The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes
Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the recept...
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| Autor*in: |
Crawford, J. Adam [verfasserIn] Kaper, James B. [verfasserIn] |
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| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Science Ltd ; 2002 |
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Online-Ressource |
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| Reproduktion: |
2002 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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| Übergeordnetes Werk: |
In: Molecular microbiology - Oxford [u.a.] : Wiley-Blackwell, 1987, 46(2002), 3, Seite 0 |
| Übergeordnetes Werk: |
volume:46 ; year:2002 ; number:3 ; pages:0 |
| Links: |
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| DOI / URN: |
10.1046/j.1365-2958.2002.03214.x |
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| 520 | |a Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. | ||
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10.1046/j.1365-2958.2002.03214.x doi (DE-627)NLEJ24355513X DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 46(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:46 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03214.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 46 2002 3 0 |
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10.1046/j.1365-2958.2002.03214.x doi (DE-627)NLEJ24355513X DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 46(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:46 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03214.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 46 2002 3 0 |
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10.1046/j.1365-2958.2002.03214.x doi (DE-627)NLEJ24355513X DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 46(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:46 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03214.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 46 2002 3 0 |
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10.1046/j.1365-2958.2002.03214.x doi (DE-627)NLEJ24355513X DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 46(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:46 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03214.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 46 2002 3 0 |
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10.1046/j.1365-2958.2002.03214.x doi (DE-627)NLEJ24355513X DE-627 ger DE-627 rakwb Crawford, J. Adam verfasserin aut The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes Oxford, UK Blackwell Science Ltd 2002 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. 2002 Blackwell Publishing Journal Backfiles 1879-2005 |2002|||||||||| Kaper, James B. verfasserin aut In Molecular microbiology Oxford [u.a.] : Wiley-Blackwell, 1987 46(2002), 3, Seite 0 Online-Ressource (DE-627)NLEJ243926537 (DE-600)1501537-3 1365-2958 nnns volume:46 year:2002 number:3 pages:0 http://dx.doi.org/10.1046/j.1365-2958.2002.03214.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 46 2002 3 0 |
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One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. 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the n-terminus of enteropathogenic escherichia coli (epec) tir mediates transport across bacterial and eukaryotic cell membranes |
| title_auth |
The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes |
| abstract |
Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. |
| abstractGer |
Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. |
| abstract_unstemmed |
Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system to translocate into host cells several effector molecules that are required for virulence. One of these, the translocated intimin receptor, Tir, inserts into the host cell cytoplasmic membrane, where it functions as the receptor for intimin, an outer membrane adhesin expressed by EPEC. A chaperone for Tir, called CesT, is required for stability of Tir in the EPEC cytoplasm. In this study, the cyaA gene reporter system was used to identify domains in Tir that mediate secretion into the culture supernatant and translocation into host cells. A Tir–CyaA fusion containing the first 15 N-terminal residues of Tir was secreted and translocated into HeLa cells by a ΔtirΔcesT mutant; however, maximal secretion and translocation was observed with the first 26 N-terminal residues of Tir. Fusions containing progressively larger N-terminal sequences of Tir were also efficiently secreted and translocated into HeLa cells by the ΔtirΔcesT strain. However, in a Δtir mutant that expresses CesT, Tir26–CyaA and an additional fusion containing the first 69 N-terminal residues of Tir were not secreted or translocated, but fusions containing larger N-terminal Tir sequences were secreted and translocated by the Δtir mutant. Wild-type EPEC secreted and translocated the Tir15–CyaA fusion, whereas longer fusions, such as Tir26–CyaA and Tir69–CyaA, were translocated to higher levels, similar to what was observed with the ΔtirΔcesT mutant. A Tir–CyaA fusion containing the CesT binding domain was translocated into HeLa cells more rapidly in the presence of CesT compared with translocation in the absence of CesT. Collectively, these results suggest that an N-terminal domain of 26 amino acids functions as a CesT-independent signal that is capable of delivering Tir into both the culture supernatant and the cytosol of host cells. Furthermore, in addition to its role in the stability of Tir, CesT may function in translocation by mediating rapid delivery of Tir into host cells. |
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| title_short |
The N-terminus of enteropathogenic Escherichia coli (EPEC) Tir mediates transport across bacterial and eukaryotic cell membranes |
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http://dx.doi.org/10.1046/j.1365-2958.2002.03214.x |
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