Pas, a Novel Protein Required for Protein Secretion and Attaching and Effacing Activities of Enterohemorrhagic
            <i>Escherichia coli</i>

Kresse, Andreas U.; Schulze, Kai; Deibel, Christina; Ebel, Frank; Rohde, Manfred; Chakraborty, Trinad; Guzmán, Carlos A.

doi:10.1128/jb.180.17.4370-4379.1998

Cited by 40 publications

(42 citation statements)

References 62 publications

(65 reference statements)

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“…There was no evidence for this even though both were expressed inside the bacterial cell (data not shown). An indication of a potential mechanism to release Tir from SepL comes from previous research that has shown a direct interaction between Tir and EscD (Pas) (Kresse et al, 1998). EscD is considered to be a protein in the inner membrane complex of the T3S (Ogino et al, 2006) and when deleted prevents both translocon and effector protein secretion.…”

Section: Discussionmentioning

confidence: 99%

Hierarchal type III secretion of translocators and effectors from Escherichia coli O157:H7 requires the carboxy terminus of SepL that binds to Tir

Wang¹,

Roe²,

McAteer³

et al. 2008

Molecular Microbiology

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SummaryType III secretion (T3S) from enteric bacteria is a co-ordinated process with a hierarchy of secreted proteins. In enteropathogenic and enterohaemorrhagic Escherichia coli, SepL and SepD are essential for translocator but not effector protein export, but how they function to control this differential secretion is not known. This study has focused on the different activities of SepL including membrane localization, SepD binding, EspD export and Tir secretion regulation. Analyses of SepL truncates demonstrated that the different functions associated with SepL can be separated. In particular, SepL with a deletion of 11 amino acids from the C-terminus was able to localize to the bacterial membrane, export translocon proteins but not regulate Tir or other effector protein secretion. From the repertoire of effector proteins only Tir was shown to bind directly to full-length SepL and the C-terminal 48 amino acids of SepL was sufficient to interact with Tir. By synchronizing induction of T3S, it was evident that the Tir-binding capacity of SepL is important to delay the release of effector proteins while the EspADB translocon is secreted. The interaction between Tir and SepL is therefore a critical step that controls the timing of T3S in attaching and effacing pathogens.

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Section: Discussionmentioning

confidence: 99%

Hierarchal type III secretion of translocators and effectors from Escherichia coli O157:H7 requires the carboxy terminus of SepL that binds to Tir

Wang¹,

Roe²,

McAteer³

et al. 2008

Molecular Microbiology

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“…The LEE encodes an outer membrane protein called intimin (EaeA) which is required for intimate attachment to host cells, the secreted proteins EspA, EspD and EspB which are required for signal transduction events leading to the formation of A/E lesions, the EspE protein which, after translocation within the host cell, phosphorylation and surface display constitutes the intimin receptor, and a type III secretion system which is essential for the translocation of the proteins involved in the formation of A/E lesions [4^7]. We have recently iden-ti¢ed a protein, named Pas, which also plays an essential role during the infection process of EHEC, being involved in the secretion of Esp proteins [8].…”

Section: Introductionmentioning

confidence: 99%

“…To better understand the biology of EHEC, we have investigated the regulation of the expression of the pas gene. The pas gene is located between the eaeA and the predicted sepL genes [7,8], but is transcribed on the complementary DNA strand [4,8]. Our previous studies showed the presence of a putative 0378-1097 / 00 / $20.00 ß 2000 Federation of European Microbiological Societies.…”

Section: Introductionmentioning

confidence: 99%

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Transcriptional regulation of the pas gene of enterohemorrhagic Escherichia coli

Beltrametti

2000

FEMS Microbiology Letters

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The Pas protein plays a key role in the pathogenesis of enterohemorrhagic Escherichia coli (EHEC), being required for the secretion of the Esp proteins. Here, the transcriptional regulation of the pas gene was analyzed through the construction of a pas::lacZ translational fusion. When bacteria were grown in Luria Bertani medium or tissue culture medium supplemented with HEPES, a bimodal activation curve was observed. The early phase of induction was not significantly modified by the incubation temperature (either 25 or 37°C), whereas the second phase, which overlaps with the late exponential growth phase, was enhanced at 37°C. The early phase was also stimulated by growth on tissue culture medium and by the addition of Ca2+, Mn2+or Mg2+ to the M9‐glucose minimal medium. Primer extension analysis showed the presence of two major starts of transcription, which were located 58 and 60 bp upstream of the ATG‐start codon of the Pas protein, respectively. Although these sites are very close to each other, the transcripts produced during the early induction phase mainly start on the −60 position, whereas the −58 start was activated during the second induction phase.

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“…Cells were washed and incubated with gold labeled goat anti-rabbit serum (1:100) for 2 h at room temperature. To retain the bacteria/cell relationship, the coverslips were washed and then ¢xed in 2% glutaraldehyde, dehydrated and embedded in Spurr's resin using standard procedures [19]. The coverslips were removed bỳ popping' them o¡ after immersion in liquid nitrogen and the resulting monolayer sectioned.…”

Section: Immunoelectron Microscopymentioning

confidence: 99%

Erwinia chrysanthemi strains cause death of human gastrointestinal cells in culture and express an intimin-like protein

Duarté¹

2000

FEMS Microbiology Letters

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The bacterium Erwinia chrysanthemi is a model plant pathogen, responsible for causing cell death in plant tissue. Cell-wall depolymerizing enzymes and avirulence proteins essential for parasitism by this bacterium utilize dedicated type II and type III secretion systems, respectively. Although E. chrysanthemi is not recognized as a mammalian pathogen, we have observed that the bacterium can adhere to, cause an oxidative stress response in and kill cultured human adenocarcinoma cells. These bacteria express a surface protein that bears immunological identity to intimin, a protein required for full virulence of enterohemorrhagic and enteropathogenic Escherichia coli. A type III secretion mutant of E. chrysanthemi was observed to have a significantly lower capability of causing death than the wild-type strain in parallel cultures of human colon adenocarcinoma cells. These observations suggest that E. chrysanthemi has the potential to parasitize mammalian hosts as well as plants. ß

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Pas, a Novel Protein Required for Protein Secretion and Attaching and Effacing Activities of Enterohemorrhagic Escherichia coli

Cited by 40 publications

References 62 publications

Hierarchal type III secretion of translocators and effectors from Escherichia coli O157:H7 requires the carboxy terminus of SepL that binds to Tir

Hierarchal type III secretion of translocators and effectors from Escherichia coli O157:H7 requires the carboxy terminus of SepL that binds to Tir

Transcriptional regulation of the pas gene of enterohemorrhagic Escherichia coli

Erwinia chrysanthemi strains cause death of human gastrointestinal cells in culture and express an intimin-like protein

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