The Baseplate of Lactobacillus delbrueckii Bacteriophage Ld17 Harbors a Glycerophosphodiesterase.
Glycerophosphodiester phosphodiesterases (GDPDs; EC 3.1.4.46) typically hydrolyze glycerophosphodiesters to sn-glycerol 3-phosphate (Gro3P) and their corresponding alcohol during patho/physiological processes in bacteria and eukaryotes. GDPD(-like) domains were identified in the structural particle of bacterial viruses (bacteriophages) specifically infecting Gram-positive bacteria. The GDPD of phage 17 (Ld17; GDPDLd17), representative of the group b Lactobacillus delbrueckii subsp. bulgaricus (Ldb)-infecting bacteriophages, was shown to hydrolyze, besides the simple glycerophosphodiester, two complex surface-associated carbohydrates of the Ldb17 cell envelope: the Gro3P decoration of the major surface polysaccharide d-galactan and the oligo(glycerol phosphate) backbone of the partially glycosylated cell wall teichoic acid, a minor Ldb17 cell envelope component. Degradation of cell wall teichoic acid occurs according to an exolytic mechanism, and Gro3P substitution is presumed to be inhibitory for GDPDLd17 activity. The presence of the GDPDLd17 homotrimer in the viral baseplate structure involved in phage-host interaction together with the dependence of native GDPD activity, adsorption, and efficiency of plating of Ca(2+) ions supports a role for GDPDLd17 activity during phage adsorption and/or phage genome injection. In contrast to GDPDLd17, we could not identify any enzymatic activity for the GDPD-like domain in the neck passage structure of phage 340, a 936-type Lactococcus lactis subsp. lactis bacteriophage.
From the School of Microbiology and.
Anneleen
A
Cornelissen
Equipe Biochimie des Produits Aquatiques, Université du Littoral-Côte d'Opale, Boulevard du Bassin Napoléon, BP 120, 62327 Boulogne-sur-mer, France.
Irina
I
Sadovskaya
National Research Council, 100 Sussex Drive, Ottawa K1A 0R6, Canada.
Evgeny
E
Vinogradov
Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques, Campus de Luminy, 13288 Marseille Cedex 09, France, CNRS, Architecture et Fonction des Macromolécules Biologiques, UMR 6098, Campus de Luminy, 13288 Marseille Cedex 09, France.
Stéphanie
S
Blangy
Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques, Campus de Luminy, 13288 Marseille Cedex 09, France, CNRS, Architecture et Fonction des Macromolécules Biologiques, UMR 6098, Campus de Luminy, 13288 Marseille Cedex 09, France.
Silvia
S
Spinelli
From the School of Microbiology and.
Eoghan
E
Casey
From the School of Microbiology and.
Jennifer
J
Mahony
Biomedical Research Institute (Biomed) and School of Life Sciences, Transnationale Universiteit Limburg, Hasselt University, Agoralaan-Building C, BE-3590 Diepenbeek, Belgium, and.
Jean-Paul
JP
Noben
Sacco srl, 22071 Cadorago CO, Italy.
Fabio
F
Dal Bello
Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques, Campus de Luminy, 13288 Marseille Cedex 09, France, CNRS, Architecture et Fonction des Macromolécules Biologiques, UMR 6098, Campus de Luminy, 13288 Marseille Cedex 09, France.
Christian
C
Cambillau
From the School of Microbiology and APC Microbiome Institute, University College Cork, Cork, Ireland, d.vansinderen@ucc.ie.
Douwe
D
van Sinderen
D001435:Bacteriophages / Q000201:enzymology* / Q000235:genetics; D048668:Lactobacillus delbrueckii / Q000378:metabolism / Q000821:virology*; D010727:Phosphoric Diester Hydrolases / Q000235:genetics / Q000378:metabolism*; D011135:Polysaccharides, Bacterial / Q000235:genetics / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
D011135:Polysaccharides, Bacterial; D014764:Viral Proteins; D010727:Phosphoric Diester Hydrolases; C038133:glycerophosphodiester phosphodiesterase
D-galactan; Lactobacillus; bacteriophage; carbohydrate; cell wall; phosphodiesterases; sn-glycerol-3-phosphate; teichoic acid