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1. Compound ID: 12876
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Cho-(1--P--6)--+ EtN-(1---P---P---4)-+
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a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Glcp-(1-2)-L-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-2)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_137777,IEDB_140087,IEDB_140108,IEDB_140122,IEDB_140624,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_150939,IEDB_151531,IEDB_158552,IEDB_190606,IEDB_2189047,IEDB_241118,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 5124
Apicella MA, Coffin J, Ketterer M, Post DMB, Day CJ, Jen FE, Jennings MP "Nontypeable Haemophilus influenzae Lipooligosaccharide Expresses a Terminal Ketodeoxyoctanoate In Vivo, Which Can Be Used as a Target for Bactericidal Antibody" -
mBio 9(4) (2018) e01401-8
Nontypeable Haemophilus influenzae (NTHi) is an important pathogen in individuals of all ages. The lipooligosaccharide (LOS) of NTHi has evolved a complex structure that can be attributed to a multiplicity of glycosyltransferases, the random switching of glycosyltransferase gene expression via phase variation, and the complex structure of its core region with multiple glycoform branch points. This article adds to that complexity by describing a multifunctional enzyme (LsgB) which optimally functions when the species is grown on a solid surface and which can add either a ketodeoxyoctanoate (KDO) or an N-acetylneuramic acid (Neu5Ac) moiety to a terminal N-acetyllactosamine structure of LOS. Our studies show that expression of lsgB is reduced four- to sixfold when NTHi is grown in broth. The substrate that the enzyme utilizes is dependent upon the concentration of free Neu5Ac (between 1 and 10 µg/ml) in the environment. In environments in which Neu5Ac is below that level, the enzyme utilizes endogenous CMP-KDO as the substrate. Our studies show that during in vivo growth in an NTHi biofilm, the KDO moiety is expressed by the organism. Monoclonal antibody 6E4, which binds KDO, is bactericidal for NTHi strains that express the KDO epitope at high levels. In a survey of 33 NTHi strains isolated from healthy and diseased individuals, the antibody was bactericidal (>90% kill) for 12 strains (36%). These studies open up the possibility of using a KDO-based glycoconjugate vaccine as part of a multicomponent vaccine against NTHi.IMPORTANCE Nontypeable Haemophilus influenzae is an important pathogen in middle ear infections in children, sinusitis in adults, and acute bronchitis in individuals with chronic obstructive lung disease. The organism is very well adapted to the human host environment, and this has hindered successful development of an effective vaccine. In this article, we describe a mechanism by which the bacteria decorates its surface lipooligosaccharide with a sugar unique to Gram-negative bacteria, ketodeoxyoctanoate (KDO). This sugar decoration is present during active infection and we have shown that an antibody directed against this sugar can result in killing of the organism. These data demonstrate that the lipooligosaccharide ketodeoxyoctanoate epitope may be a novel NTHi-specific candidate vaccine antigen.
Haemophilus influenzae, Lipooligosaccharide, sialic acid, vaccine, bactericidal activity, Biofilm, ELISA, keto-deoxyoctanoate, nontypeable Haemophilus influenzae
NCBI PubMed ID: 30065093Publication DOI: 10.1128/mBio.01401-18Journal NLM ID: 101519231Publisher: Washington, DC: American Society for Microbiology
Correspondence: michael-apicella@uiowa.edu
Institutions: Department of Microbiology and Immunology, Carver College of Medicine, The University of Iowa, Iowa City, Iowa, USA, Buck Institute for Age Research, Novato, California, USA, Institute for Glycomics, Griffith University, Gold Coast Campus, Southport, Queensland, Australia
Methods: DNA techniques, ELISA, Western blotting, statistical analysis, SPR, monoclonal antibodies
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2. Compound ID: 15290
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Subst-(1-2)-EtN-(1--P--6)--a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ Ste-(1-2)-+ Ste-(1-1)-+
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a-Neup5Ac-(2-3)-{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-?)-}}}b-D-Galp-(1-4)-b-D-GlcpNAc-(1-?)-a-D-Manp-(1-4)-a-D-GlcpN-(1-6)-myoIno-(1--P--3)--Gro
Subst = protein |
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Structure type: structural motif or average structure
Trivial name: procyclin glycoprotein
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130655,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140116,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_143242,IEDB_143632,IEDB_144983,IEDB_144993,IEDB_146100,IEDB_149174,IEDB_150933,IEDB_150939,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153529,IEDB_158533,IEDB_158550,IEDB_158552,IEDB_190606,IEDB_241107,IEDB_423120,IEDB_423128,IEDB_474450,IEDB_534865,IEDB_983930,SB_115,SB_116,SB_131,SB_136,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_191,SB_195,SB_196,SB_198,SB_30,SB_39,SB_44,SB_67,SB_68,SB_7,SB_72,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 5943
Heng J, Naderer T, Ralph SA, McConville MJ "Glycosylated compounds of parasitic protozoa" -
Book: Microbial Glycobiology (series: Structures, Relevance and Applications) (2010) 203-231
This chapter describes the range of glycan structures and pathways that are found in different parasitic protozoa. All parasitic protists express a range of glycoconjugates that form protective protein-rich or carbohydrate-rich surface coats. Protein-rich coats are typically found on developmental stages that inhabit nonhydrolytic niches, such as the bloodstream and nonacidified intracellular vacuoles. These coats are commonly dominated by a limited repertoire of antigenically diverse proteins that are commonly, but not always, glycosylphosphatidylinositol- (GPI-) anchored and modified with N- or O-glycans. Carbohydrate-rich coats are commonly found on developmental stages that dwell within hydrolytic environments, such as vertebrate and arthropod digestive tracts and lysosomal vacuoles. These coats are dominated by GPI-anchored glycoproteins that are heavily modified with N-glycans, O-glycans, or phosphoglycans. Free GPI glycolipids (not attached to protein) can also be abundant or dominant components of these coats. Some parasitic protists can also form highly resistant cyst stages encased within polysaccharide-rich cell walls. Considerable progress has been made in defining the structures of the surface and intracellular glycans of the parasitic protists, their biosynthesis and the role that individual components play in parasite infectivity.
O-glycosylation, Glycosylphosphatidylinositol, N-glycosylation, protozoan parasites, Phosphoglycosylation
Publication DOI: 10.1016/B978-0-12-374546-0.00012-2Publisher: Amsterdam: Elsevier
Correspondence: malcolmm@unimelb.edu.au
Editors: Moran A
Institutions: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia
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