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Structure paper

TitleStructural basis for non-canonical integrin engagement by Bordetella adenylate cyclase toxin.
Journal, issue, pagesCell Rep, Vol. 40, Issue 7, Page 111196, Year 2022
Publish dateAug 16, 2022
AuthorsJory A Goldsmith / Andrea M DiVenere / Jennifer A Maynard / Jason S McLellan /
PubMed AbstractIntegrins are ubiquitous cell-surface heterodimers that are exploited by pathogens and toxins, including leukotoxins that target β integrins on phagocytes. The Bordetella adenylate cyclase toxin ...Integrins are ubiquitous cell-surface heterodimers that are exploited by pathogens and toxins, including leukotoxins that target β integrins on phagocytes. The Bordetella adenylate cyclase toxin (ACT) uses the αβ integrin as a receptor, but the structural basis for integrin binding and neutralization by antibodies is poorly understood. Here, we use cryoelectron microscopy to determine a 2.7 Å resolution structure of an ACT fragment bound to αβ. This structure reveals that ACT interacts with the headpiece and calf-2 of the α subunit in a non-canonical manner specific to bent, inactive αβ. Neutralizing antibody epitopes map to ACT residues involved in α binding, providing the basis for antibody-mediated attachment inhibition. Furthermore, binding to αβ positions the essential ACT acylation sites, which are conserved among toxins exported by type I secretion systems, at the cell membrane. These findings reveal a structural mechanism for integrin-mediated attachment and explain antibody-mediated neutralization of ACT intoxication.
External linksCell Rep / PubMed:35977491 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.1 Å
Structure data

26738

7usl

EMDB-26738, PDB-7usl:
Integrin alphaM/beta2 ectodomain in complex with adenylate cyclase toxin RTX751 and M1F5 Fab
Method: EM (single particle) / Resolution: 2.7 Å

26739

7usm

EMDB-26739, PDB-7usm:
Integrin alphaM/beta2 ectodomain
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-27122: Global refinement for integrin alphaM/beta2 ectodomain in complex with adenylate cyclase toxin RTX751 and M1F5 Fab
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-27123: Tailpiece local refinement for integrin alphaM/beta2 ectodomain in complex with adenylate cyclase toxin RTX751 and M1F5 Fab
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-27124: Acylation domain local refinement for integrin alphaM/beta2 ectodomain in complex with adenylate cyclase toxin RTX751 and M1F5 Fab
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-27125: Global refinement for integrin alphaM/beta2 ectodomain
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-27126: Tailpiece local refinement for integrin alphaM/beta2 ectodomain
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • homo sapiens (human)
  • bordetella pertussis (bacteria)
KeywordsTOXIN / Receptor / Complex / Integrin / CELL ADHESION / Complement

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