Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
The structure was elucidated in this paperNCBI PubMed ID: 30687274Publication DOI: 10.3389/fmicb.2018.03288Journal NLM ID: 101548977Publisher: Lausanne: Frontiers Research Foundation
Correspondence: Dr. Konstantin A. Miroshnikov <kmi
ibch.ru>
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia, Research Center 'PhytoEngineering' Ltd., Rogachevo, Russia, Immanuel Kant Baltic Federal University, Kaliningrad, Russia, Winogradsky Institute of Microbiology, Federal Research Center 'Fundamentals of Biotechnology', Russian Academy of Sciences, Moscow, Russia
Dickeya solani is a recently emerged virulent bacterial potato pathogen that poses a major threat to world agriculture. Because of increasing antibiotic resistance and growing limitations in antibiotic use, alternative antibacterials such as bacteriophages are being developed. Myoviridae bacteriophages recently re-ranked as a separate Ackermannviridae family, such as phage PP35 described in this work, are the attractive candidates for this bacterial biocontrol. PP35 has a very specific host range due to the presence of tail spike protein PP35 gp156, which can depolymerize the O-polysaccharide (OPS) of D. solani. The D. solani OPS structure, →2)-β-D-6-deoxy-D-altrose-(1→, is so far unique among soft-rot Pectobacteriaceae, though it may exist in non-virulent environmental Enterobacteriaceae. The phage tail spike depolymerase degrades the shielding polysaccharide, and launches the cell infection process. We hypothesize that non-pathogenic commensal bacteria may maintain the population of the phage in soil environment.
polysaccharide, bacteriophage, genomics, Dickeya solani, depolymerase, Lelliottia, tail spike protein
Structure type: homopolymer
Location inside paper: abstract, fig.6
Compound class: O-polysaccharide, O-antigen
Methods: 13C NMR, 1H NMR, NMR-2D, DNA techniques, GPC, electron microscopy, phage degradation, phylogenetic analysis, HR-ESI-MS, phage characterization, phage genome comparison
NCBI Taxonomy refs (TaxIDs): 1089444,
2065208,
198628Reference(s) to other database(s): GTC:G91814UH
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
report error