scholarly journals A Proteomic Study on the Membrane Protein Fraction of T Cells Confirms High Substrate Selectivity for the ER Translocation Inhibitor Cyclotriazadisulfonamide

2021 ◽  
pp. 100144
Author(s):  
Eva Pauwels ◽  
Claudia Rutz ◽  
Becky Provinciael ◽  
Joren Stroobants ◽  
Dominique Schols ◽  
...  
Keyword(s):  
T Cells ◽  
Membrane Protein ◽  
Protein Fraction ◽  
Substrate Selectivity ◽  
High Substrate ◽  
Proteomic Study

scholarly journals Neonatal and Maternal Immunological Responses to Conserved Epitopes within the DBL-γ3 Chondroitin Sulfate A-Binding Domain of Plasmodium falciparum Erythrocyte Membrane Protein 1

2005 ◽  
Vol 73 (12) ◽  
pp. 7988-7995 ◽  
Author(s):  
Kim Brustoski ◽  
Martin Kramer ◽  
Ulrike Möller ◽  
Peter G. Kremsner ◽  
Adrian J. F. Luty
Keyword(s):  
T Cells ◽  
Plasmodium Falciparum ◽  
Membrane Protein ◽  
Chondroitin Sulfate ◽  
Erythrocyte Membrane ◽  
Venous Blood ◽  
Binding Domain ◽  
Erythrocyte Membrane Protein ◽  
Conserved Regions ◽  
Chondroitin Sulfate A

ABSTRACT Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) mediates the adherence of P. falciparum-infected erythrocytes to placental syncytiotrophoblasts via interactions with chondroitin sulfate A (CSA), a characteristic of pregnancy-associated malaria. Pregnancy-associated malaria predicts increased susceptibility of newborns to malaria, and it is postulated that transplacental passage of parasite antigen induces immune regulatory activity in the neonate. We wished to examine the immune responsiveness to a CSA-binding domain of PfEMP1, the DBL-γ3 domain, in cord and maternal venous blood obtained from pregnancies with various histories of P. falciparum infection. We assessed in vitro T-cell cytokine and plasma immunoglobulin G (IgG) and IgM responses to four peptides corresponding to highly conserved regions of a DBL-γ3 domain common to central African parasite isolates. The presence of placental P. falciparum infection at delivery was associated with elevated frequencies of DBL-γ3 peptide-specific CD3+ interleukin-10-positive T cells in cord blood, while treatment and clearance of infection prior to delivery was associated with elevated frequencies of CD3+ gamma interferon-positive T cells. DBL-γ3 peptide-specific IgM antibodies were detected in 12 of 60 (20%) cord plasma samples from those born to mothers with P. falciparum infection during pregnancy. Consistent with polyclonal anti-PfEMP1 antibody responses that are associated with protection against pregnancy-associated malaria, the presence of maternal IgG antibodies with specificity for one of the DBL-γ3 peptides showed a parity-dependent profile. These data demonstrate that peptides corresponding to conserved regions of the DBL-γ3 domain of PfEMP1 are immunogenic in P. falciparum-infected mothers and their offspring.

scholarly journals Herpesvirus saimiri Tip-484 membrane protein markedly increases p56lck activity in T cells.

1997 ◽  
Vol 71 (1) ◽  
pp. 378-382 ◽  
Author(s):  
T Lund ◽  
M M Medveczky ◽  
P G Medveczky
Keyword(s):  
T Cells ◽  
Membrane Protein ◽  
Herpesvirus Saimiri

The relationships between Epstein-Barr virus latent membrane protein 1 and regulatory T cells in Hodgkin's lymphoma

2007 ◽  
Vol 35 (4) ◽  
pp. 596-604 ◽  
Author(s):  
Neil A. Marshall ◽  
Dominic J. Culligan ◽  
Jane Tighe ◽  
Peter W. Johnston ◽  
Robert N. Barker ◽  
...  
Keyword(s):  
T Cells ◽  
Regulatory T Cells ◽  
Membrane Protein ◽  
Epstein Barr Virus ◽  
Latent Membrane Protein ◽  
Hodgkin's Lymphoma ◽  
Latent Membrane Protein 1 ◽  
Barr Virus ◽  
Epstein Barr ◽  
Virus Latent Membrane Protein

scholarly journals Studies on membrane proteins involved in ribosome binding on the rough endoplasmic reticulum. Ribophorins have no ribosome-binding activity

1987 ◽  
Vol 245 (3) ◽  
pp. 811-819 ◽  
Author(s):  
H Yoshida ◽  
N Tondokoro ◽  
Y Asano ◽  
K Mizusawa ◽  
R Yamagishi ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Rat Liver ◽  
Concanavalin A ◽  
Protein Fraction ◽  
Proteolytic Enzymes ◽  
Binding Capacity ◽  
Liver Microsomes ◽  
Binding Activity ◽  
Rat Liver Microsomes ◽  
Ribosome Binding

A membrane protein fraction showing affinity for ribosomes was isolated from rat liver microsomes (microsomal fractions) in association with ribosomes by treatment of the microsomes with Emulgen 913 and then solubilized from the ribosomes with sodium deoxycholate. This protein fraction was separated into two fractions, glycoproteins, including ribophorins I and II, and non-glycoproteins, virtually free from ribophorins I and II, on concanavalin A-Sepharose columns. The two fractions were each reconstituted into liposomes to determine their ribosome-binding activities. The specific binding activity of the non-glycoprotein fraction was approx. 2.3-fold higher than that of the glycoprotein fraction. The recovery of ribosome-binding capacity of the two fractions was about 85% of the total binding capacity of the material applied to a concanavalin A-Sepharose column, and about 90% of it was found in the non-glycoprotein fraction. The affinity constants of the ribosomes for the reconstituted liposomes were somewhat higher than those for stripped rough microsomes. The mode of ribosome binding to the reconstituted liposomes was very similar to that to the stripped rough microsomes, in its sensitivity to proteolytic enzymes and its strong inhibition by increasing KCl concentration. These results support the idea that ribosome binding to rat liver microsomes is not directly mediated by ribophorins I and II, but that another unidentified membrane protein(s) plays a role in ribosome binding.

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