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Taxonomic group: protista / Evosea (Phylum: Evosea)
Associated disease: infection due to Entamoeba histolytica [ICD11: XN82F

]

NCBI PubMed ID: 16274663
Journal NLM ID: 0372516
Publisher: Academic Press
Institutions: Departamento de Biomedicina Molecular, Centro de Investigacion y de Estudios Avanzados del IPN, Mexico, DF, Mexico

EhABP-120 is the first filamin identified in the parasitic protozoan Entamoeba histolytica. Filamins are a family of cross-linking actin-binding proteins that promote a dynamic orthogonal web. They have been reported to interact directly with more than 30 cellular proteins and some phosphoinositides. The biochemical consequences of these interactions may have either positive or negative effects on the cross-linking function and also form a link between the cytoskeleton and plasma membrane. In this study, the EhABP-120 carboxy-terminal domain (END) was biochemically characterized. This domain was able to associate to 3-sulfate galactosyl ceramide, a new lipid target for a member of the filamin family. Also, the END domain was able to dimerize 'in vitro.' Molecular modeling analysis showed that the dimeric region is stabilized by a disulfide bond. Electrostatic and docking studies suggest that an electropositive concave pocket at the dimeric END domain interacts simultaneously with several sulfogalactose moieties of the sulfatide.

chemistry, genetics, metabolism, Non-U.S.Gov't, analysis, molecular, lipid, Molecular Sequence Data, molecular modeling, Substrate Specificity, glycolipid, Cell Membrane, proteins, protein structure, models, amino acid sequence, ceramide, Sequence Alignment, Animals, Research Support, Tertiary, ABP-120, Filamin, Entamoeba histolytica, Sulfatide, Dimer, Contractile Proteins, Cytoskeleton, Family, Microfilament Proteins, Sulfoglycosphingolipids, Transfection

Structure type: oligomer
Trivial name: S-GalCer
Contained glycoepitopes: IEDB_136044,IEDB_136095,IEDB_137472,IEDB_141794,IEDB_190606,SB_1,SB_118,SB_139,SB_165,SB_166,SB_187,SB_195,SB_7,SB_82,SB_88

Methods: molecular modeling, 32P labeling, Confocal laser scanning microscopy
Biosynthesis and genetic data: biosynthesis data

NCBI Taxonomy refs (TaxIDs): 5759
Show glycosyltransferases

There are 2 chemically distinct structures. Please, select:

[1*]O[C@@H]1O[C@H](CO)[C@H](O)[C@H](OS(=O)(=O)O)[C@H]1O

SVG MW SMILES 3D mol Ionize

R1 = CER

Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)

NCBI PubMed ID: 37830811
Publication DOI: 10.1128/mbio.01395-23
Journal NLM ID: 101519231
Publisher: Washington, DC: American Society for Microbiology
Correspondence: M.C. Roper <mcroper

ucr.edu>
Institutions: Department of Microbiology and Plant Pathology, University of California , Riverside, California, USA, Complex Carbohydrate Research Center, University of Georgia , Athens, USA, Department of Computer Science, Wellesley College , Wellesley, Massachusetts, USA, Department of Biology, University of Wisconsin , Stevens Point, Wisconsin, USA

Xylella fastidiosa is a Gram-negative bacterium that causes disease in many economically important crops. It colonizes the plant host xylem and the mouthparts of its insect vectors where it produces exopolysaccharide (EPS) and forms robust biofilms. Typically, the ability to form a biofilm enhances virulence, but X. fastidiosa does not fit neatly into that paradigm. Instead, X. fastidiosa enters into biofilms to attenuate its movement in the xylem, which, in turn, slows disease progression. In most of its over 600 known plant hosts, X. fastidiosa behaves as a benign commensal, but in some hosts like Vitis vinifera grapevines, it acts as a pathogen. Its ability to attenuate its own virulence in susceptible hosts may be a remnant of its commensal lifestyle in other hosts. Here, we demonstrate that X. fastidiosa utilizes a β-1,4 endoglucanase to cleave its self-produced β-1,4-glucan exopolysaccharide polymer to process it from a higher molecular weight to a lower molecular weight polymer. This processing mediates surface adherence of the cells and ultimately governs overall biofilm architecture, indicating enzymatic pruning of the EPS plays a key role in biofilm-mediated attenuation of X. fastidiosa in planta and, thus, is a key vestige that links its commensal behaviors to its parasitic behaviors in specific hosts. IMPORTANCE: It is well established that exopolysaccharide (EPS) is an integral structural component of bacterial biofilms necessary for assembly and maintenance of the three-dimensional architecture of the biofilm. However, the process and role of EPS turnover within a developing biofilm is not fully understood. Here, we demonstrated that Xylella fastidiosa uses a self-produced endoglucanase to enzymatically process its own EPS to modulate EPS polymer length. This enzymatic processing of EPS dictates the early stages of X. fastidiosa's biofilm development, which, in turn, affects its behavior in planta. A deletion mutant that cannot produce the endoglucanase was hypervirulent, thereby linking enzymatic processing of EPS to attenuation of virulence in symptomatic hosts, which may be a vestige of X. fastidiosa's commensal behavior in many of its other non-symptomatic hosts.

exopolysaccharide, biofilms, plant pathogens, grapevine

Structure type: polymer chemical repeating unit
Location inside paper: Fig. 4A
Compound class: EPS

Methods: extraction, Confocal laser scanning microscopy, SEM, cell-cell aggregation assay, BiofilmQ software analysis, reducing sugar assay
Comments, role: EPS subunits from wild type and ΔengXCA2 were identical and about 60% of the side chains terminated in β-Glc and 40% in β-GlcA residues.
3D data: quantitative 3D image analysis of biofilms

NCBI Taxonomy refs (TaxIDs): 2371
Show glycosyltransferases

SMILES errors: -4)/[bDGlcp(1-2)aDManp(1-3)]bDGlcp(1-4)bDGlcp(1-4)[bDGlcpA(1-2)aDManp(1-3)]bDGlcp(1-4)bDGlcp(1-4)/n=?//[bDGlcp(1-2)aDManp(1-3)]bDGlcp(1-4)bDGlcp(1-4)/n=?/[bDGlcp(1-2)aDManp(1-3)]bDGlcp(1-4)bDGlcp(1-:
SMILES error: could not calculate brutto descriptors of a molecule from SMILES [*]O[C@@H]1[C@@H](CO)O[C@@H](O[C@@H]2[C@@H](CO)O[C@@H](O[C@@H]3[C@@H](CO)O[C@@H](O[C@@H]4[C@@H](CO)O[C@@H](O[C@@H]5[C@@H](CO)O[C@@H](O[C@@H]6[C@@H](CO)O[C@@H](O[C@@H]7[C@@H](CO)O[C@@H](O[C@@H]8[C@@H](CO)O[C@@H](O[C@@H]9[C@@H](CO)O[C@@H](O[C@@H]%10[C@@H](CO)O[C@@H](O[C@@H]%11[C@@H](CO)O[C@@H](O[C@@H]%12[C@@H](CO)O[C@@H](O[C@@H]%13[C@@H](CO)O[C@@H](O[C@@H]%14[C@@H](CO)O[C@@H](O[C@@H]%15[C@@H](CO)O[C@@H](O[C@@H]%16[C@@H](CO)O[C@@H](O[C@@H]%17[C@@H](CO)O[C@@H](O[C@@H]%18[C@@H](CO)O[C@@H](O[C@@H]%19[C@@H](CO)O[C@@H](O[C@@H]%20[C@@H](CO)O[C@@H]([*])[C@H](O)[C@H]%20O)[C@H](O)[C@H]%19O[C@H]%19O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%19O[C@@H]%19O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%19O)[C@H](O)[C@H]%18O)[C@H](O)[C@H]%17O[C@H]%17O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%17O[C@@H]%17O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%17O)[C@H](O)[C@H]%16O)[C@H](O)[C@H]%15O[C@H]%15O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%15O[C@@H]%15O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%15O)[C@H](O)[C@H]%14O)[C@H](O)[C@H]%13O[C@H]%13O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%13O[C@@H]%13O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%13O)[C@H](O)[C@H]%12O)[C@H](O)[C@H]%11O[C@H]%11O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%11O[C@@H]%11O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]%11O)[C@H](O)[C@H]%10O)[C@H](O)[C@H]9O[C@H]9O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]9O[C@@H]9O[C@H](CO)[C@@H](O)[C@H](O)[C@H]9O)[C@H](O)[C@H]8O)[C@H](O)[C@H]7O[C@H]7O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]7O[C@@H]7O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]7O)[C@H](O)[C@H]6O)[C@H](O)[C@H]5O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O[C@@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@H]5O)[C@H](O)[C@H]4O)[C@H](O)[C@H]3O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]3O[C@@H]3O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]3O)[C@H](O)[C@H]2O)[C@H](O)[C@H]1O[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]1O[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O
Invalid SMILES [*]O[C@@H]1[C@@H](CO)O[C@@H](O[C@@H]2[C@@H](CO)O[C@@H](O[C@@H]3[C@@H](CO)O[C@@H](O[C@@H]4[C@@H](CO)O[C@@H](O[C@@H]5[C@@H](CO)O[C@@H](O[C@@H]6[C@@H](CO)O[C@@H](O[C@@H]7[C@@H](CO)O[C@@H](O[C@@H]8[C@@H](CO)O[C@@H](O[C@@H]9[C@@H](CO)O[C@@H](O[C@@H]%10[C@@H](CO)O[C@@H](O[C@@H]%11[C@@H](CO)O[C@@H](O[C@@H]%12[C@@H](CO)O[C@@H](O[C@@H]%13[C@@H](CO)O[C@@H](O[C@@H]%14[C@@H](CO)O[C@@H](O[C@@H]%15[C@@H](CO)O[C@@H](O[C@@H]%16[C@@H](CO)O[C@@H](O[C@@H]%17[C@@H](CO)O[C@@H](O[C@@H]%18[C@@H](CO)O[C@@H](O[C@@H]%19[C@@H](CO)O[C@@H](O[C@@H] [C@@H](CO)O[C@@H]([*])[C@H](O)[C@H] O)[C@H](O)[C@H]%19O[C@H]%19O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%19O[C@@H]%19O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%19O)[C@H](O)[C@H]%18O)[C@H](O)[C@H]%17O[C@H]%17O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%17O[C@@H]%17O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%17O)[C@H](O)[C@H]%16O)[C@H](O)[C@H]%15O[C@H]%15O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%15O[C@@H]%15O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%15O)[C@H](O)[C@H]%14O)[C@H](O)[C@H]%13O[C@H]%13O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%13O[C@@H]%13O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%13O)[C@H](O)[C@H]%12O)[C@H](O)[C@H]%11O[C@H]%11O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]%11O[C@@H]%11O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]%11O)[C@H](O)[C@H]%10O)[C@H](O)[C@H]9O[C@H]9O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]9O[C@@H]9O[C@H](CO)[C@@H](O)[C@H](O)[C@H]9O)[C@H](O)[C@H]8O)[C@H](O)[C@H]7O[C@H]7O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]7O[C@@H]7O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]7O)[C@H](O)[C@H]6O)[C@H](O)[C@H]5O[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]5O[C@@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@H]5O)[C@H](O)[C@H]4O)[C@H](O)[C@H]3O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]3O[C@@H]3O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]3O)[C@H](O)[C@H]2O)[C@H](O)[C@H]1O[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]1O[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O