Pantoea stewartii WceF is a glycan biofilm modifying enzyme with a bacteriophage tailspike-like fold

Autor: Irmscher, T., Roske, Y., Gayk, I., Dunsing, V., Chiantia, S., Heinemann, U., Barbirz, S.
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Models
Molecular
Protein Conformation
alpha-Helical
Cancer Research
bacterial pathogenesis
Glycoside Hydrolases
MBTH
3-methyl-2-benzothiazolinon-hydrazone
Genetic Vectors
Gene Expression
Oligosaccharides
bacteriophage tailspike
CE
capillary electrophoresis
Crystallography
X-Ray
biofilm
IMAC
immobilized metal affinity chromatography
Bacterial Proteins
Escherichia coli
oligosaccharide
Bacteriophages
Protein Interaction Domains and Motifs
glycoside hydrolase
Cloning
Molecular
Pantoea stewartii
TSP
tailspike protein
X-ray crystallography
Binding Sites
Pantoea
Polysaccharides
Bacterial
Viral Tail Proteins
Plants
Recombinant Proteins
Carbohydrate Sequence
Structural Homology
Protein
Biofilms
EPS
exopolysaccharide
exopolysaccharide
Protein Conformation
beta-Strand
parallel beta-helix
Protein Multimerization
500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften
Research Article
RU
repeat unit
Protein Binding
Zdroj: Journal of Biological Chemistry
The Journal of Biological Chemistry
Popis: Pathogenic microorganisms often reside in glycan-based biofilms. Concentration and chain length distribution of these mostly anionic exopolysaccharides (EPS) determine the overall biophysical properties of a biofilm and result in a highly viscous environment. Bacterial communities regulate this biofilm state via intracellular small-molecule signaling to initiate EPS synthesis. Reorganization or degradation of this glycan matrix, however, requires the action of extracellular glycosidases. So far, these were mainly described for bacteriophages that must degrade biofilms for gaining access to host bacteria. The plant pathogen Pantoea stewartii (P. stewartii) encodes the protein WceF within its EPS synthesis cluster. WceF has homologs in various biofilm forming plant pathogens of the Erwinia family. In this work, we show that WceF is a glycosidase active on stewartan, the main P. stewartii EPS biofilm component. WceF has remarkable structural similarity with bacteriophage tailspike proteins (TSPs). Crystal structure analysis showed a native trimer of right-handed parallel ��-helices. Despite its similar fold, WceF lacks the high stability found in bacteriophage TSPs. WceF is a stewartan hydrolase and produces oligosaccharides, corresponding to single stewartan repeat units. However, compared with a stewartan-specific glycan hydrolase of bacteriophage origin, WceF showed lectin-like autoagglutination with stewartan, resulting in notably slower EPS cleavage velocities. This emphasizes that the bacterial enzyme WceF has a role in P. stewartii biofilm glycan matrix reorganization clearly different from that of a bacteriophage exopolysaccharide depolymerase.
Databáze: OpenAIRE
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