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| Title | Structure of lymphostatin, a large multi-functional virulence factor of pathogenic Escherichia coli. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 16, Issue 1, Page 5389, Year 2025 |
| Publish date | Jun 25, 2025 |
 Authors | Matthias Griessmann / Tim Rasmussen / Vanessa J Flegler / Christian Kraft / Ronja Schneider / Max Hateley / Lukas Spantzel / Mark P Stevens / Michael Börsch / Bettina Böttcher /   |
| PubMed Abstract | Lymphostatin is a key virulence factor of enteropathogenic and enterohaemorrhagic Escherichia coli, playing roles in bacterial colonisation of the gut and in the inhibition of lymphocyte ...Lymphostatin is a key virulence factor of enteropathogenic and enterohaemorrhagic Escherichia coli, playing roles in bacterial colonisation of the gut and in the inhibition of lymphocyte proliferation and proinflammatory responses. The protein's glycosyltransferase and cysteine protease motifs are required for activity against lymphocytes, but high-resolution structural information has proven elusive. Here, we describe the structure of lymphostatin from enteropathogenic E. coli O127:H6, determined by electron cryo-microscopy at different pH values. We observe three conformations of a highly complex molecule with two glycosyltransferase domains, one PaToxP-like protease domain, an ADP-ribosyltransferase domain, a vertex domain and a delivery domain. Long linkers hold these domains together and occlude the catalytic sites of the N-terminal glycosyltransferase and protease domains. Lymphostatin binds to bovine T-lymphocytes and HEK-293T cells, forming clusters at the plasma membrane that are internalized. With six distinct domains, lymphostatin can be regarded as a multitool of pathogenic Escherichia coli, enabling complex interactions with host cells. |
 External links | Nat Commun / PubMed:40562750 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.7 - 4.4 Å |
| Structure data |  EMDB-19982: Lymphostatin, conformation 1, N-terminal part  EMDB-19983: Lymphostatin, conformation 1, local refinement C-terminal part  EMDB-19984: Lymphostatin, conformation 2, N-terminal part  EMDB-19985: Lymphostatin, conformation 2 , local refinement C-terminal part EMDB-19987, PDB-9euv: EMDB-19988, PDB-9euw:  EMDB-52985: Lymphostatin Conformation II, Hepes buffer pH8 - consensus map  EMDB-52986: Lymphostatin -Conformation II - Local-Refinement GT-domains  EMDB-52987: Lymphostatin - Conformation II - pH 8, Hepes, focussed on center  EMDB-52988: Lymphostatin - Conformation II - pH8 Hepes, focussed on delivery  EMDB-52989: Lymphostatin - Conformation II - pH 8 Hepes - focussed on C-term EMDB-52990, PDB-9qb8:  EMDB-52991: Lymphostatin - conformation III - pH 8 focussed on delivery domain  EMDB-52992: Lymphostatin - Conformation III - pH 8 focussed on centre  EMDB-52993: Lymphostatin - Conformation III - pH 8 - focussed on C-term  EMDB-52994: Lymphostatin - conformation III - pH 8 focussed on N-term  EMDB-52995: Lymphostatin - Conformation III - pH 8 - consensus map EMDB-52996, PDB-9qbb:  EMDB-53164: Lymphostatin - pH8 phosphate buffer - focussed on C-term  EMDB-53165: Lymphostatin- pH 8.0 phosphate buffer - focussed on delivery domain S1  EMDB-53166: Lymphostatin - pH 8 phosphate buffer - focussed on centre  EMDB-53167: Lymphostatin - pH 8.0 phosphate - focussed on GT-domain  EMDB-53168: Lymphostatin at pH 8 in Phosphate buffer - Consensus Map EMDB-53169, PDB-9qhh:  EMDB-53286: Lymphostatin - Conformation I - pH 6.5 phosphate buffer  EMDB-53287: Lymphostatin - conformation II - pH 6.5 phosphate buffer |
| Chemicals |  ChemComp-MN: |
| Source |
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 Keywords | TOXIN / bacterial virulence factor / glycosyltransferase / protease / Virulence Factor Lymphostatin LifA Conformation II / Virulence Factor Lymphostatin LifA Conformation III / Lymphostatin virulence factor A/E bacteria Toxin-like |
escherichia coli o127:h6 str. e2348/69 (bacteria)