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Taxonomic group: bacteria / Firmicutes (Phylum: Firmicutes)

NCBI PubMed ID: 6111553
Publication DOI: 10.1128/JB.146.2.467-475.1981
Journal NLM ID: 2985120R
Publisher: American Society for Microbiology
Institutions: Institut für Physiologische Chemie, Universität Erlangen-Nürnberg, D-8520 Erlangen, Federal Republic of Germany

Native substitution with the D-alanine ester of lipoteichoic acids (LTAs) affects their immunological properties, the capacity to bind divalent cations, and LTA carrier activity. In this study we tested the influence of the D-alanine ester on anti-autolytic activity, using extracellular autolysin from Staphylococcus aureus and nine LTAs with alanine/phosphorus molar ratios of between 0.23 and 0.71. The inhibitory activity, highest with alanine-free LTA, exponentially decreased with increasing alanine content, approaching zero at substitutions of greater than 0.6. Correspondingly, dipolar ionic phospholipids were not inhibitory, in contrast to negatively charged ones. Glycosylation of LTA up to an extent of 0.5 did not depress inhibitory activity, and even at a degree of 0.8 the effect was comparatively small. On comparison of LTAs from various sources, differences in lipid structures and chain lengths were without effect. The inhibitory activity drastically decreased when the glycolipid carried a single glycerophosphate residue or the hydrophilic chain had the unusual structure [6→Gal(α1→6)Gal(α1→3)Gro-(2 comes from 1 αGal)-P]n, in which digalactosyl moieties connect the α-galactosylated glycerophosphate units. Principally, the same results were obtained with the more complex system of autolysis of S. aureus cells. We hypothesize that the anti-autolytic activity of LTA resides in a sequence of glycerophosphate units and that the negative charges of appropriately spaced phosphodiester groups play a crucial role. The alanine ester effect is discussed with respect to the putative in vivo regulation of autolysins by LTA.

Structure type: oligomer
Location inside paper: XVI
Compound class: glycolipid, glycerophosphoglycolipid, lipoteichoate derivative
Contained glycoepitopes: IEDB_130695,IEDB_134624,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_144999,IEDB_146664,IEDB_151528,IEDB_161523,IEDB_190606,IEDB_232584,IEDB_241118,IEDB_983931,SB_163,SB_192,SB_7

Related record ID(s): 131720, 131723, 131724, 131725, 131727, 231726
NCBI Taxonomy refs (TaxIDs): 1358
Show glycosyltransferases

There is only one chemically distinct structure:

[1*]OC[C@H]1O[C@H](OCC(CO[2*])O[2*])[C@H](O[C@H]2O[C@H](COP(=O)(O)OCC(CO[C@H]3O[C@H](CO[C@H]4O[C@H](COP(=O)(O)OCC(CO[C@H]5O[C@H](CO[C@H]6O[C@H](COP(=O)(O)OCC(CO[C@H]7O[C@H](CO[C@H]8O[C@H](COP(=O)(O)OCC(CO[C@H]9O[C@H](CO[C@H]%10O[C@H](COP(=O)(O)OCC(CO[C@H]%11O[C@H](CO[C@H]%12O[C@H](CO)[C@H](O)[C@H](O)[C@H]%12O)[C@H](O)[C@H](O)[C@H]%11O)O[C@H]%11O[C@H](CO)[C@H](O)[C@H](O)[C@H]%11O)[C@H](O)[C@H](O)[C@H]%10O)[C@H](O)[C@H](O)[C@H]9O)O[C@H]9O[C@H](CO)[C@H](O)[C@H](O)[C@H]9O)[C@H](O)[C@H](O)[C@H]8O)[C@H](O)[C@H](O)[C@H]7O)O[C@H]7O[C@H](CO)[C@H](O)[C@H](O)[C@H]7O)[C@H](O)[C@H](O)[C@H]6O)[C@H](O)[C@H](O)[C@H]5O)O[C@H]5O[C@H](CO)[C@H](O)[C@H](O)[C@H]5O)[C@H](O)[C@H](O)[C@H]4O)[C@H](O)[C@H](O)[C@H]3O)O[C@H]3O[C@H](CO)[C@H](O)[C@H](O)[C@H]3O)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](O)[C@@H]1O

SVG MW SMILES 3D mol Ionize

R1 = 95%LIP
R2 = LIP
Warning = sub-repeat ending at xXP?: large unit count (7) was reduced to 5

Taxonomic group: bacteria / Firmicutes (Phylum: Firmicutes)

NCBI PubMed ID: 8294463
Journal NLM ID: 2985121R
Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Northwest Center for Medical Education, Indiana University School of Medicine, Gary 46408

The same 70-kDa protein, present on the surface of mouse lymphocytes, served as the predominant binding site for heparin, heparinoids, and bacterial lipoteichoic acids, as well as peptidoglycan and lipopolysaccharides. This conclusion was supported by the following results: (a) all of these compounds photoaffinity cross-linked to one major 70-kDa 6.5-7.0 pI protein that co-migrated on two-dimensional polyacrylamide gel electrophoresis; (b) peptide maps of the 70-kDa proteins digested with chymotrypsin, subtilisin, protease V, or papain yielded the same peptides for heparin-, lipoteichoic acid-, peptidoglycan-, and lipopolysaccharide-binding proteins; (c) cross-linking of peptidoglycan, lipopolysaccharide, lipoteichoic acid, and heparin was competitively inhibited by the same compounds with the same order of potency, i.e. carboxyl-reduced sulfated heparin > peptidoglycan > pentosan polysulfate > heparin > chitin > dextran sulfate > trestatin sulfate > polyanetholesulfonate > fucoidan > beta-cyclodextrin tetradecasulfate > heparan sulfate > carrageenan lambda > lipoteichoic acids > Re-lipopolysaccharide > lipopolysaccharide > lipid A > polygalacturonic acid; and (d) cross-linking of each of these ligands was not inhibited by carboxyl-reduced heparin, dextran, beta-cyclodextrin, trestatin, carrageenan kappa, chondroitin 4-sulfate, chondroitin 6-sulfate, beta-D-glucan, carboxy-methylcellulose, levan, alpha-D-mannan, and glycogen. The minimum size of the molecule that bound was 7-9 glycan residues, whereas, di- and trisaccharides did not bind. There was a logarithmic linear relationship between the strength of the binding and the length of the polymer (up to > 1500 glycan residues), which indicates an avidity effect of the cooperative binding of one polymeric molecule to several receptor molecules on the cell surface. The 70-kDa receptor, therefore, has a broad, but limited specificity of binding for non-charged (peptidoglycan and chitin), highly negatively charged (heparin and heparinoids), and weakly negatively charged (lipoteichoic acids, lipopolysaccharides, and lipid A) ligands.

Structure type: oligomer
Location inside paper: LTA S.f.
Compound class: glycolipid, lipoteichoate derivative
Contained glycoepitopes: IEDB_130695,IEDB_140628,IEDB_142488,IEDB_144998,IEDB_144999,IEDB_146664,IEDB_1597446,IEDB_161523,IEDB_232584,IEDB_241118,IEDB_983931,SB_192

Related record ID(s): 136955, 136956, 136957, 136958, 136960, 136962, 136963, 136965, 136967, 236963
NCBI Taxonomy refs (TaxIDs): 1351
Show glycosyltransferases

There are too many chemically distinct structures (243) corresponding to the specified structure with alternative fragments (<..>), so only one was processed further:

LIP(1-1)[%?DGlc?(1-2)%?DGlc?(1-2)?DGlc?(1-2)[%?DGlc?(1-2)%?DGlc?(1-2)?DGlc?(1-2)[%?DGlc?(1-2)%?DGlc?(1-2)?DGlc?(1-2)[%?DGlc?(1-2)%?DGlc?(1-2)?DGlc?(1-2)[%?DGlc?(1-2)%?DGlc?(1-2)?DGlc?(1-2)[x?Gro(1-P-3)]x?Gro(1-P-3)]x?Gro(1-P-3)]x?Gro(1-P-3)]x?Gro(1-P-3)]x?Gro(1-P-3)x?Gro(1-P-6)aDGlcp(1-2)[LIP(1-2)[LIP(1-3)]x?Gro(1-P-6)]aDGlcp(1-3),LIP(1-2)]x?Gro

There are too many chemically distinct structures (~32768) for the variant above as well, so only one is shown:

LIP(1-1)[%?DGlcp(1-2)%?DGlcp(1-2)?DGlcp(1-2)[%?DGlcp(1-2)%?DGlcp(1-2)?DGlcp(1-2)[%?DGlcp(1-2)%?DGlcp(1-2)?DGlcp(1-2)[%?DGlcp(1-2)%?DGlcp(1-2)?DGlcp(1-2)[%?DGlcp(1-2)%?DGlcp(1-2)?DGlcp(1-2)[x?Gro?(1-P-3)]x?Gro?(1-P-3)]x?Gro?(1-P-3)]x?Gro?(1-P-3)]x?Gro?(1-P-3)]x?Gro?(1-P-3)x?Gro?(1-P-6)aDGlcp(1-2)[LIP(1-2)[LIP(1-3)]x?Gro?(1-P-6)]aDGlcp(1-3),LIP(1-2)]x?Gro?

[1*]OCC(CO[C@H]1O[C@H](COP(=O)(O)OCC(CO[1*])O[1*])[C@@H](O)[C@H](O)[C@H]1O[C@H]1O[C@H](COP(=O)(O)OCC(O)COP(=O)(O)OCC(COP(=O)(O)OCC(COP(=O)(O)OCC(COP(=O)(O)OCC(COP(=O)(O)OCC(COP(=O)(O)OCC(O)CO)OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2OC2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](O)[C@H](O)[C@H]1O)O[1*]

SVG MW SMILES 3D mol Ionize

R1 = LIP
Warning = sub-repeat ending at xXP?: variable unit count (12-31) was assumed to be 12
Warning = sub-repeat ending at xXP?: large unit count (12) was reduced to 5