Pregled bibliografske jedinice broj: 7479
Immune evasion potential of the murine cytomegalovirus gene m04
Immune evasion potential of the murine cytomegalovirus gene m04 // Immunology Letters (Abstract Issue) / Wagner, Hermann ; Heeg, H. ; Pfeffer, Klaus (ur.).
Amsterdam: Elsevier, 1997. str. 354-355 (predavanje, međunarodna recenzija, sažetak, znanstveni)
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Naslov
Immune evasion potential of the murine cytomegalovirus gene m04
Autori
Lučin, Pero ; Kučić, Natalia ; Crnković, Irena ; Jonjić, Stipan ; Koszinowski, Ulrich H.
Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni
Izvornik
Immunology Letters (Abstract Issue)
/ Wagner, Hermann ; Heeg, H. ; Pfeffer, Klaus - Amsterdam : Elsevier, 1997, 354-355
Skup
13th European Immunology Meeting
Mjesto i datum
Amsterdam, Nizozemska, 22.06.1997. - 25.06.1997
Vrsta sudjelovanja
Predavanje
Vrsta recenzije
Međunarodna recenzija
Ključne riječi
murine cytomegalovirus; viral genes; cytomegalovirus glycoprotein; MHC class I molecules; immune evasion; NK cells
Sažetak
Introduction: Two glycoprotein families are located at the oposite ends of murine cytomegalovirus (MCMV) genome. The m02 glycoprotein family has 15 members, and at least two of them potentially interfere with antigen presentation in the MHC class I pathway. The glycoprotein of 34 kDa encoded by the m04 gene was identified by coprecipitation with MHC class i molecules from the cell surface in the IFN-gamma treated fibroblasts. Materials and Methods: Glycoprotein maruration was studied by immunoprecipitation after metabolic labelling. Cell surface expression was followed by immunoflorescence and cell surface biotinylation. Recombinant viruses were produced using cre-loxP recombination system and selected on the basis of lacZ gene exspression. Biological relevance of m04 gene was tested in vivo after infection of immunodeficient nu/nu mice and immunocompetent C57B1/6 mice. Results: gp 34 is a type 1 glycoprotein with 5 potential glycosylation sites and 3 N-linked glycand. In cells exspressing MHC class I trimolecular complexes, a proportion og the gp34 binds to MHC and is exported to the cell surface. gp34 molecules exported to the cell surface acquire only one endoH resistant N-linked glycand. If gp34 is expressed in Ň-2 microglobulin deficient cells, it does not bind to MHC class I heavy chains. In these cells the gp34 does not acquire endoH resistance glycans and cannotbe exported to the cell surface without MHC class I trimolecular complexes. Experimets with MCMV-mutant in which the gp 34 is deleted have shown that m04 gene is neither responsible for the MHC class I transport block nor for backsorting of the cell surface resident MHC molecules. The immune evasion potential of the gp34 is tested in vivo by comparing virulence and organ replication of the wild type MCMV, the m04 deletion mutant and revertant virus. These studies are currently under way.
Izvorni jezik
Engleski
Znanstvena područja
Temeljne medicinske znanosti
POVEZANOST RADA
Ustanove:
Medicinski fakultet, Rijeka