Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10969574 | Vaccine | 2010 | 9 Pages |
Abstract
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 μm long (4 MDa). The bead-like structures along the polymer are 5.8 ± 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.
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Immunology
Authors
Andrei Soliakov, J. Robin Harris, Allan Watkinson, Jeremy H. Lakey,