Protein secretion systems in Fusobacterium nucleatum: genomic identification of Type 4 piliation and complete Type V pathways brings new insight into mechanisms of pathogenesis.
Recent genomic analyses of the two sequenced strains F. nucleatum subsp. nucleatum ATCC 25586 and F. nucleatum subsp. vincentii ATCC 49256 suggested that the major protein secretion systems were absent. However, such a paucity of protein secretion systems is incongruous with F. nucleatum pathogenesis. Moreover, the presence of one or more such systems has been described for every other Gram-negative organism sequenced to date. In this investigation, the question of protein secretion in F. nucleatum was revisited. In the current study, the absence in F. nucleatum of a twin-arginine translocation system (TC #2.A.64.), a Type III secretion system (TC #3.A.6.), a Type IV secretion system (TC #3.A.7.) and a chaperone/usher pathway (TC #1.B.11.) was confirmed. However, contrary to previous findings, our investigations indicated that a Type I protein secretion system was also absent from F. nucleatum. In contrast, members of the holin family (TC #1.E) and the machinery required for a Type 4 piliation/fimbriation system (TC #3.A.15.2.) were identified using a variety of bioinformatic tools. Furthermore, a complete range of proteins resembling members of the Type V secretion pathway, i.e., the Type Va (autotransporter; TC #1.B.12.), Type Vb (two-partner secretion system; TC #1.B.20.) and Type Vc (YadA-like trimeric autotransporter; TC #1.B.42.), was found. This work provides new insight into the protein secretion and virulence mechanisms of F. nucleatum.
The Institute for Biomedical Research (IBR), The University of Birmingham-The Medical School, Division of Immunity and Infection, Bacterial Pathogenesis and Genomics Unit, Edgbaston, Birmingham B15 2TT, UK.
Mickaël
M
Desvaux
Arshad
A
Khan
Scott A
SA
Beatson
Anthony
A
Scott-Tucker
Ian R
IR
Henderson
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D018407:Bacterial Physiological Phenomena; D001483:Base Sequence; D018441:Biofilms; D019295:Computational Biology / Q000379:methods; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D005673:Fusobacterium / Q000378:metabolism; D016967:Fusobacterium nucleatum / Q000235:genetics* / Q000472:pathogenicity*; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010802:Phylogeny; D011485:Protein Binding; D011487:Protein Conformation; D021382:Protein Sorting Signals; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D017386:Sequence Homology, Amino Acid; D012984:Software; D014774:Virulence
D021382:Protein Sorting Signals