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erythrocyte

Not Open Access | PI(3)P-independent and -dependent pathways function together in a vacuolar translocation sequence to target malarial proteins to the host erythrocyte

October 1, 2012 - 17:14 -- Patrick Sampao
Author(s): 
Souvik Bhattacharjee, Kaye D. Speicher, Robert V. Stahelin, David W. Speicher, Kasturi Haldar
Reference: 
Molecular and Biochemical Parasitology, Volume 185, Issue 2, October 2012, Pages 106-113

MalariaWorldWe have previously shown that the R to A mutation in the HT motif, abrogates VTS binding to PI(3)P (Kd > 5 μM). We now show that remarkably, the R to A mutant is exported to the host erythrocyte, for both membrane and soluble reporters, although the efficiency of export is reduced to ∼30% of that seen with a complete VTS.

Medical Condition: 

Molecular interactions and signaling mechanisms during erythrocyte invasion by malaria parasites

October 19, 2011 - 09:09 -- Patrick Sampao
Author(s): 
Deepak Gaur, Chetan E Chitnis
Reference: 
Current Opinion in Microbiology, Volume 14, Issue 4, August 2011, Pages 422-428

MalariaWorldHere, we review recent studies on interactions between erythrocyte binding antigens (EBA) and PfRH proteins from the parasite and erythrocyte receptors involved in invasion.

Structural Characterization of the Erythrocyte Binding Domain of the Reticulocyte Binding Protein Homologue Family of Plasmodium yoelii

June 22, 2011 - 14:17 -- Patrick Sampao
Author(s): 
Ardina Grüber, Karthigayan Gunalan, Jeya Kumar Ramalingam, Malathy S. S. Manimekalai, Gerhard Grüber, and Peter R. Preiser
Reference: 
Infect. Immun., Jul 2011; 79: 2880 - 2888.

In the study described here, we delineated the erythrocyte binding domain (EBD) of one member of the RH family, termed Py235, from Plasmodium yoelii.

Parasite-encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum-infected erythrocyte

September 14, 2010 - 07:31 -- Patrick Sampao
Author(s): 
Simone K., Melanie R., et al.
Reference: 
Cellular Microbiology, Vol 12, Issue 10, pg 1398–1420, Oct 2010

Here, we have generated transfectant lines expressing GFP- or HA-Strep-tagged versions of these proteins, and used these to investigate both localization and other properties of these Hsp40 co-chaperones.

Medical Treatment: 

Open Access | Plasmodium falciparum FIKK Kinase Members Target Distinct Components of the Erythrocyte Membrane

July 29, 2010 - 11:46 -- Kabogo Ndegwa
Author(s): 
Marta C. Nunes, Mami Okada, Christine Scheidig-Benatar, Brian M. Cooke, Artur Scherf
Reference: 
PLoS ONE 5(7): e11747

Our results suggest that FIKK members phosphorylate different membrane skeleton proteins of the infected erythrocyte in a stage-specific manner, inducing alterations in the mechanical properties of the parasite-infected red blood cell.

Targeting glutathione by dimethylfumarate protects against experimental malaria by enhancing erythrocyte cell membrane scrambling

July 19, 2010 - 12:44 -- Kabogo Ndegwa
Author(s): 
M Ghashghaeinia, D Bobbala, T Wieder, S Koka, J ück, B Fehrenbacher, M Rocken, M Schaller, F Lang, K Ghoreschi
Reference: 
Am J Physiol Cell Physiol (July 14, 2010)

The balance between GSH-levels and oxidative stress is critical for cell survival. The GSH-levels of erythrocytes are dramatically decreased during infection with Plasmodium spp.

Prevalence of 5′ insertion mutants and analysis of single nucleotide polymorphism in the erythrocyte binding-like 1 (ebl-1) gene in Kenyan Plasmodium falciparum field isolates

June 30, 2010 - 15:11 -- Patrick Sampao
Author(s): 
Elijah K. Githui, David S. Peterson, Rashid A. Aman, Abdirahman I. Abdi
Reference: 
Infection, Genetics and Evolution, Volume 10, Issue 6, August 2010, Pages 833-838

This study is now extended to include field isolates collected from sites within Kenya. DNA isolated from blood samples of infected patients was utilized to amplify the region I sequence of ebl-1 gene in order to investigate polymorphism in the region immediately adjacent to the 5′ cysteine-rich domains, and to determine the prevalence of an insertion mutant that effectively knocks out the gene.

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Open Access | Complement Receptor 1 Is a Sialic Acid-Independent Erythrocyte Receptor of Plasmodium falciparum

June 29, 2010 - 09:50 -- Kabogo Ndegwa
Author(s): 
Carmenza Spadafora, Gordon A. Awandare, Karen M. Kopydlowski, Jozsef Czege, J. Kathleen Moch, Robert W. Finberg, George C. Tsokos, José A. Stoute
Reference: 
PLoS Pathog 6(6): e1000968

Plasmodium falciparum is a highly lethal malaria parasite of humans. A major portion of its life cycle is dedicated to invading and multiplying inside erythrocytes.

Medical Treatment: 

Open Access | Protein Kinase A Dependent Phosphorylation of Apical Membrane Antigen 1 Plays an Important Role in Erythrocyte Invasion by the Malaria Parasite

June 29, 2010 - 09:43 -- Kabogo Ndegwa
Author(s): 
Kerstin Leykauf, Moritz Treeck, Paul R. Gilson, Thomas Nebl, Thomas Braulke, Alan F. Cowman, Tim W. Gilberger, Brendan S. Crabb
Reference: 
PLoS Pathog 6(6): e1000941

Apicomplexan parasites are obligate intracellular parasites that infect a variety of hosts, causing significant diseases in livestock and humans. The invasive forms of the parasites invade their host cells by gliding motility, an active process driven by parasite adhesion proteins and molecular motors.

Open Access | Complement Receptor 1 Is a Sialic Acid-Independent Erythrocyte Receptor of Plasmodium falciparum

June 22, 2010 - 07:16 -- Kabogo Ndegwa
Author(s): 
Carmenza Spadafora, Gordon A. Awandare, Karen M. Kopydlowski, Jozsef Czege, J. Kathleen Moch, Robert W. Finberg, George C. Tsokos, José A. Stoute
Reference: 
PLoS Pathog 6(6): e1000968

Plasmodium falciparum is a highly lethal malaria parasite of humans. A major portion of its life cycle is dedicated to invading and multiplying inside erythrocytes. The molecular mechanisms of erythrocyte invasion are incompletely understood. P. falciparum depends heavily on sialic acid present on glycophorins to invade erythrocytes.

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