Complexes of HLA-G protein on the cell surface are important for leukocyte Ig-like receptor-1 function.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F03%3A23033071" target="_blank" >RIV/68378050:_____/03:23033071 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Complexes of HLA-G protein on the cell surface are important for leukocyte Ig-like receptor-1 function.

Popis výsledku v původním jazyce

The nonclassical class I MHC molecule HLA-G is selectively expressed on extravillous cytotrophoblast cells. HLA-G can inhibit the killing mediated by NK cells via interaction with the inhibitory NK cell receptor LIR-1. Comparison of the sequence of the HLA-G molecule to other class I MHC proteins revealed two unique cysteine residues 42 and 147. Mutating these cysteine residues resulted in a dramatic decrease in LIR-1 Ig binding. The mutated HLA-G transfectants were less effective in the inhibition of NK killing. The involvement of the cysteine residues in the formation of HLA-G protein oligomers was demonstrated. The cysteine residue 42 is critical for the expression of such complexes. These oligomers, unique among the class I MHC proteins, probably bind to LIR-1 with increased avidity, resulting in an enhanced inhibitory function of LIR-1 and an impaired killing function of NK cells.

Název v anglickém jazyce

Complexes of HLA-G protein on the cell surface are important for leukocyte Ig-like receptor-1 function.

Popis výsledku anglicky

The nonclassical class I MHC molecule HLA-G is selectively expressed on extravillous cytotrophoblast cells. HLA-G can inhibit the killing mediated by NK cells via interaction with the inhibitory NK cell receptor LIR-1. Comparison of the sequence of the HLA-G molecule to other class I MHC proteins revealed two unique cysteine residues 42 and 147. Mutating these cysteine residues resulted in a dramatic decrease in LIR-1 Ig binding. The mutated HLA-G transfectants were less effective in the inhibition of NK killing. The involvement of the cysteine residues in the formation of HLA-G protein oligomers was demonstrated. The cysteine residue 42 is critical for the expression of such complexes. These oligomers, unique among the class I MHC proteins, probably bind to LIR-1 with increased avidity, resulting in an enhanced inhibitory function of LIR-1 and an impaired killing function of NK cells.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EC - Imunologie

OECD FORD obor

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Projekt

<a href="/cs/project/LN00A026" target="_blank" >LN00A026: Centrum molekulární a buněčné imunologie</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2003

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Immunology

ISSN

0022-1767

e-ISSN

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Svazek periodika

171

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

4

Strana od-do

1343-1351

Kód UT WoS článku

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EID výsledku v databázi Scopus

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