Isolation of a major cell envelope protein from Fusobacterium nucleatum

Abstract

A major, heat-modifiable cell envelope protein was identified in Fusobacterium nucleatum FDC 364 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This protein, designated HM-1, had apparent molecular weights of 38,500 and 50,000 when heated in sodium dodecyl sulfate at 50 and 100°C, respectively. Whole cells were labeled with 125I, and the results suggested that the HM-1 protein may be exposed on the bacterial surface. The HM-1 protein was isolated in association with the peptidoglycan by extraction of whole cells or cell envelopes with 2% sodium dodecyl sulfate at 55°C. Heating the peptidoglycan-HM-1 protein complex in the detergent at 100°C resulted in the quantitative release of the protein. Isoelectric focusing experiments and amino acid analysis revealed that the HM-1 protein had a basic character and was moderately hydrophilic. Various strains of F. nucleatum as well as three oral fusiform isolates contained a serologically related protein. The abundance and location of the HM-1 protein in F. nucleatum suggest that it has the potential to participate in cell surface-related interactions of this bacterium.