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. 1985 Apr;4(4):1013–1018. doi: 10.1002/j.1460-2075.1985.tb03732.x

A novel virulence-associated cell surface structure composed of 47-kd protein subunits in Yersinia enterocolitica.

M Zaleska, K Lounatmaa, M Nurminen, E Wahlström, P H Mäkelä
PMCID: PMC554293  PMID: 4018036

Abstract

A fresh human isolate of Yersinia enterocolitica serotype 03, and its derivative that had lost the virulence-associated 46-Md plasmid, were grown under defined conditions and compared for their outer membrane protein and cell surface structure. Under these conditions, the virulent strain grown at 37 degrees C expressed one major outer membrane protein (47 kd) not present in the plasmidless strain or in either strain grown at room temperature. A 200-kd protein also seen in the same preparations was shown to be an oligomer composed of the 47-kd protein subunits. Four different electron microscopic techniques showed tack-like projections covering the surface of those bacteria that expressed the 47-kd protein. These were specifically labeled with antibody to the 47-kd protein. This surface structure appeared to mediate aggregation (auto-agglutination) of the bacteria bringing their surfaces into unusually close apposition.

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Selected References

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