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РЖ ВИНИТИ 34 (BI39) 97.03-04К1.75

Antigen topography is critical for interaction of IgG2 anti-red-cell antibodies with Fc'гамма' receptors [Text] / Belinda M. Kumpel [et al.] // Brit. J. Haematol. - 1996. - Vol. 94, N 1. - P175-183 . - ISSN 0007-1048
Перевод заглавия: Топография антигена является критическим для взаимодействия антитела IgG2 против эритроцитов с рецептором Fc'гамма'
Аннотация: IgG antibodies to the Rh D polypeptide on red cells are normally IgG1 or IgG3, whereas antibodies produced in response to carbohydrate antigens such as the A and B blood groups are predominantly IgG2. The consequences of this isotype restriction for the immune destruction of red cells were investigated. Human IgG2 anti-D and IgG2 anti-A were isolated by affinity purification from an unusual anti-D serum (DEL) and anti-A sera, respectively. These antibodies were compared with IgG1 and IgG3 monoclonal anti-D in in vitro functional assays of the interaction between IgG-coated red cells (EA-IgG) and cells bearing IgG Fc receptors (Fc'гамма'R). Dimeric IgG2 anti-D bound efficiently to cell lines transfected with Fc'гамма'RIIa-H131, an allotypic form of Fc'гамма'RIIa which readily interacts with IgG2, IgG1 and IgG3. Unexpectedly, however, -D-phenotype red cells coated with IgG2 anti-D did not form rosettes with these cells, whereas EA-IgG2 anti-A and EA-IgG1 and EA-IgG3 anti-D effectively formed rosettes with these transfectants at the same sensitization level. In antibody-dependent cell-mediated cytotoxicity (ADCC) assays, lysis of EA-IgG2 anti-A was mediated via Fc'гамма'RIIa, whereas lysis of EA-IgG1 and EA-IgG3 anti-D was mediated via Fc'гамма'RI or Fc'гамма'RIII; EA-IgG2 anti-D was inactive in all functional assays. These experiments suggest that both IgG subclass and antigen structure affect functional IgG-Fc'гамма'R interactions. The topography of the Rh D antigen, ensures that anti-D is bound near the lipid bilayer surrounded by the glycocalyx. This may sterically hinder access of Fc'гамма'RIIa-H131 to the Fc'гамма'R recognition site on the relatively inflexible IgG2 anti-D, but not to that of IgG1 or IgG3 anti-D. In contrast, IgG2 bound to the A antigen on glycoproteins is not so constrained. The topography of the D and A antigens may thus determine whether functional interactions of red-cell-bound IgG2 anti-D and IgG2 anti-A with cells bearing Fc'гамма' receptors can occur. Великобритания, International Blood Groop Reference Lab., Bristol. Библ. 48

ГРНТИ	34.43.33

ВИНИТИ 341.43.33.05
Рубрики: АНТИГЕНЫ ЭРИТРОЦИТОВ
ВЗАИМОДЕЙСТВИЕ С IGG2 АНТИТЕЛАМИ
ЗНАЧЕНИЕ ЛОКАЛИЗАЦИИ АНТИГЕНА
РОЛЬ РЕЦЕПТОРОВ FC ГАММА
ЧЕЛОВЕК

Доп.точки доступа:
Kumpel, Belinda M.; van, de Winkel Jan G.J.; Westerdaal, Nomdo A.C.; Hadley, Andrew G.; Dugoujon, J.Michel; Blancher, Antoine

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