Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.1.53 (sialidase)
2,694 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the present work, gustatory glands (von Ebner's glands) of the horse tongue were examined by means of five peroxidase-conjugated lectins (PNA, DBA, SBA, UEA I, WGA), with and without prior sialidase digestion, in order to investigate the presence and distribution of carbohydrate residues in secretory cells and duct cells. The most intense staining of secretory cells was observed with PNA after pre-treatment with neuraminidase. This indicates that the terminal trisaccharide sequence sialic acid- (alpha 2-->3, 6) galactosyl (beta 1-->3) N-acetylgalactosamine is the most frequent oligosaccharide chain present in glycoproteins secreted by horse gustatory glands. Secretory cells also contained oligosaccharides with terminal alpha-N-acetylgalactosamine and N-acetylglucosamine, whereas fucose was found in only a few glandular cells. The apical cytoplasm of duct lining cells reacted with all the lectins except WGA.
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PMID:A lectin histochemical study of gustatory (von Ebner's) glands of the horse tongue. 858 3

Nine strains of Streptococcus oralis, isolated from blood cultures of patients with infective endocarditis or from the oral cavity as part of the normal flora, were examined for their ability to elaborate sialidase (neuraminidase) and N-acetylglucosaminidase, enzymes which are involved in the degradation of glycoproteins. Both glycosidases were induced when bacteria were grown in a minimal medium supplemented with porcine gastric mucin, a model glycoprotein, and repressed when growth occurred in the presence of glucose. Cell-free extracts mucin-grown cultures expressed elevated levels of N-acetylneuraminate pyruvate-lyase (the first intracellular enzyme in the pathway of N-acetylneuraminate catabolism), N-acetylglucosamine (glcNAc)-6-phosphate deacetylase and glucosamine-6-phosphate deaminase (enzymes involved in the intracellular catabolism of GlcNAc 6-phosphate); activity of each of these intracellular enzymes was markedly repressed when bacteria were grown in media supplemented with alpha 1-acid glycoprotein, a major component of human plasma. Cells from these cultures expressed high levels of sialidase, N-acetylglucosaminidase, and the intracellular enzymes involved in the catabolism of N-acetyl-sugars released by action of these glycosidases. High-resolution 1H-NMR spectroscopy of spent culture supernatants revealed that sialic acid and GlcNAc residues of the molecularly mobile oligosaccharide side-chains of alpha 1-acid glycoprotein had been hydrolysed and the released sugars internalized by the bacteria. These data indicate that S. oralis has the ability to hydrolyse constituents of oligosaccharide side-chains of host-derived glycoproteins and to utilize simultaneously these released carbohydrates. The biochemical characteristics induced by the growth of S. oralis on glycoproteins may play a role in the survival and persistence of these bacteria at the infection site in vivo.
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PMID:Metabolism of glycoprotein-derived sialic acid and N-acetylglucosamine by Streptococcus oralis. 870 62

The pathogenicity of enterobacteria often correlates with their production of neuraminidase (sialidase). Forty-nine Helicobacter pylori isolates have therefore been examined for their production of neuraminidase and other glycosidases. All 49 isolates produced considerable neuraminidase (median 228 IU/microg protein, interquartile range 121-370), pH optimum 7.5. Nine of the 49 also produced fucosidase (median 23 IU/microg protein, interquartile range 12-39), pH optimum 7.0. Production of these enzymes did not correlate with bacterial Cag A expression or duodenal ulceration. Neutrophils exposed to neuraminidase show increased adherence to endothelium so the neuraminidase production by H. pylori could partly explain the predominant neutrophil inflammatory infiltrate seen in H. pylori-associated gastritis. Inhibition of this enzyme by use of neuraminidase-inhibitors could be a useful therapeutic approach.
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PMID:The production of neuraminidase and fucosidase by Helicobacter pylori: their possible relationship to pathogenicity. 874 5

Streptococcus pneumoniae is believed to produce more than one form of neuraminidase, but there has been uncertainty as to whether this is due to posttranslational modification of a single gene product or the existence of more than one neuraminidase-encoding gene. Only one stable pneumococcal neuraminidase gene (designated nanA) has been described. In the present study, we isolated and characterized a second neuraminidase gene (designated nanB), which is located close to nanA on the pneumococcal chromosome (approximately 4.5kb downstream). nanB was located on an operon separate from that of nanA, which includes at least five other open reading frames. NanB has a predicted size of 74.5 kDa after cleavage of a 29-amino-acid signal peptide. There was negligible amino acid homology between NanA and NanB, but NanB did exhibit limited homology with the sialidase of Clostridium septicum. NanB was purified from recombinant Escherichia coli and found to have a pH optimum of 4.5, compared with 6.5 to 7.0 for NanA. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis suggested that NanB has a molecular size of approximately 65 kDa. The discrepancy between this estimate and the size predicted from the nucleotide sequence is most likely a consequence of C-terminal processing or anomalous electrophoretic behavior.
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PMID:Cloning and characterization of nanB, a second Streptococcus pneumoniae neuraminidase gene, and purification of the NanB enzyme from recombinant Escherichia coli. 875 48

Neuraminidases have been implicated in various processes involving the interaction of pathogens and their receptor cells. Trypanosoma cruzi, the agent of Chagas disease, has an unusual neuraminidase, able to transfer bound alpha(2-3)sialic acid to a suitable acceptor rather than to water: the trans-sialidase (TcTS). This enzyme is encoded by a family of several homologous genes, some of them rendering inactive the products. We have shown that enzymatically active proteins have Tyr in position 342, whereas inactive TcTS contain a His342. We have now mutated this Tyr residue to Phe or Thr. Both mutant proteins resulted in enzymatically inactive products. Chimeras expressing parts of Salmonella typhimurium neuraminidase (NANH) and TcTS were constructed. Only the construct containing the complete NANH molecule fused to the last 272 residues of TcTS had neuraminidase activity. However this construct did not present TcTS activity. This finding suggests that other residues present in the homology region are required for TcTS activity.
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PMID:Effect of primary structure modifications in Trypanosoma cruzi neuraminidase/trans-sialidase activities. 883 1

A defect of lysosomal neuraminidase (sialidase N-acetyl-neuramine acid hydrolase EC 3.2.1.18) leads to a wide spectrum of phenotypes, the most severe of which is nephrosialidosis. A 4-year-old boy of related parents, born at term with hydrops fetalis, is reported. Hydrocephalus was detected at 2 months of age. The child's course over 3 years was characterized by slow growth and psychomotor development. He had mild hepatosplenomegaly, joint restriction, gingival hypertrophy, lens opacities and cherry-red spot. Coarse facial features and depressed nasal bridge were discreet. At the age of 3.5 years, he developed gradual progressive edema, decreased activity and increased fatigue. A diagnosis of nephrotic syndrome was made because of massive proteinuria. Thin-layer chromatography of urinary oligosaccharides revealed the presence of several abnormal sialyloligosaccharides. The diagnosis was confirmed by measurement of neuraminidase activity in cultured skin fibroblasts.
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PMID:Neuraminidase deficiency presenting as a nephrosialidosis: the first case detected in Poland. 894 16

The 35/50 kDa mucin-like surface glycoprotein (gp35/50) of Trypanosoma cruzi metacyclic trypomastigotes has been implicated in mammalian cell invasion. In this study we investigated whether the sialyl residues of gp35/50 are required for interaction of parasites with target cells. After treatment with bacterial neuraminidase, the metacyclic forms (G strain) remained reactive with the monoclonal antibody (mAb) 10D8 but lost their reactivity with mAb 3C9, that recognizes sialic acid-containing epitopes on gp35/50, and entered HeLa cells in significantly higher numbers as compared to untreated controls. Resialylation of gp35/50, by incubation of parasites with T. cruzi trans-sialidase and sialyl lactose, restored the reactivity with mAb 3C9 as well as the affinity for sialic acid specific lectin. Accordingly, the rate of invasion of resialylated parasites was reduced to levels similar to those observed before desialylation. Purified G strain gp35/50, desialylated by neuraminidase treatment, bound to HeLa cells more than its sialylated counterpart. The Ca2+ signaling activity, which has been associated with cell invasion, was also determined by measuring the cytosolic Ca2+ concentration ([Ca2+]i), in HeLa cells upon interaction with sonicated extracts from untreated or neuraminidase-treated parasites, or with purified gp35/50 in its sialylated or desialylated form. Consistent with the results of cell invasion assay, the desialylated parasite preparations, as well as the sialic acid free gp35/50, induced an average elevation in [Ca2+]i significantly higher than that triggered by untreated controls. None of these effects, namely the increase in infectivity and Ca2+ signaling activity, was observed with neuraminidase-treated CL strain metacyclic trypomastigotes, which express a variant form of sialic acid gp35/50 molecule that is not recognized by mAb 10D8 and apparently is not involved in target cell invasion.
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PMID:Removal of sialic acid from mucin-like surface molecules of Trypanosoma cruzi metacyclic trypomastigotes enhances parasite-host cell interaction. 904 21

Activation of peripheral blood CD4+ helper T lymphocytes establishes a permissive state for growth of HIV-1. Activated T lymphocytes expressed increased sialidase (neuraminidase) activity and were hyposialylated. Treatment of freshly isolated peripheral blood mononuclear cells (PBMCs) with microbial neuraminidase (NANase) or phytohemagglutinin (PHA) prior to infection at low multiplicity with T cell line-adapted HIV-1IIIB resulted in production of large amounts of p24 antigen and reverse transcriptase. In contrast, neither viral component was detected in the medium of mock-treated cells infected at a similar multiplicity through 21 days in culture. The titer of a stock solution of HIV-1IIIB was 1.4 +/- 0.18 log10 greater in NANase-treated PBMCs than in mock-treated cells; the titer was similarly raised 1.5 to 1.76 +/- 0.18 log10 in PHA-treated cells. Growth of the primary isolate HIV-1(91/US/056) was also enhanced in NANase-treated PBMCs; the titer of a stock solution of HIV-1(91/US/056 was 1.0 +/- 0.16 log10 greater in NANase-treated PBMCs than in mock-treated cells 7 days after infection. No enhancement of viral growth in PBMCs was detected when NANase was heat-inactivated or specifically inhibited with 2,3-dehydro-2-desoxy-N-acetyl-neuraminic acid prior to use. Treatment of PBMCs with NANase did not alter the distribution of lymphocyte subsets nor change the density of CD4 antigen per cell after 7 days in culture. Whereas PHA treatment of PBMCs was mitogenic, pretreatment with NANase was not; the amount of [3H]thymidine incorporated into DNA and culture growth characteristics were similar for NANase- and mock-treated cells. Thus, desialylation of PBMCs promoted a permissive state for growth of HIV-1 without affecting the rate of DNA synthesis or relative number of target CD4+ cells.
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PMID:Desialylation of peripheral blood mononuclear cells promotes growth of HIV-1. 912 18

Serum neuraminidase (NA, sialidase) activity has been demonstrated in acute poststreptococcal glomerulonephritis (APSGN) and implicated in the pathogenesis of the disease. Recent investigations show that neuraminidase-treated leukocytes accumulate preferentially in kidneys; therefore, we were interested in knowing if desialized cells infiltrate the kidney in APSGN. We first tested the capacity of peanut agglutinin lectin (PNA) to detect injected NA-treated leukocytes in the kidney of rats. NA-treated leukocytes were transfused and desialized cells were identified with fluorescein-conjugated peanut lectin (FITC-PNA) in renal tissue. PNA positive cells were identified in rat kidneys 3 hours after injection (glomeruli: 1.67 +/- 0.19 cells/g.c.s.; interstitium: 0.50 +/- 0.12 cells/int). Sections from available renal biopsy material of APSGN (n = 11), other glomerulonephritis (n = 28) and normal kidneys (n = 5) were double-stained with FITC-PNA and with monoclonal antibody to the CD11b molecule, which is expressed on polymorphonuclear and monocytes the main types of infiltrating cells during APSGN. Desialized (FITC-PNA positive) cells were found in the glomeruli (2.17 +/- SEM 0.22 cells per glomerular cross section, g.c.s.) and interstitium (0.61 +/- 0.15 cells per 0.0625 mm2, int) in all biopsies of APSGN. Only in 2 of 28 other glomerulonephritis showed desialized cells. More than 80% of the PNA positive cells in APSGN expressed the CD11b molecule and the infiltration was more intense in early biopsies. In conclusion, desialized leukocytes represent a significant part of the inflammatory infiltrate in APSGN. This finding gives support for a role of NA in the disease and provides clinical validation for a mechanism of renal cellular infiltration suggested by experimental observations.
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PMID:Histological evidence of neuraminidase involvement in acute nephritis: desialized leukocytes infiltrate the kidney in acute post-streptococcal glomerulonephritis. 912 87

Neuraminidase (sialidase), a potential virulence factor in bacteria, was demonstrated in Haemophilus parasuis, an invasive swine pathogen, but not in four other pathogens of the Pasteurellaceae family: H. influenzae, H. somnus, H. paragallinarum, or Actinobacillus pleuropneumoniae. H. parasuis neuraminidase had an acidic pH optimum and a specificity for several substrates also cleaved by other bacterial neuraminidases. Similar to the neuraminidase of Pasteurella multocida, H. parasuis neuraminidase was cell associated and did not require divalent cations for activity. Exogenous sialic acid added to growth medium of H. parasuis was cleared after a lag of about 10 h and these cultures grew to a greater final density than cultures without added sialic acid, indicating that exogenous sialic acid is metabolized. The role of sialidase in providing nutrients to H. parasuis may be an important factor in its obligate parasitism.
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PMID:Neuraminidase (sialidase) activity of Haemophilus parasuis. 923 20


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