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Type III secretion of EspB in enterohemorrhagic Escherichia coli O157:H7

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Abstract

EspB of enterohemorrhagic Escherichia coli O157:H7 is one of the type III proteins, categorized as translocators, that are secreted in abundance. To define the secretion determinants, different fragments of EspB were fused in recombinant proteins and the proteins secreted into media analyzed by Western blot. The results indicated that the C-terminal 30 residues of EspB were dispensable for secretion whereas the N-terminal first 117 residues played a major role. However, this N-terminal segment alone was not sufficient to confer the secretion. To acquire basic activity, the EspB fusion protein had to contain the N-terminal segment and another segment consisting of either residues 118–190 or residues 191–282. It is possible that the N-terminal region may act as the primary component of the secretion signal while other determinants help to maintain a conformation of EspB favorable for secretion. However, alternative mechanisms cannot be completely excluded. Not withstanding this, the signal for the type III secretion of EspB is apparently distinct from those previously described for the secretion of effector proteins such as Yops in Yersinia.

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Acknowledgements

This research was supported in parts by grant 89-B-FA22-2-4 (Program for Promoting Academic Excellence of Universities) from the Department of Education and grants NSC 89-2320-B010-105 and NSC 90-2320-B-010-053 from the National Science Council, Taiwan, ROC.

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Correspondence to Wan-Jr Syu.

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Chiu, HJ., Lin, WS. & Syu, WJ. Type III secretion of EspB in enterohemorrhagic Escherichia coli O157:H7. Arch Microbiol 180, 218–226 (2003). https://doi.org/10.1007/s00203-003-0579-7

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  • DOI: https://doi.org/10.1007/s00203-003-0579-7

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