Innate immunity protein Tag7 (PGRP-S) activates lymphocytes capable of Fasl-Fas-dependent contact killing of virus-infected cells.
IUBMB Life
; 69(12): 971-977, 2017 12.
Article
en En
| MEDLINE
| ID: mdl-29083508
ABSTRACT
The innate immunity protein Tag7 (PGRP-S, PGLYRP1) is involved in antimicrobial and antitumor defense. As shown in our previous studies, Tag7 specifically interacts with the major heat shock protein Hsp70 to form a stable Tag7-Hsp70 complex with cytotoxic activity against tumor cells. A stable complex of Tag7 with the calcium-binding protein Mts1 (S100A4) stimulates migration of lymphocytes. Moreover, Tag7 can activate cytotoxic lymphocytes that recognize and kill HLA-negative tumor cells. Here, we have shown that Tag 7 treatment of human peripheral blood mononuclear cells (PBMCs) results in activation of different cytotoxic lymphocyte populations-natural killer (NK) cells and CD8+ NKG2D+ T lymphocytes-that kill Moloney murine leukemia virus (MMLV) infected SC-1 cells using different mechanisms of cell death induction. This mechanism in NK cells is based on the release of granzymes, which activate apoptosis in target cells, while CD8+ NKG2D+ T lymphocytes recognize the noncanonical MicA antigen on the surface of virus-containing cells and kill them via the FasL-Fas interaction, triggering the apoptotic or necroptotic cell death pathway. Preliminary incubation of PBMCs with virus-infected cells and following incubation with Tag7 results in activation of lymphocytes with a different phenotype. These lymphocytes change the spectrum of target cells and the mechanism of cell death induction, and their interaction with target cells is not species-specific. © 2017 IUBMB Life, 69(12)971-977, 2017.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Células Asesinas Naturales
/
Linfocitos T Citotóxicos
/
Citocinas
/
Receptor fas
/
Citotoxicidad Inmunológica
/
Proteína Ligando Fas
Idioma:
En
Revista:
IUBMB Life
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Año:
2017
Tipo del documento:
Article
País de afiliación:
Rusia