Autotransporters as scaffolds for novel bacterial adhesins:: Surface properties of Escherichia coli cells displaying Jun/Fos dimerization domains

被引：34

作者：

Veiga, E ^{[1
]}

de Lorenzo, V ^{[1
]}

Fernández, LA ^{[1
]}

机构：

[1] CSIC, Ctr Nacl Biotecnol, Dept Microbial Biotechnol, E-28049 Madrid, Spain

来源：

JOURNAL OF BACTERIOLOGY | 2003年 / 185卷 / 18期

关键词：

D O I：

10.1128/JB.185.18.5585-5590.2003

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Hybrid proteins containing the beta-autotransporter domain of the immunoglobulin A (IgA) protease of Neisseria gonorrhoea (IgAbeta) and the partner leucine zippers of the eukaryotic transcriptional factors Fos and Jun were expressed in Escherichia coli. Such fusion proteins targeted the leucine zipper modules to the cell surface. Cells displaying the Junbeta sequence flocculated shortly after induction of the hybrid protein. E. coli cells expressing separately Fosbeta and Junbeta chimeras formed stable bacterial consortia. These associations were physically held by tight intercell ties caused by the protein-protein interactions of matching dimerization domains. The role of autotransporters in the emergence of new adhesins is discussed.

引用

页码：5585 / 5590

页数：6

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