| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-201 |
Sentence |
denotes |
Functional relationships of the genetic locus encoding the glycosyltransferase enzymes involved in expression of the lacto-N-neotetraose terminal lipopolysaccharide structure in Neisseria meningitidis. |
| T1 |
0-201 |
Sentence |
denotes |
Functional relationships of the genetic locus encoding the glycosyltransferase enzymes involved in expression of the lacto-N-neotetraose terminal lipopolysaccharide structure in Neisseria meningitidis. |
| T2 |
202-427 |
Sentence |
denotes |
The biosynthetic function of the lgtABE genetic locus of Neisseria meningitidis was determined by structural analysis of lipopolysaccharide (LPS) derived from mutant strains and enzymic assay for glycosyltransferase activity. |
| T2 |
202-427 |
Sentence |
denotes |
The biosynthetic function of the lgtABE genetic locus of Neisseria meningitidis was determined by structural analysis of lipopolysaccharide (LPS) derived from mutant strains and enzymic assay for glycosyltransferase activity. |
| T3 |
428-612 |
Sentence |
denotes |
LPS was obtained from mutants generated by insertion of antibiotic resistance cassets in each of the three genes lgtA, lgtB, lgtE of the N. meningitidis immunotype L3 strain phi3 MC58. |
| T3 |
428-612 |
Sentence |
denotes |
LPS was obtained from mutants generated by insertion of antibiotic resistance cassets in each of the three genes lgtA, lgtB, lgtE of the N. meningitidis immunotype L3 strain phi3 MC58. |
| T4 |
613-737 |
Sentence |
denotes |
LPS from the parent strain expresses the terminal lacto-N-neotetraose structure, Galbeta1-->4GlcNAcbeta1-->3Galbeta1-->4Glc. |
| T4 |
613-737 |
Sentence |
denotes |
LPS from the parent strain expresses the terminal lacto-N-neotetraose structure, Galbeta1-->4GlcNAcbeta1-->3Galbeta1-->4Glc. |
| T5 |
738-911 |
Sentence |
denotes |
Mild hydrazine treatment of the LPS afforded O-deacylated samples that were analyzed directly by electrospray ionization mass spectrometry (ESI-MS) in the negative ion mode. |
| T5 |
738-911 |
Sentence |
denotes |
Mild hydrazine treatment of the LPS afforded O-deacylated samples that were analyzed directly by electrospray ionization mass spectrometry (ESI-MS) in the negative ion mode. |
| T6 |
912-1073 |
Sentence |
denotes |
In conjunction with results from sugar analysis, ESI-MS revealed successive loss of the sugars Gal, GlcNAc, and Gal in lgt B, lgt A, and lgt E LPS, respectively. |
| T6 |
912-1073 |
Sentence |
denotes |
In conjunction with results from sugar analysis, ESI-MS revealed successive loss of the sugars Gal, GlcNAc, and Gal in lgt B, lgt A, and lgt E LPS, respectively. |
| T7 |
1074-1253 |
Sentence |
denotes |
The structure of a sample of O- and N-deacylated LPS derived by aqueous KOH treatment of lgt B LPS was determined in detail by two-dimensional homo- and heteronuclear NMR methods. |
| T7 |
1074-1253 |
Sentence |
denotes |
The structure of a sample of O- and N-deacylated LPS derived by aqueous KOH treatment of lgt B LPS was determined in detail by two-dimensional homo- and heteronuclear NMR methods. |
| T8 |
1254-1423 |
Sentence |
denotes |
Using a synthetic beta-GlcNAc acceptor and a beta-lactose acceptor, the glycosyltransferase activities encoded by the lgtB and lgtA genes were unambiguously established. |
| T8 |
1254-1423 |
Sentence |
denotes |
Using a synthetic beta-GlcNAc acceptor and a beta-lactose acceptor, the glycosyltransferase activities encoded by the lgtB and lgtA genes were unambiguously established. |
| T9 |
1424-1654 |
Sentence |
denotes |
These data provide the first definitive evidence that the three genes encode the respective glycosyltransferases required for biosynthesis of the terminal trisaccharide moiety of the lacto-N-neotetraose structure in Neisseria LPS. |
| T9 |
1424-1654 |
Sentence |
denotes |
These data provide the first definitive evidence that the three genes encode the respective glycosyltransferases required for biosynthesis of the terminal trisaccharide moiety of the lacto-N-neotetraose structure in Neisseria LPS. |
| T10 |
1655-1847 |
Sentence |
denotes |
From ESI-MS data, it was also determined that the Gal-deficient LPS expressed by the lgt E mutant is identical to that of the major component expressed by immunotype L3 galE-deficient strains. |
| T10 |
1655-1847 |
Sentence |
denotes |
From ESI-MS data, it was also determined that the Gal-deficient LPS expressed by the lgt E mutant is identical to that of the major component expressed by immunotype L3 galE-deficient strains. |
| T11 |
1848-1979 |
Sentence |
denotes |
The galE gene which encodes for UDP-glucose-4-epimerase plays an essential role in the incorporation of Gal into meningococcal LPS. |
| T11 |
1848-1979 |
Sentence |
denotes |
The galE gene which encodes for UDP-glucose-4-epimerase plays an essential role in the incorporation of Gal into meningococcal LPS. |