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erythrocyte membrane

NOT Open Access | Erythrocyte membrane proteins involved in the immune response to Plasmodium falciparum and Plasmodium vivax infection

April 7, 2021 - 11:58 -- NOT Open Access
Castro-Salguedo C, Mendez-Cuadro D, Moneriz C
Parasitol Res. 2021 Apr 2

Invasion of Plasmodium into the red blood cell involves the interactions of a substantial number of proteins, with red cell membrane proteins as the most involved throughout the process from entry to exit. The objective of this work was to identify proteins of the human erythrocyte membrane capable of generating an antigenic response to P. falciparum and P. vivax infection, with the goal of searching for new molecular targets of interest with an immunological origin to prevent Plasmodium infection.

NOT Open Access | Conus venom fractions inhibit the adhesion of Plasmodium falciparum erythrocyte membrane protein 1 domains to the host vascular receptors

December 30, 2020 - 13:38 -- NOT Open Access
Padilla A, Dovell S, Chesnokov O, Hoggard M, Oleinikov AV, Marí F
J Proteomics. 2020 Dec 26:104083

Using high-throughput BioPlex assays, we determined that six fractions from the venom of Conus nux inhibit the adhesion of various recombinant PfEMP-1 protein domains (PF08_0106 CIDR1α3.1, PF11_0521 DBL2β3, and PFL0030c DBL3X and DBL5e) to their corresponding receptors (CD36, ICAM-1, and CSA, respectively). The protein domain-receptor interactions permit P. falciparum-infected erythrocytes (IE) to evade elimination in the spleen by adhering to the microvasculature in various organs including the placenta. The sequences for the main components of the fractions, determined by tandem mass spectrometry, yielded four T-superfamily conotoxins, one (CC-Loop-CC) with I-IV, II-III connectivity and three (CC-Loop-CXaaC) with a I-III, II-IV connectivity.

Stochastic bond dynamics facilitates alignment of malaria parasite at erythrocyte membrane upon invasion

May 19, 2020 - 15:29 -- Open Access
Hillringhaus S, Dasanna AK, Gompper G, Fedosov DA
Elife. 2020 May 18;9. pii: e56500

Malaria parasites invade healthy red blood cells (RBCs) during the blood stage of the disease. Even though parasites initially adhere to RBCs with a random orientation, they need to align their apex toward the membrane in order to start the invasion process. Using hydrodynamic simulations of a RBC and parasite, where both interact through discrete stochastic bonds, we show that parasite alignment is governed by the combination of RBC membrane deformability and dynamics of adhesion bonds.

Immunization with virus-like particles conjugated to CIDRα1 domain of Plasmodium falciparum erythrocyte membrane protein 1 induces inhibitory antibodies

March 31, 2020 - 15:57 -- Open Access
Charlotte Harmsen, Louise Turner, Susan Thrane, Adam F. Sander, Thor G. Theander and Thomas Lavstsen
Malaria Journal 2020 19:132, 30 March 2020

During the erythrocytic cycle, Plasmodium falciparum malaria parasites express P. falciparum Erythrocyte Membrane Protein 1 (PfEMP1) that anchor the infected erythrocytes (IE) to the vascular lining of the host. The CIDRα1 domain of PfEMP1 is responsible for binding host endothelial protein C receptor (EPCR), and increasing evidence support that this interaction triggers severe malaria, accounting for the majority of malaria-related deaths. In high transmission regions, children develop immunity to severe malaria after the first few infections. This immunity is believed to be mediated by antibodies targeting and inhibiting PfEMP1, causing infected erythrocytes to circulate and be cleared in the spleen. The development of immunity to malaria coincides with acquisition of broad antibody reactivity across the CIDRα1 protein family. Altogether, this identifies CIDRα1 as an important vaccine target. However, the antigenic diversity of the CIDRα1 domain family is a challenge for vaccine development.

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