Identification of EPS-degrading activity within the tail spikes of the novel Pseudomonas putida phage AF.
We report the study of phage AF, the first member of the canonical lambdoid phage group infecting Pseudomonas putida. Its 42.6 kb genome is related to the "epsilon15-like viruses" and the "BPP-1-like viruses", a clade of bacteriophages shaped by extensive horizontal gene transfer. The AF virions display exopolysaccharide (EPS)-degrading activity, which originates from the action of the C-terminal domain of the tail spike (Gp19). This protein shows high similarity to the tail spike of the T7-like P. putida-infecting phage φ15. These unrelated phages have an identical host spectrum and EPS degradation characteristics, designating the C-terminal part of Gp19 as sole determinant for these functions. While intact AF particles have biofilm-degrading properties, Gp19 and non-infectious AF particles do not, emphasizing the role of phage amplification in biofilm degradation.
Laboratory of Gene Technology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, Leuven B-3001, Belgium.
Anneleen
A
Cornelissen
Pieter-Jan
PJ
Ceyssens
Victor N
VN
Krylov
Jean-Paul
JP
Noben
Guido
G
Volckaert
Rob
R
Lavigne
D004279:DNA, Viral / Q000737:chemistry / Q000235:genetics; D016679:Genome, Viral; D006868:Hydrolysis; D008969:Molecular Sequence Data; D011134:Polysaccharides / Q000378:metabolism*; D017105:Pseudomonas Phages / Q000201:enzymology*; D016958:Pseudomonas putida / Q000821:virology*; D017422:Sequence Analysis, DNA; D017376:Viral Tail Proteins / Q000378:metabolism*
D004279:DNA, Viral; D011134:Polysaccharides; D017376:Viral Tail Proteins