作为新型细菌黏附素支架的自转运蛋白：展示Jun/Fos二聚化结构域的大肠杆菌细胞的表面特性
Autotransporters as scaffolds for novel bacterial adhesins: surface properties of Escherichia coli cells displaying Jun/Fos dimerization domains.
作者信息
Veiga Esteban, de Lorenzo Víctor, Fernández Luis Angel
机构信息
Department of Microbial Biotechnology, Centro Nacional de Biotecnología CSIC, Campus de Cantoblanco, 28049 Madrid, Spain.
出版信息
J Bacteriol. 2003 Sep;185(18):5585-90. doi: 10.1128/JB.185.18.5585-5590.2003.
Abstract
Hybrid proteins containing the beta-autotransporter domain of the immunoglobulin A (IgA) protease of Neisseria gonorrhoea (IgA beta) 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 Jun beta sequence flocculated shortly after induction of the hybrid protein. E. coli cells expressing separately Fos beta 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.
摘要
含有淋病奈瑟菌免疫球蛋白A（IgA）蛋白酶的β-自转运结构域（IgAβ）以及真核转录因子Fos和Jun的伴侣亮氨酸拉链的杂合蛋白在大肠杆菌中表达。此类融合蛋白将亮氨酸拉链模块靶向至细胞表面。诱导杂合蛋白后不久，展示Junβ序列的细胞发生絮凝。分别表达Fosβ和Junβ嵌合体的大肠杆菌细胞形成了稳定的细菌联合体。这些联合体通过匹配的二聚化结构域之间的蛋白质-蛋白质相互作用所导致的紧密细胞间连接而物理性地维系在一起。文中讨论了自转运蛋白在新粘附素出现过程中的作用。
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Autotransporters as scaffolds for novel bacterial adhesins: surface properties of Escherichia coli cells displaying Jun/Fos dimerization domains.作为新型细菌黏附素支架的自转运蛋白：展示Jun/Fos二聚化结构域的大肠杆菌细胞的表面特性
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