and therapeutic strategies.
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19Plasmodium knowlesi - chemistry
20Plasmodium knowlesi - metabolism
21Plasmodium knowlesi - pathogenicity
22Protein Binding
23Protein Folding
24Protein Structure, Tertiary
25Protozoal diseases
26Structure-Activity Relationship
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abstractMolecular processes that govern pathogenic features of erythrocyte invasion and cytoadherence in malaria are reliant on Plasmodium-specific Duffy-binding-like domains (DBLs). These cysteine-rich modules recognize diverse host cell-surface receptors during pathogenesis. DBLs of parasite erythrocyte-binding proteins mediate invasion, and those from the antigenically variant P. falciparum erythrocyte membrane protein 1 (PfEMP1) have been implicated in cytoadherence. The simian and human malarial parasites, P. knowlesi and P. vivax, invade human erythrocytes exclusively through the host DARC receptor (Duffy antigen receptor for chemokines). Here we present the crystal structure of the P. knowlesi DBL domain (Pkα-DBL), which binds to DARC during invasion of human erythrocytes. Pkα-DBL retains the overall fold observed in DBLs from P. falciparum erythrocyte-binding antigen (EBA)-175 (ref. 4). Mapping the residues that have previously been implicated in binding highlights a fairly flat but exposed site for DARC recognition in subdomain 2 of Pkα-DBL; this is in sharp contrast to receptor recognition by EBA-175 (ref. 4). In Pkα-DBL, the residues that contact DARC and the clusters of residues under immune pressure map to opposite surfaces of the DBL, and suggest a possible mechanism for immune evasion by P. vivax. Our comparative structural analysis of Pkα-DBL and P. falciparum EBA-175 provides a framework for the understanding of malaria parasite DBLs, and may affect the development of new prophylactic and therapeutic strategies.
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