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erythrocyte membrane

Effect of malaria parasite shape on its alignment at erythrocyte membrane

July 21, 2021 - 18:10 -- Open Access
Author(s): 
Dasanna AK, Hillringhaus S, Gompper G, Fedosov DA
Reference: 
Elife. 2021 Jul 21;10:e68818

During the blood stage of malaria pathogenesis, parasites invade healthy red blood cells (RBC) to multiply inside the host and evade the immune response. When attached to RBC, the parasite first has to align its apex with the membrane for a successful invasion. Since the parasite's apex sits at the pointed end of an oval (egg-like) shape with a large local curvature, apical alignment is in general an energetically un-favorable process.

4D analysis of malaria parasite invasion offers insights into erythrocyte membrane remodeling and parasitophorous vacuole formation

June 23, 2021 - 13:37 -- Open Access
Author(s): 
Geoghegan ND, Evelyn C, Rogers KL, et al.
Reference: 
Nat Commun. 2021 Jun 15;12(1):3620

Host membrane remodeling is indispensable for viruses, bacteria, and parasites, to subvert the membrane barrier and obtain entry into cells. The malaria parasite Plasmodium spp. induces biophysical and molecular changes to the erythrocyte membrane through the ordered secretion of its apical organelles. To understand this process and address the debate regarding how the parasitophorous vacuole membrane (PVM) is formed, we developed an approach using lattice light-sheet microscopy, which enables the parasite interaction with the host cell membrane to be tracked and characterized during invasion.

Antibody Levels to Plasmodium falciparum Erythrocyte Membrane Protein 1-DBLgamma11 and DBLdelta-1 Predict Reduction in Parasite Density

June 16, 2021 - 14:53 -- Open Access
Author(s): 
Araj BN, Swihart B, Fried M, et al.
Reference: 
mSystems. 2021 Jun 15:e0034721

Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a variant surface antigen family expressed on infected red blood cells that plays a role in immune evasion and mediates adhesion to vascular endothelium. PfEMP1s are potential targets of protective antibodies as suggested by previous seroepidemiology studies. Here, we used previously reported proteomic analyses of PfEMP1s of clinical parasite isolates collected from Malian children to identify targets of immunity.

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
Author(s): 
Castro-Salguedo C, Mendez-Cuadro D, Moneriz C
Reference: 
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
Author(s): 
Padilla A, Dovell S, Chesnokov O, Hoggard M, Oleinikov AV, Marí F
Reference: 
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
Author(s): 
Hillringhaus S, Dasanna AK, Gompper G, Fedosov DA
Reference: 
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
Author(s): 
Charlotte Harmsen, Louise Turner, Susan Thrane, Adam F. Sander, Thor G. Theander and Thomas Lavstsen
Reference: 
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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