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-Structure paper
タイトル | Structure of lymphostatin, a large multi-functional virulence factor of pathogenic Escherichia coli. |
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ジャーナル・号・ページ | Nat Commun, Vol. 16, Issue 1, Page 5389, Year 2025 |
掲載日 | 2025年6月25日 |
![]() | Matthias Griessmann / Tim Rasmussen / Vanessa J Flegler / Christian Kraft / Ronja Schneider / Max Hateley / Lukas Spantzel / Mark P Stevens / Michael Börsch / Bettina Böttcher / ![]() ![]() |
PubMed 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 2.7 - 4.4 Å |
構造データ | ![]() 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 |
化合物 | ![]() ChemComp-MN: |
由来 |
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![]() | 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 |