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1 Gal(beta1-4)GlcNac(beta1-3)Gal(beta1-4)Glc (lacto-N-neotetraose).
2 were much lower than the strains expressing lacto-N-neotetraose.
3 that recognizes the terminal disaccharide of lacto-N-neotetraose.
8 ons; a trend toward higher concentrations of lacto-N-neotetraose being associated with reduced transm
9 against RBCs can be blocked with the glycan lacto-N-neotetraose by inhibiting binding to the cell su
10 tor (ASGP-R) and the terminal lactosamine of lacto-N-neotetraose-expressing gonococcal lipooligosacch
11 ominantly ester C4b-LOS bonds were seen when lacto-N-neotetraose formed the terminus of the glycose c
12 trated that F62, but not the strains lacking lacto-N-neotetraose, formed extensive and intimate assoc
13 ed ions consistent with known LOS which have lacto-N-neotetraose (Galbeta1-->4GlcNAcbeta1-->3Galbeta1
15 dies (mAbs) 1B2(+) and 06B4(+)) and GalNAc-->lacto-N-neotetraose (gangliosyl; mAb 1-1-M+) oligosaccha
16 sult indicated that the inability to add the lacto-N-neotetraose group to the 559 LOS is not due to a
17 LOS produced by mutant 559 revealed that the lacto-N-neotetraose group which is attached to heptose I
18 dherence of F62, but not the strains lacking lacto-N-neotetraose, induced the rearrangement of actin
19 An antigen that is dependent on the glycose lacto-N-neotetraose induces IgG in humans that is bacter
20 failed to bind to immobilized sialic acid or lacto-N-neotetraose, known pneumococcal ligands on eukar
21 ce of bacteria to epithelial cells in vitro--lacto-N-neotetraose (LNnT) and its alpha2-3- and alpha2-
22 erogroup C meningococcal strains bearing the lacto-N-neotetraose (LNnT) structure on lipooligosacchar
23 he lipooligosaccharide sialic acid acceptor, lacto-N-neotetraose (LNnT), of nine meningococcal strain
26 and Neisseria meningitidis both express the lacto-N-neotetraose (LNT) lipooligosaccharide (LOS) mole
27 ely; the other (termed 398079) expressed the lacto-N-neotetraose (LNT; Galbeta1 --> 4GlcNAcbeta1 -->
28 isogenic derivative that expressed only the lacto-N-neotetraose LOS (F62 Delta lgtD), adhered to, an
29 n the absence of detectable Opa protein, the lacto-N-neotetraose LOS promotes gonococcal invasion int
30 ssing the lacto-N-neotetraose and the galNac-lacto-N-neotetraose LOS, and its isogenic derivative tha
31 e terminal Galbeta1-->4GlcNAc epitope in the lacto-N-neotetraose moiety of the wild-type LOS structur
33 ed no binding to its nonfucosylated homolog, lacto-N-neotetraose, or to oligosaccharides present on k
34 rains that express LOS molecules lacking the lacto-N-neotetraose structure were similar to that seen
35 tudies indicated that an interaction between lacto-N-neotetraose-terminal LOS and ASGP-R allows gonoc
37 ease in fucosyl-disialyl-lacto-N-hexaose and lacto-N-neotetraose was associated with 0.04% higher (P
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