Cutting edge: Outer membrane protein A (OmpA) binds to and activates human macrophages

被引：75

作者：

Soulas, C ^{[1
]}

Baussant, T ^{[1
]}

Aubry, JP ^{[1
]}

Delneste, Y ^{[1
]}

Barillat, N ^{[1
]}

Caron, G ^{[1
]}

Renno, T ^{[1
]}

Bonnefoy, JY ^{[1
]}

Jeannin, P ^{[1
]}

机构：

[1] Ctr Immunol Pierre Fabre, F-74164 St Julien En Genevois, France

来源：

JOURNAL OF IMMUNOLOGY | 2000年 / 165卷 / 05期

关键词：

D O I：

10.4049/jimmunol.165.5.2335

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Outer membrane protein (Omp)A is highly represented and conserved in the Enterobacteriaceae family. Using a recombinant OmpA From Klehsiella pneumoniae (P40), we have analyzed the interaction between OmpA and macrophages. We report that Alexa(488)-labeled P40 binds (at 4 degreesC) to murine and human macrophages in a dose-dependent manner and is rapidly internalized (at 37 degreesC), No binding or internalization of the Alexa(488)-labeled glycophorin A control protein is observed under the same conditions, Furthermore, P40 up-regulates the production of IL-1 beta, IL-8, IL-10, IL-12, and TNF-alpha by human macrophages and of NO by the RAW 264.7 murine macrophage cell line, P40 also synergizes with IFN-gamma and suboptimal concentrations of LPS to up-regulate the production of these mediators. In conclusion, P40 binds to and activates macrophages, These data suggest that recognition of OmpA by macrophages may be an initiating event in the antibacterial host response.

引用

页码：2335 / 2340

页数：6

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