Recombinant Duffy binding-like-? domains of Plasmodium falciparum erythrocyte membrane protein 1 elicit antibodies in rats that recognise conserved epitopes

2003 ◽  
Vol 90 (6) ◽  
pp. 467-472 ◽  
Author(s):  
Raphael M. Oguariri ◽  
Denise Mattei ◽  
Cristina Tena-Tom�s ◽  
Anne-Catrin Uhlemann ◽  
Peter G. Kremsner ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Erythrocyte Membrane Protein ◽  
Falciparum Erythrocyte Membrane Protein

scholarly journals DNA secondary structures are associated with recombination in major Plasmodium falciparum variable surface antigen gene families

2013 ◽  
Vol 42 (4) ◽  
pp. 2270-2281 ◽  
Author(s):  
Adam F. Sander ◽  
Thomas Lavstsen ◽  
Thomas S. Rask ◽  
Michael Lisby ◽  
Ali Salanti ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Gene Families ◽  
Secondary Structures ◽  
Erythrocyte Membrane Protein ◽  
Sexual Stages ◽  
Dna Secondary Structures ◽  
Parasitic Pathogens ◽  
Falciparum Erythrocyte Membrane Protein

Abstract Many bacterial, viral and parasitic pathogens undergo antigenic variation to counter host immune defense mechanisms. In Plasmodium falciparum, the most lethal of human malaria parasites, switching of var gene expression results in alternating expression of the adhesion proteins of the Plasmodium falciparum-erythrocyte membrane protein 1 class on the infected erythrocyte surface. Recombination clearly generates var diversity, but the nature and control of the genetic exchanges involved remain unclear. By experimental and bioinformatic identification of recombination events and genome-wide recombination hotspots in var genes, we show that during the parasite’s sexual stages, ectopic recombination between isogenous var paralogs occurs near low folding free energy DNA 50-mers and that these sequences are heavily concentrated at the boundaries of regions encoding individual Plasmodium falciparum-erythrocyte membrane protein 1 structural domains. The recombinogenic potential of these 50-mers is not parasite-specific because these sequences also induce recombination when transferred to the yeast Saccharomyces cerevisiae. Genetic cross data suggest that DNA secondary structures (DSS) act as inducers of recombination during DNA replication in P. falciparum sexual stages, and that these DSS-regulated genetic exchanges generate functional and diverse P. falciparum adhesion antigens. DSS-induced recombination may represent a common mechanism for optimizing the evolvability of virulence gene families in pathogens.

scholarly journals Identification of Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) as the Rosetting Ligand of the Malaria Parasite P. falciparum

1998 ◽  
Vol 187 (1) ◽  
pp. 15-23 ◽  
Author(s):  
Qijun Chen ◽  
Antonio Barragan ◽  
Victor Fernandez ◽  
Annika Sundström ◽  
Martha Schlichtherle ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Membrane Protein ◽  
Heparan Sulfate ◽  
Erythrocyte Membrane ◽  
Plasmodium Falciparum Malaria ◽  
Glutathione S Transferase ◽  
Binding Motifs ◽  
Erythrocyte Membrane Protein ◽  
Adhesive Interactions ◽  
Falciparum Erythrocyte Membrane Protein

Severe Plasmodium falciparum malaria is characterized by excessive sequestration of infected and uninfected erythrocytes in the microvasculature of the affected organ. Rosetting, the adhesion of P. falciparum–infected erythrocytes to uninfected erythrocytes is a virulent parasite phenotype associated with the occurrence of severe malaria. Here we report on the identification by single-cell reverse transcriptase PCR and cDNA cloning of the adhesive ligand P. falciparum erythrocyte membrane protein 1 (PfEMP1). Rosetting PfEMP1 contains clusters of glycosaminoglycan-binding motifs. A recombinant fusion protein (Duffy binding-like 1–glutathione S transferase; Duffy binding-like-1–GST) was found to adhere directly to normal erythrocytes, disrupt naturally formed rosettes, block rosette reformation, and bind to a heparin-Sepharose matrix. The adhesive interactions could be inhibited with heparan sulfate or enzymes that remove heparan sulfate from the cell surface whereas other enzymes or similar glycosaminoglycans of a like negative charge did not affect the binding. PfEMP1 is suggested to be the rosetting ligand and heparan sulfate, or a heparan sulfate–like molecule, the receptor both for PfEMP1 binding and naturally formed erythrocyte rosettes.

scholarly journals Plasmodium falciparum Erythrocyte Membrane Protein 1 Diversity in Seven Genomes – Divide and Conquer

2010 ◽  
Vol 6 (9) ◽  
pp. e1000933 ◽  
Author(s):  
Thomas S. Rask ◽  
Daniel A. Hansen ◽  
Thor G. Theander ◽  
Anders Gorm Pedersen ◽  
Thomas Lavstsen
Keyword(s):  
Plasmodium Falciparum ◽  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Divide And Conquer ◽  
Erythrocyte Membrane Protein ◽  
Falciparum Erythrocyte Membrane Protein

Classification of adhesive domains in the Plasmodium falciparum Erythrocyte Membrane Protein 1 family

2000 ◽  
Vol 110 (2) ◽  
pp. 293-310 ◽  
Author(s):  
Joseph D Smith ◽  
Gangadharan Subramanian ◽  
Benoit Gamain ◽  
Dror I Baruch ◽  
Louis H Miller
Keyword(s):  
Plasmodium Falciparum ◽  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Erythrocyte Membrane Protein ◽  
Falciparum Erythrocyte Membrane Protein

scholarly journals Evidence for in vitro and in vivo expression of the conserved VAR3 (type 3) plasmodium falciparum erythrocyte membrane protein 1

2012 ◽  
Vol 11 (1) ◽  
Author(s):  
Christian W Wang ◽  
Thomas Lavstsen ◽  
Dominique C Bengtsson ◽  
Pamela A Magistrado ◽  
Sanne S Berger ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Membrane Protein ◽  
Erythrocyte Membrane ◽  
Erythrocyte Membrane Protein ◽  
In Vivo Expression ◽  
Type 3 ◽  
Falciparum Erythrocyte Membrane Protein
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