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001-es BibID:BIBFORM068923
Első szerző:Antal-Szalmás Péter (laboratóriumi szakorvos)
Cím:Spare CD14 molecules on human monocytes enhance the sensitivity for low LPS concentrations / Antal-Szalmás Péter, Poppelier Miriam J. J. G, Sümegi Andrea, van der Bruggen Tjomme, Verhoef Jan, van Kessel Kok P. M., van Strijp Jos A. G
Dátum:2004
ISSN:0165-2478
Megjegyzések:Human monocytes express on their plasma membrane relatively large number of CD14 molecules, known to play a crucial role in thelipopolisaccharide (LPS)-mediated cellular activation. Indirect data (J. Biol. Chem. 270 (1995) 9904) suggest that not all of these CD14molecules participate in LPS-signaling, but the importance of these spare receptors and the exact number of CD14 involved in activation upondifferent LPS-stimuli is not known. Using different concentrations of a blocking anti-CD14 monoclonal antibody (mAb 60bca) we createdmonocytes with graded amounts of CD14. The exact number of occupied and free receptors was quantitated by flow cytometry and specialmAb-labeled standard beads. The number of free CD14 molecules per monocyte in the presence of 10, 3.33, 0.73, 0.25 and 0.041 g/mlmAb was 0, 13 100, 49 300, 97 700 and 165 900. Stimulation of these partially blocked monocytes with 0.1, 1, 10 and 100 ng/ml ReLPS inthe presence of 3% human serum revealed that already 13 100 and 97 700 CD14 molecules provided a maximal Tumor necrosis factor (TNF ) mRNA response using 100 and 10 ng/ml ReLPS, while the activation totally depended on the number of available CD14 moleculesin the case of 1 and 0.1 ng/ml ReLPS. Our data imply that the number of CD14 molecules available for LPS-binding influence the cellularresponse. In the presence of higher concentrations of LPS only fractions of CD14 participate in the cell activation, while the presence of thespare receptors enhance the sensitivity against lower LPS amounts.
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
CD14
Megjelenés:Immunology Letters 93 : 1 (2004), p. 11-15. -
További szerzők:Poppelier, Miriam J. J. G Sümegi Andrea (1969-) (biológus) van der Bruggen, Tjomme Verhoef, Jan Kessel, Kok P. M., van Strijp, Jos A. G., van
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Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM037557
Első szerző:Vida András (molekuláris biológus, genetikus)
Cím:Fusion of the Fc part of human IgG1 to CD14 enhances its binding to gram-negative bacteria and mediates phagocytosis by Fc receptors of neutrophils / András Vida, Bart Bardoel, Fin Milder, László Majoros, Andrea Sümegi, Attila Bácsi, György Vereb, Kok P. M. van Kessel, Jos A. G. van Strijp, Péter Antal-Szalmás
Dátum:2012
ISSN:0165-2478
Megjegyzések:Microbial resistance to antimicrobial drugs is promoting a search for new antimicrobial agents that target highly conservative structures of pathogens. Human CD14 a known pattern recognition receptor (PRR) which recognizes multiple ligands from different microbes might be a worthy candidate. The aim of our work was to create a CD14/Fc dimer protein and evaluate its whole bacteria binding and opsonizing capabilities. Fusion of CD14 with the fragment crystallisable (Fc) part of human IgG1 could not only lead to an artificial opsonin but the dimerization through the Fc part might also increase its affinity to different ligands. Human CD14 and the Fc part of human IgG1 was fused and expressed in HEK293 cells. A histidine tagged CD14 (CD14/His) was also expressed as control. Using flow cytometry we could prove that CD14/Fc bound to whole Gram-negative bacteria, especially to short lipopolysaccharide (Ra and Re) mutants, and weak interaction was observed between the fusion protein and Listeria monocytogenes. Other Gram-positive bacteria and fungi did not show any association with CD14/Fc. CD14/His showed about 50-times less potent binding to Gram-negative bacteria. CD14/Fc acted as an opsonin and enhanced phagocytosis of these bacteria by neutrophil granulocytes, monocyte-derived macrophages and dendritic cells. Internalization of bacteria was confirmed by trypan blue quenching and confocal microscopy. On neutrophils the Fc part of the fusion protein was recognized by Fc receptors (CD16, CD32), as determined by blocking experiments. CD14/Fc enhanced the killing of bacteria in an ex vivo whole blood assay. Our experiments confirm that PRR/Fc fusion proteins can give a boost to FcR dependent phagocytosis and killing provided the antimicrobial part binds efficiently to microbes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
CD14
Fc
Gram-negative bacteria
Opsonization
Phagocytosis
Molekuláris Medicina
Megjelenés:Immunology Letters. - 146 : 1-2 (2012), p. 31-39. -
További szerzők:Bardoel, Bart Milder, Fin Majoros László (1966-) (szakorvos, klinikai mikrobiológus) Sümegi Andrea (1969-) (biológus) Bácsi Attila (1967-) (immunológus) Vereb György (1965-) (biofizikus, orvos) Kessel, Kok P. M., van Strijp, Jos A. G., van Antal-Szalmás Péter (1968-) (laboratóriumi szakorvos)
Pályázati támogatás:T046694
OTKA
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Celluláris hematológia - immunológia
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
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Intézményi repozitóriumban (DEA) tárolt változat
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