Bordetella holmesii Lipopolysaccharide Hide and Seek Game with Pertussis: Structural Analysis of the O-Specific Polysaccharide and the Core Oligosaccharide of the Type Strain ATCC 51541

Abstract

Whooping cough is a highly contagious disease caused predominantly by Bordetella pertussis, but it also comprises of a pertussis-like illness caused by B. holmesii. The virulence factors of B. holmesii and their role in the pathogenesis remain unknown. Lipopolysaccharide is the main surface antigen of all Bordetellae. Data on the structural features of the lipopolysaccharide (LPS) of B. holmesii are scarce. The poly- and oligosaccharide components released by mild acidic hydrolysis of the LPS were separated and investigated by 1H and 13C NMR spectroscopy, mass spectrometry, and chemical methods. The structures of the O-specific polysaccharide and the core oligosaccharide of B. holmesii ATCC 51541 have been identified for the first time. The novel pentasaccharide repeating unit of the B. holmesii O-specific polysaccharide has the following structure: {→2)-α-l-Rhap-(1→6)-α-d-Glcp-(1→4)-[β-d-GlcpNAc-(1→3]-α-d-Galp-(1→3)-α-d-GlcpNAc-(1→}n. The SDS-PAGE and serological cross-reactivities of the B. holmesii LPS suggested the similarity between the core oligosaccharides of B. holmesii ATCC 51541 and B. pertussis strain 606. The main oligosaccharide fraction contained a nonasaccharide. The comparative analysis of the NMR spectra of B. holmesii core oligosaccharide fraction with this of the B. pertussis strain 606 indicated that the investigated core oligosaccharides were identical.

Cyanobacterial Harmful Bloom Lipopolysaccharides Induce Pro-Inflammatory Effects in Immune and Intestinal Epithelial Cells In Vitro

“…Rough and semi-rough LPS types, which are typically present in LPS isolates from G- bacteria with high endotoxin activities, such as E. coli , P. aeruginosa [ 33 , 34 , 35 , 36 , 37 , 39 ], Bordetella , or Salmonella [ 46 , 47 ], were not detected in most LPS isolated from cyanobacterial biomasses. Despite this, some samples displayed high levels of endotoxin activity (HAB-Mi and Microcystis PCC7806 LPS) or pro-inflammatory effects (HAB-Pl, HAB-Do, and HAB-Mi LPSs in intestinal cells), which were comparable to equivalent concentrations of E. coli or P. aeruginosa LPS.…”

Primary Structure of Glycans by NMR Spectroscopy

“…Even though the analysis of the anomeric region of a 1 H NMR spectrum is usually enough to perceive the chemical shift differences of diastereomeric pairs, in some cases the analysis of 13 C chemical shifts through an 1 H, 13 C-HSQC spectrum will offer better resolution. A derivatization process that uses ( S )-(+)-2-methylbutyric anhydride as reagent was first proposed by York et al and has successfully been applied in the determination of the absolute configuration of different neutral monosaccharide components (viz., d -Glc, d -Gal, l -Rha, d -Rib, d -Xyl, l -Ara, and d -GlcN) present in the EPS of Nostoc commune DRH-1, S. thermophilus ST1 (Figure ), the O-antigen polysaccharide of B. holmesii strain ATCC 51541, and glycosides from M. salicifolia bark. − An alternative derivatization method that involves the glycosylation of the free monosaccharides with ( R )- or ( S )-2-butanol was reported by Lundborg et al, and has been employed in the absolute configuration analysis of the O-antigen polysaccharides of E. coli O59 and O155, and the EPS of L. plantarum C88. ,, In the latter procedure, and when NMR spectroscopic data of standard derivatives are available, the analysis of the NMR data of the mixture can be carried out in a semiautomated manner using the component analysis module of the CASPER program …”

Krztusiec I „Efekt Czerwonej Królowej”

“…OS z przyłączonym dystalnym trójcukrem jest dodekasacharydem [9]. Struktury OS rdzenia innych bakterii z rodzaju Bordetella oraz pałeczki B. holmesii wykazują duże podobieństwo [75], dlatego OS i jego pochodne wydają się być odpowiednimi kandydatami na antygeny szczepionkowe. Glikokoniugaty OS z toksoidem tężcowym indukują powstawanie specyficznych przeciwciał, rozpoznających epitopy LPS na powierzchni komórek bakteryjnych [43].…”