Isolation of a major cell envelope protein from Fusobacterium nucleatum.
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 degrees 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 degrees C. Heating the peptidoglycan-HM-1 protein complex in the detergent at 100 degrees 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.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000302:isolation & purification*; D005673:Fusobacterium / Q000032:analysis / Q000302:isolation & purification* / Q000648:ultrastructure; D006801:Humans; D009055:Mouth / Q000382:microbiology; D013045:Species Specificity
D000596:Amino Acids; D001426:Bacterial Proteins