6533b862fe1ef96bd12c6333

RESEARCH PRODUCT

The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states

Jeremy H. LakeyAndrei SoliakovJ. Robin HarrisJ. Robin HarrisAllan Watkinson

subject

Models MolecularProtein FoldingPolymersVirulence FactorsYersinia pestismedicine.medical_treatmentVirulence factorMicrobiologychemistry.chemical_compoundProtein structureAdjuvants ImmunologicBacterial ProteinsMicroscopy Electron TransmissionmedicineProtein Structure QuaternaryBacterial Capsuleschemistry.chemical_classificationAntigens BacterialPlaguePlague VaccineGeneral VeterinaryGeneral Immunology and MicrobiologybiologyPublic Health Environmental and Occupational HealthHemocyaninPolymerbiology.organism_classificationInfectious DiseasesMonomerYersinia pestischemistryBiophysicsMolecular MedicinePlague vaccineProtein folding

description

Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism. Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa). The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins. Short polymers often form circles, presumably by DSE. We also provide the first images of proteins bound to alhydrogel adjuvant. Caf1, hemocyanin and anthrax PA are all resolved clearly and Caf1 exhibits adjuvant bound stretches with long intervening loops draped from the edges.

yearjournalcountryeditionlanguage
2010-01-08Vaccine
https://doi.org/10.1016/j.vaccine.2010.05.074