Pasteurella species and related taxa are opportunistic pathogens parasitizing on mucous membranes of higher organisms containing sialic acids. Therefore, sialidase is a virulence factor which up to now has been described to be present in P. haemolytica, P. multocida, and P. volantium. Because of some taxonomic changes and the description of many new species or still unnamed groups, the presence of sialidase and the metabolic successor enzyme, N-acetylneuraminate lyase, was investigated in 65 Pasteurella or Pasteurella-like strains. The detection of enzymes was performed by colorimetry, by paper chromatography and immunoelectrophoresis. Using bovine submaxillary mucin as substrate, sialidases were produced in all strains studied although the activities were different. Most strains but not all were positive in N-acetylneuraminate lyase, too. Taken together, the strains of Pasteurella sensu stricto showed the strongest activities of sialidase, those of the Pasteurella aerogenes complex the lowest. However, because of loss of sialidase activity during subcultivation, there is little feasibility to characterize Pasteurella species by these enzymes.
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http://dx.doi.org/10.1016/s0934-8840(11)80896-0 | DOI Listing |
Front Aging Neurosci
February 2024
Department of Neurology, Zhongnan Hospital, Wuhan University, Wuhan, China.
Background: Vascular depression (VaD) is a depressive disorder closely associated with cerebrovascular disease and vascular risk factors. It remains underestimated owing to challenging diagnostics and limited information regarding the pathophysiological mechanisms of VaD. The purpose of this study was to analyze the proteomic signatures and identify the potential biomarkers with diagnostic significance in VaD.
View Article and Find Full Text PDFSci Adv
June 2023
Department of Pediatrics, Centre Hospitalier Universitaire Sainte-Justine Research Center, University of Montreal, Montreal, QC, Canada.
Deleterious variants in acetylneuraminate pyruvate lyase (NPL) cause skeletal myopathy and cardiac edema in humans and zebrafish, but its physiological role remains unknown. We report generation of mouse models of the disease: , carrying the human p.Arg63Cys variant, and with a 116-bp exonic deletion.
View Article and Find Full Text PDFArch Biochem Biophys
January 2023
Division of Chemical Biology and Medicinal Chemistry, College of Pharmacy, University of Texas, Austin, TX, 78712, USA; Institute for Cellular and Molecular Biology, University of Texas, Austin, TX, 78712, USA. Electronic address:
Chembiochem
July 2022
Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, Nanjing, China.
Aldolases are enzymes that reversibly catalyze the cleavage of carbon-carbon bonds. Here we describe a recombinant sialic acid aldolase originating from the freshwater snail Biomphalaria glabrata (sNPL), and compare its substrate spectrum with a sialic acid aldolase originating from chicken (chNPL). In contrast to vertebrate animals which can synthesize, degrade, and incorporate sialic acids on glycoconjugate ubiquitously, snails (as all mollusks) cannot synthesize sialic acids endogenously, and therefore the biological function and substrate scope of sNPL ought to differ significantly from vertebrate sialic aldolases such as chNPL.
View Article and Find Full Text PDFCarbohydr Res
June 2022
Glycomics and Glycan Bioengineering Research Center (GGBRC), College of Food Science and Technology, Nanjing Agricultural University, 210095, Nanjing, China. Electronic address:
N-acetylneuraminic acid (sialic acid) is an abundantly found carbohydrate moiety covering the surface of all vertebrate cells and secreted glycoproteins. The human N-acetylneuraminate pyruvate lyase (NPL) interconverts sialic acid to N-acetylmannosamine and pyruvate, and mutations of the NPL gene were found to cause sialuria and impair the functionality of muscles. Here we report the soluble and functional expression of human NPL in Escherichia coli, which allowed us to study the biochemical properties of two clinically relevant NLP mutations (Asn45Asp and Arg63Cys).
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