Surface display of the receptor-binding domain of the F17a-G fimbrial adhesin through the autotransporter AIDA-I leads to permeability of bacterial cells.
Surface display of the receptor-binding domain of the F17a-G fimbrial adhesin through the autotransporter AIDA-I leads to permeability of bacterial cells.
复制标题
F17a-G 菌毛粘附素的受体结合域通过自转运蛋白 AIDA-I 的表面展示导致细菌细胞的通透性。
作者：
Nani van Gerven;M. Sleutel;F. Deboeck;H. De Greve;J. Hernalsteens
Surface exposure of antigens on bacterial cells can be critical for eliciting an effective antibody response. Therefore, we investigated the cellular localization of the fimbrial F17a-G receptor-binding domain, fused to the translocator domain of the AIDA-I autotransporter. Synthesis of the fusion protein, under the control of the L-arabinose-inducible PBAD promoter, was shown to permeabilize Escherichia coli K-12 and Salmonella enterica serovar Typhimurium cells. The presence of permeable cells interfered with several methods that are typically used to determine surface exposure of proteins, such as protease treatment and whole-cell ELISA. Double immunofluorescence microscopy, using a second antibody directed against beta-galactosidase, a bacterial protein expressed in the cytoplasm, allowed the simultaneous detection of antigen expression and permeability in individual cells.
DOI：
10.1073/pnas.94.15.8168
发表时间：
1997-07-22
影响因子：
11.1
作者：
Siegele, DA;Hu, JC
通讯作者：
Hu, JC
影响因子：
56.9
作者：
Langermann, S;Palaszynski, S;Hultgren, SJ
通讯作者：
Hultgren, SJ