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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/22502

Title: The Baseplate of Lactobacillus delbrueckii Bacteriophage Ld17 Harbors a Glycerophosphodiesterase
Authors: Cornelissen, Anneleen
Sadovskaya, Irina
Vinogradov, Evgeny
Blangy, Stephanie
Spinelli, Silvia
Casey, Eoghan
Mahony, Jennifer
Noben, Jean-Paul
Dal Bello, Fabio
Cambillau, Christian
van Sinderen, Douwe
Issue Date: 2016
Citation: JOURNAL OF BIOLOGICAL CHEMISTRY, 291(32), p. 16816-16827
Abstract: Glycerophosphodiester phosphodiesterases (GDPDs; EC 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; GDPD(Ld17)), 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 GDPD(Ld17) activity. The presence of the GDPD(Ld17) 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 Ca2+ ions supports a role for GDPD(Ld17) activity during phage adsorption and/or phage genome injection. In contrast to GDPD(Ld17), 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.
Notes: [Cornelissen, Anneleen; Casey, Eoghan; Mahony, Jennifer; van Sinderen, Douwe] Univ Coll Cork, Sch Microbiol, Western Rd, Cork, Ireland. [van Sinderen, Douwe] Univ Coll Cork, APC Microbiome Inst, Western Rd, Cork, Ireland. [Sadovskaya, Irina] Univ Littoral Cote dOpale, Equipe Biochim Prod Aquat, Blvd Bassin Napoleon,BP 120, F-62327 Boulogne Sur Mer, France. [Vinogradov, Evgeny] CNR, 100 Sussex Dr, Ottawa, ON K1A 0R6, Canada. [Blangy, Stephanie; Spinelli, Silvia; Cambillau, Christian] Aix Marseille Univ, Architecture & Fonct Macromol Biol, Campus Luminy, F-13288 Marseille 09, France. [Blangy, Stephanie; Spinelli, Silvia; Cambillau, Christian] CNRS, Architecture & Fonct Macromol Biol, UMR 6098, Campus Luminy, F-13288 Marseille 09, France. [Noben, Jean-Paul] Hasselt Univ, Biomed Res Inst Biomed, Agoralaan Bldg C, BE-3590 Diepenbeek, Belgium. [Noben, Jean-Paul] Hasselt Univ, Sch Life Sci, Transnat Univ Limburg, Agoralaan Bldg C, BE-3590 Diepenbeek, Belgium. [Dal Bello, Fabio] Sacco Srl, I-22071 Cadorago, CO, Italy.
URI: http://hdl.handle.net/1942/22502
DOI: 10.1074/jbc.M116.728279
ISI #: 000380826700037
ISSN: 0021-9258
Category: A1
Type: Journal Contribution
Validation: ecoom, 2017
Appears in Collections: Research publications

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