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PfEMP1

Red blood cell blood group A antigen level affects the ability of heparin and PfEMP1 antibodies to disrupt Plasmodium falciparum rosettes

November 23, 2021 - 09:29 -- Open Access
Author(s): 
Pontus Hedberg, Madle Sirel, Kirsten Moll, Mpungu Steven Kiwuwa, Petter Höglund, Ulf Ribacke and Mats Wahlgren
Reference: 
Malaria Journal 2021 20:441, 18 November 2021

The histo-blood group ABO system has been associated with adverse outcomes in COVID-19, thromboembolic diseases and Plasmodium falciparum malaria. An integral part of the severe malaria pathogenesis is rosetting, the adherence of parasite infected red blood cells (RBCs) to uninfected RBCs. Rosetting is influenced by the host’s ABO blood group (Bg) and rosettes formed in BgA have previously been shown to be more resilient to disruption by heparin and shield the parasite derived surface antigens from antibodies. However, data on rosetting in weak BgA subgroups is scarce and based on investigations of relatively few donors.

Malian adults maintain serologic responses to virulent PfEMP1s amid seasonal patterns of fluctuation

July 20, 2021 - 11:54 -- Open Access
Author(s): 
Ventimiglia NT, Stucke EM, Travassos MA, et al.
Reference: 
Sci Rep. 2021 Jul 13;11(1):14401

Plasmodium falciparum erythrocyte membrane protein-1s (PfEMP1s), diverse malaria proteins expressed on the infected erythrocyte surface, play an important role in pathogenesis, mediating adhesion to host vascular endothelium. Antibodies to particular non-CD36-binding PfEMP1s are associated with protection against severe disease.

Not Open Access | Complement C1s cleaves PfEMP1 at interdomain conserved sites inhibiting Plasmodium falciparum cytoadherence

June 1, 2021 - 12:26 -- NOT Open Access
Author(s): 
Azasi Y, Low LM, Miller LH, et al.
Reference: 
Proc Natl Acad Sci U S A. 2021 Jun 1;118(22):e2104166118

Cytoadhesion of Plasmodium falciparum-infected erythrocytes (IEs) to the endothelial lining of blood vessels protects parasites from splenic destruction, but also leads to detrimental inflammation and vessel occlusion. Surface display of the P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesion ligands exposes them to host antibodies and serum proteins. PfEMP1 are important targets of acquired immunity to malaria, and through evolution, the protein family has expanded and diversified to bind a select set of host receptors through antigenically diversified receptor-binding domains.

NOT Open Access | Genetic diversity and distribution patterns of PfEMP1 in Plasmodium falciparum isolates along the Thai-Myanmar border

May 26, 2021 - 14:25 -- NOT Open Access
Author(s): 
Sirisabhabhorn K, Chaicharoenkul W, Muhamad P, Na-Bangchang K
Reference: 
Parasitol Int. 2021 May 22:102397

Duffy binding-like domain (DBL) and cysteine-rich interdomain region (CIDR) domain genes of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) encode malaria virulence proteins. The variants of these genes have been reported to be associated with severe/complicated malaria. The present study investigated the prevalence and distribution patterns of DBLα0.6/9, DBLα1.1, DBLα1 not var3 genes, DBLα2/α1.1/2/4/7, DBLβ12 & DBLβ3/5, DBLε8, CIDRα1.4, and CIDRα1.6 of P. falciparum isolates along the Thai-Myanmar border.

Structure-Guided Design of a Synthetic Mimic of an Endothelial Protein C Receptor-Binding PfEMP1 Protein

January 12, 2021 - 15:06 -- Open Access
Author(s): 
Barber NM, Lau CKY, Turner L, Watson G, Thrane S, Lusingu JPA, Lavstsen T, Higgins MK
Reference: 
mSphere. 2021 Jan 6;6(1):e01081-20

Structure-guided vaccine design provides a route to elicit a focused immune response against the most functionally important regions of a pathogen surface. This can be achieved by identifying epitopes for neutralizing antibodies through structural methods and recapitulating these epitopes by grafting their core structural features onto smaller scaffolds. In this study, we conducted a modified version of this protocol. We focused on the PfEMP1 protein family found on the surfaces of erythrocytes infected with Plasmodium falciparum A subset of PfEMP1 proteins bind to endothelial protein C receptor (EPCR), and their expression correlates with development of the symptoms of severe malaria.

Longitudinal analysis of naturally acquired PfEMP1 CIDR domain variant antibodies identifies associations with malaria protection

May 21, 2020 - 06:21 -- Open Access
Author(s): 
Obeng-Adjei N, Larremore DB, Tran TM, et al.
Reference: 
JCI Insight. 2020 May 19:137262

Malaria pathogenicity is determined, in part, by the adherence of Plasmodium falciparum infected erythrocytes to the microvasculature mediated via specific interactions between PfEMP1 variant domains to host endothelial receptors. Naturally acquired antibodies against specific PfEMP1 variants can play an important role in clinical protection against malaria.

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