Growth conditions and outer membrane proteins of Fusobacterium nucleatum

Abstract

– Fusobacterium nucleatum strains ATCC 10953, ATCC 25586, F1 F3, F6, and Fevl were grown in different media. The influence of growth conditions on the outer membrane proteins (OMPs) was analyzed by sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS‐PAGE). There were no apparent differences in the outer membrane protein profiles when cells in the same phase of growth in various rich media were compared. Differences, however, were observed between early logarithmic phase and stationary phase cells. Thus several proteins were only synthesized during late logarithmic and stationary phase. Synthesis of some of these proteins, in particular a 65K and a 14K protein, seemed to depend on the presence of peptides in the medium. In a complete medium, these proteins were synthesized after depletion of some amino acids, and peptides were then utilized.

Taxonomy, biology, and periodontal aspects of Fusobacterium nucleatum.

“…Fusobacteria require rich media for growth and usually grow well in media containing Trypticase, peptone, or yeast extract (16,17). Much attention has been paid to the utilization of amino acids and peptides by F. nucleatum (16, 19, 23, 50, 54, 71, 94, 97, 100, 160, 182, 189, 226, 228, 238-240, 242, 253, 254).…”

Similarities between Fusobacterium nucleatum and Bacteroides fragilis studied by two DNA probes derived from Fusobacterium nucleatum

“…In addition to variations in mol. mass, the actual gene products being expressed are dependent on factors such as growth conditions and growth phase (20).…”

Immunogenicity of a Fap2 peptide mimotope of Fusobacterium nucleatum and its potential use in the diagnosis of colorectal cancer

“…F. nucleatum is a non-spore forming, non-motile, gram-negative, spindle-shaped opportunistic anaerobic bacteria that can be found in the oral cavity and the gastrointestinal tract [ 5 ]. Its cell envelope is composed of outer and inner membranes flanking a periplasmic space and outer membrane proteins which comprise a third of its mass [ 6 ].…”