The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
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Identification of a novel sialic acid transporter in Haemophilus ducreyiLocalization of the domains of the Haemophilus ducreyi trimeric autotransporter DsrA involved in serum resistance and binding to the extracellular matrix proteins fibronectin and vitronectinMetabolic incorporation of unnatural sialic acids into Haemophilus ducreyi lipooligosaccharides.Characterization of lipooligosaccharides from Haemophilus ducreyi containing polylactosamine repeats.Cloning and characterization of the lipooligosaccharide galactosyltransferase II gene of Haemophilus ducreyiHaemophilus ducreyi produces a novel sialyltransferase. Identification of the sialyltransferase gene and construction of mutants deficient in the production of the sialic acid-containing glycoform of the lipooligosaccharide.The lbgAB gene cluster of Haemophilus ducreyi encodes a beta-1,4-galactosyltransferase and an alpha-1,6-DD-heptosyltransferase involved in lipooligosaccharide biosynthesisIdentification of genes involved in the expression of atypical lipooligosaccharide structures from a second class of Haemophilus ducreyi.Haemophilus ducreyi is susceptible to protegrin.Involvement of the Haemophilus ducreyi gmhA gene product in lipooligosaccharide expression and virulence.Genetic analysis of a pyocin-resistant lipooligosaccharide (LOS) mutant of Haemophilus ducreyi: restoration of full-length LOS restores pyocin sensitivityCharacterization of a WaaF (RfaF) homolog expressed by Haemophilus ducreyi.Characterization of a Haemophilus ducreyi mutant deficient in expression of cytolethal distending toxin.Expression of sialylated or paragloboside-like lipooligosaccharides are not required for pustule formation by Haemophilus ducreyi in human volunteers.Haemophilus ducreyi lipooligosaccharide mutant defective in expression of beta-1,4-glucosyltransferase is virulent in humans.Incorporation of N-acetylneuraminic acid into Haemophilus somnus lipooligosaccharide (LOS): enhancement of resistance to serum and reduction of LOS antibody binding.Identification of tandem genes involved in lipooligosaccharide expression by Haemophilus ducreyi.Characterization of a transposon Tn916-generated mutant of Haemophilus ducreyi 35000 defective in lipooligosaccharide biosynthesis.Sialylation of lipooligosaccharides is dispensable for the virulence of Haemophilus ducreyi in humansCovalent modification of Lys19 in the CTP binding site of cytidine 5'-monophosphate N-acetylneuraminic acid synthetase.Sialic acids siglec interaction: a unique strategy to circumvent innate immune response by pathogens.Role of lgtC in resistance of nontypeable Haemophilus influenzae strain R2866 to human serumMetabolic Glycoengineering with N-Acyl Side Chain Modified Mannosamines.The Hd0053 gene of Haemophilus ducreyi encodes an alpha2,3-sialyltransferase.The lipooligosaccharides of pathogenic gram-negative bacteria.Molecular characterization of Haemophilus ducreyi isolates from different geographical locations.Purification, cloning, and expression of a cytidine 5'-monophosphate N-acetylneuraminic acid synthetase from Haemophilus ducreyi.
P2860
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P2860
The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
@ast
The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
@en
type
label
The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
@ast
The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
@en
prefLabel
The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
@ast
The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
@en
P2093
P2860
P1476
The lipooligosaccharides of Haemophilus ducreyi are highly sialylated.
@en
P2093
A A Campagnari
B W Gibson
P2860
P304
P356
10.1128/JB.178.2.564-570.1996
P407
P577
1996-01-01T00:00:00Z