DARC extracellular domain remodeling in maturating reticulocytes explains Plasmodium vivax tropism.

PubWeight™: 0.75‹?›

🔗 View Article (PMID 28754683)

Published in Blood on July 28, 2017

Authors

Elina Ovchynnikova1,2, Francesca Aglialoro1,2, Arthur E H Bentlage2,3, Gestur Vidarsson2,3, Nichole D Salinas4, Marieke von Lindern1,2, Niraj H Tolia4,5, Emile van den Akker1,2

Author Affiliations

1: Department Hematopoiesis, Sanquin Research, Amsterdam, The Netherlands.
2: Landsteiner Laboratory, Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands.
3: Department of Experimental Immunohematology, Sanquin Research, Amsterdam, The Netherlands; and.
4: Department of Molecular Microbiology and.
5: Department of Biochemistry and Molecular Biophysics, Washington University, St. Louis, MO.

Articles cited by this

The neglected burden of Plasmodium vivax malaria. Am J Trop Med Hyg (2001) 11.74

Estimating the global clinical burden of Plasmodium falciparum malaria in 2007. PLoS Med (2010) 7.22

Neglect of Plasmodium vivax malaria. Trends Parasitol (2007) 4.07

Identification of the erythrocyte binding domains of Plasmodium vivax and Plasmodium knowlesi proteins involved in erythrocyte invasion. J Exp Med (1994) 4.01

A receptor for the malarial parasite Plasmodium vivax: the erythrocyte chemokine receptor. Science (1993) 3.60

Protein 4.1R-dependent multiprotein complex: new insights into the structural organization of the red blood cell membrane. Proc Natl Acad Sci U S A (2008) 2.18

Plasmodium vivax: restricted tropism and rapid remodeling of CD71-positive reticulocytes. Blood (2014) 1.97

Dimerization of Plasmodium vivax DBP is induced upon receptor binding and drives recognition of DARC. Nat Struct Mol Biol (2011) 1.48

Identification of an erythrocyte component carrying the Duffy blood group Fya antigen. Science (1984) 1.16

Significant biochemical, biophysical and metabolic diversity in circulating human cord blood reticulocytes. PLoS One (2013) 1.15

Red blood cell invasion by Plasmodium vivax: structural basis for DBP engagement of DARC. PLoS Pathog (2014) 1.10

Purification and characterization of an erythrocyte membrane protein complex carrying Duffy blood group antigenicity. Possible receptor for Plasmodium vivax and Plasmodium knowlesi malaria parasite. J Biol Chem (1989) 1.07

Angle-scanning SPR imaging for detection of biomolecular interactions on microarrays. Biosens Bioelectron (2007) 1.02

Global Epidemiology of Plasmodium vivax. Am J Trop Med Hyg (2016) 0.93

Broadly neutralizing epitopes in the Plasmodium vivax vaccine candidate Duffy Binding Protein. Proc Natl Acad Sci U S A (2016) 0.86

Structural analysis of the synthetic Duffy Binding Protein (DBP) antigen DEKnull relevant for Plasmodium vivax malaria vaccine design. PLoS Negl Trop Dis (2015) 0.86

Label-free cell profiling. Anal Biochem (2013) 0.80

The human Kell blood group binds the erythroid 4.1R protein: new insights into the 4.1R-dependent red cell membrane complex. Br J Haematol (2015) 0.79