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High resolution electrospray ionization tandem mass spectrometry (HR-ESI–MS/MS) was used to analyze cardiolipins (Ptd 2Gro) including their plasmalogen forms from three species of the anaerobic beer-spoilage bacterial genus Pectinatus. Cardiolipins including their plasmalogens were analyzed by HR-ESI–MS/MS on Orbitrap and almost 100 cardiolipins (i.e. tetra-acyl—Ptd 2Gro, plasmenyl-tri-acyl—PlsPtd 2Gro, and di-plasmenyl-di-acyl—Pls 2Ptd 2Gro) of three classes were identified. The structures of the molecular species that consist of various regioisomers and structurally similar compounds were revealed in detail. The high resolution mass spectrometry allowed the unambiguous structural assignment of Ptd 2Gro, PlsPtd 2Gro, and Pls 2Ptd 2Gro in the three species of Pectinatus, which contain predominantly odd numbered fatty acids. [ABSTRACT FROM AUTHOR]

Liquid chromatography-electrospray tandem mass spectrometry (LC/ESI-MS/MS) was used to analyze phospholipids from three species of the anaerobic beer-spoilage bacterial genus Pectinatus. Analysis of total lipids by HILIC (Hydrophilic Interaction Liquid Chromatography) column succeeded in separating diacyl- and plasmalogen phospholipids. Plasmalogens were then analyzed by means of the ESI-MS/MS and more than 220 molecular species of four classes of plasmalogens (PlsCho (choline plasmalogen), PlsEtn (ethanolamine plasmalogen), PlsGro (glycerol plasmalogen), and PlsSer (serine plasmalogen)) were identified. Major molecular species were c-p19:0/15:0 PlsEtn and PlsSer, which accounted for more than 4% of the total lipids. [ABSTRACT FROM AUTHOR]

Flagellin proteins lacking the N- or C-terminus form polymers of reduced filament stability and straight morphology, in contrast In the coiled native flagella. In the present study, the N-terminal amino acid sequence of flagellins of the anaerobic beer spoilage bacteria Pectinatus cerevisiiphilus and Pectinatus frisingiensis as well as Enterobacter aerogenes and Pseudomonas sp. were determined. Sequence similarity was revealed between these and the N-termini of all known eubacterial flagellins. Synthetic peptides corresponding to the first 15 amino acid residues of the flagellins of Pectinatus, Campylobacter jejuni, E. aerogenes or Proteus mirabilis flagellins had a spontaneous tendency under physiological conditions to form 4–6 nm broad, 1–2 μn long fibrillar structures that had a tendency to form clusters. In contrast, the Pectinatus peptide missing residues 1–3 did not form fibrils. The peptide missing residues 13–15 formed fibrils less easily, and the peptide missing residues 11–15 formed fibrils almost without clustering. In electron micrographs, the fibrillisation of the bacterial flagellar peptides resembled that of β-amyloid and prion peptides. 1H-NMR and infrared spectroscopy studies with homology analysis indicate that although the flagellar N-terminal peptides are flexible with many conformational minima, they have a significant tendency to form β-type structures and a loop in the middle of the peptide. The hydrophobic character of the N-terminus together with the property of forming a conserved β-strand-loop-β-strand motif may be related to a mechanism involved in attaining the propel morphology and stability of the flagellar filament, by providing a device for facilitating the attachment of the flagellin monomers to each other. The flagellar peptides represent a new class of fibril-forming peptides. [ABSTRACT FROM AUTHOR]

Mild acid hydrolysis of the smooth-type lipopolysaccharide (LPS) of Pectinatus frisingensis afforded no polysaccharide but monomeric 6-deoxy-L-altrose (L-6dAlt) which was identified by anion-exchange chromatography in borate buffer, GLC/MS, 1H-NMR spectroscopy, and optical rotation. LPS was degraded with alkali under reductive conditions to give a completely O-deacylated polysaccharide, which was studied by methylation analysis, 1H-NMR and 13C-NMR spectroscopy, including sequential, selective spin-decoupling, two-dimensional correlation spectroscopy (COSY), COSY with relayed coherence transfer, two-dimensional heteronuclear 13C, 1H-COSY, one-dimensional NOE and two-dimensional rotating-frame NOE spectroscopy. It was found that the O-specific polysaccharide chain of P. frisingensis LPS is a homopolymer of 6-deoxy-L-altrofuranose built up of tetrasaccharide-repeating units having the following structure: [This text does not exist in ASCII] Similarly, mild acid degradation of smooth-type LPS of Pectinatus cerevisiiphilus resulted in depolymerisation of the polysaccharide chain to give a disaccharide consisting of D-glucose and D-fucose. Study of the disaccharide by methylation analysis and alkali-degraded LPS by one-dimensional and two-dimensional 1H-NMR and 13C-NMR spectroscopy showed that the O-specific polysaccharide of P. cerevisiiphilus has the following structure: →2)-β-D-Fucf-(1→2)-α-D-Glcp-(1→. [ABSTRACT FROM AUTHOR]