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Changes in the erythrocyte membrane induced by invasion allow cytoadhesion of infected erythrocytes (IEs) to the host endothelium, which can lead to severe complications. Binding to endothelial cell receptors (ECRs) is mainly mediated by members of the erythrocyte membrane protein 1 (EMP1) family, encoded by genes. Malaria infection causes several common symptoms, with fever being the most apparent. In this study, the effects of febrile conditions on cytoadhesion of predominately knobless erythrocytes infected with the laboratory isolate IT4 to chondroitin-4-sulfate A (CSA), intercellular adhesion molecule 1 (ICAM-1), and CD36 were investigated. IEs enriched for binding to CSA at 40 °C exhibited significantly increased binding capacity relative to parasites enriched at 37 °C. This interaction was due to increased expression and trafficking of the corresponding EMP1 to the IE surface as well as to a selection of knobby IEs. Furthermore, the enrichment of IEs to ICAM-1 at 40 °C also led to selection of knobby IEs over knobless IEs, whereas enrichment on CD36 did not lead to a selection. In summary, these findings demonstrate that knobs are crucial for parasitic survival in the host, especially during fever episodes, and thus, that selection pressure on the formation of knobs could be controlled by the host.
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http://dx.doi.org/10.3390/microorganisms8020174 | DOI Listing |
Disabil Rehabil Assist Technol
August 2022
Department of Rehabilitation Science and Technology, University of Pittsburgh, Pittsburgh, PA, USA.
Purpose: Rolling resistance is a drag force that increases the required propulsion force of manual wheelchair users (MWU) and increases the risk of upper extremity pain and injury.
Materials And Methods: To understand the influence of different design, environmental, and setup factors on rolling resistance (RR), a series of tests were performed on a range of wheels and casters using a drum-based equipment with the capability to measure RR forces. Independent factors were varied including load, camber, toe, speed, tire pressure, and surface, using ranges anticipated in the community.
Microorganisms
January 2020
Bernhard Nocht Institute for Tropical Medicine, 20359 Hamburg, Germany.
Changes in the erythrocyte membrane induced by invasion allow cytoadhesion of infected erythrocytes (IEs) to the host endothelium, which can lead to severe complications. Binding to endothelial cell receptors (ECRs) is mainly mediated by members of the erythrocyte membrane protein 1 (EMP1) family, encoded by genes. Malaria infection causes several common symptoms, with fever being the most apparent.
View Article and Find Full Text PDFBiochemistry
May 2004
Institut für Biochemie und Molekularbiologie I, Universitätsklinikum Hamburg-Eppendorf, Martinistrasse 52, D-20246 Hamburg, Germany.
MeCP2 has been identified as a chromatin-associated protein that recognizes MAR elements as well as methyl-CpGs. To characterize target sequences of MeCP2 in human cells, we employed two complementary methods. First, by use of a preparative chromatin immunoprecipitation protocol, we created from MCF7 cells a library enriched with sequences bound to MeCP2.
View Article and Find Full Text PDFSoutheast Asian J Trop Med Public Health
June 1998
Faculty of Science, Mahidol University, Bangkok, Thailand.
The tegument of bile-dwelling Fasciola gigantica is the interfacing layer that helps the parasite to maintain its homeostasis, and evade the hostile environment, including the host's immune attacks. The tegument is a syncytial layer about 10 mm thick, that is formed by the fusion of cytoplasmic processes of tegument cells, whose soma lie underneath the two muscle layers. The surface of the tegument is highly folded and invaginated into numerous ridges, pits and spines, which help to increase the surface area of the tegument for the absorption and exchanging of molecules, as well as for attachment.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
April 1987
Erythrocytes infected with a knobby variant of Plasmodium falciparum selectively bind IgG autoantibodies in normal human serum. Quantification of membrane-bound IgG, by use of 125I-labeled protein A, revealed that erythrocytes infected with the knobby variant bound 30 times more protein A than did noninfected erythrocytes; infection with a knobless variant resulted in less than a 2-fold difference compared with noninfected erythrocytes. IgG binding to knobby erythrocytes appeared to be related to parasite development, since binding of 125I-labeled protein A to cells bearing young trophozoites (less than 20 hr after parasite invasion) was similar to binding to uninfected erythrocytes.
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