Ornithobacterium rhinotracheale has neuraminidase activity causing desialylation of chicken and turkey serum and tracheal mucus glycoproteins

ZusammenfassungDieser Artikel gibt einen Überblick über die von Bordetella avium, Gallibacterium anatis, Ornithobacterium rhinotracheale, Riemerella anatipestifer sowie Enterococcus cecorum verursachten Erkrankungen beim Geflügel. Die Identifizierung dieser nahezu ausschließlich bei Vögeln vorkommenden bakteriellen Erreger mithilfe biochemischer Methoden wird erläutert und alternative molekularbiologische Identifikationsmethoden werden diskutiert.

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Exemplar Abstract for Ornithobacterium rhinotracheale Vandamme et al. 1994.

The NamesforLife Abstracts ◽

10.1601/ex.17403 ◽

2003 ◽

Author(s):

Charles Thomas Parker ◽

Dorothea Taylor ◽

George M Garrity

Keyword(s):

Ornithobacterium Rhinotracheale

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Primary structure determination of five sialylated oligosaccharides derived from bronchial mucus glycoproteins of patients suffering from cystic fibrosis. The occurrence of the NeuAc alpha(2----3)Gal beta(1----4)[Fuc alpha(1----3)] GlcNAc beta(1----.) structural element revealed by 500-MHz 1H NMR spectroscopy.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)47263-2 ◽

1984 ◽

Vol 259 (14) ◽

pp. 9051-9058 ◽

Cited By ~ 13

Author(s):

G Lamblin ◽

A Boersma ◽

A Klein ◽

P Roussel ◽

H van Halbeek ◽

...

Keyword(s):

Cystic Fibrosis ◽

Nmr Spectroscopy ◽

1H Nmr ◽

Structure Determination ◽

Primary Structure ◽

1H Nmr Spectroscopy ◽

Structural Element ◽

Bronchial Mucus ◽

Mucus Glycoproteins

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Neuraminidase activity in the mucolipidoses (types I, II and III) and the cherry-red spot myoclonus syndrome

Clinica Chimica Acta ◽

10.1016/0009-8981(79)90031-7 ◽

1979 ◽

Vol 99 (2) ◽

pp. 97-105 ◽

Cited By ~ 18

Author(s):

M. Potier ◽

G. Beauregard ◽

M. Bélisle ◽

L. Mameli ◽

V.Nguyen Hong ◽

...

Keyword(s):

Neuraminidase Activity ◽

Cherry Red Spot

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Calcospherite-like bodies and caseous necrosis in tracheal mucus from a dog with tuberculosis

Veterinary Clinical Pathology ◽

10.1111/j.1939-165x.2004.tb00369.x ◽

2004 ◽

Vol 33 (3) ◽

pp. 168-172 ◽

Cited By ~ 6

Author(s):

Natali B. Bauer ◽

Emma O'Neill ◽

Brian J. Sheahan ◽

Joseph Cassidy ◽

Hester McAllister

Keyword(s):

Caseous Necrosis ◽

Tracheal Mucus

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SERUM NEURAMINIDASE ACTIVITY IS INCREASED IN CRITICALLY ILL PATIENTS.

Critical Care Medicine ◽

10.1097/00003246-200612002-00036 ◽

2006 ◽

Vol 34 ◽

pp. A9

Author(s):

Alessandro Rapotec ◽

Michael Piagnerelli ◽

Jean-Louis Vincent ◽

Karim Zouaoui Boudjeltia ◽

Thibaut Richard ◽

...

Keyword(s):

Critically Ill ◽

Critically Ill Patients ◽

Neuraminidase Activity

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Mechanism of Interference Mediated by Human Parainfluenza Virus Type 3 Infection

Journal of Virology ◽

10.1128/jvi.74.24.11792-11799.2000 ◽

2000 ◽

Vol 74 (24) ◽

pp. 11792-11799 ◽

Cited By ~ 21

Author(s):

Maria-Arantxa Horga ◽

G. Luca Gusella ◽

Olga Greengard ◽

Natalia Poltoratskaia ◽

Matteo Porotto ◽

...

Keyword(s):

Virus Type ◽

Fluorescent Protein ◽

Parainfluenza Virus ◽

Wild Type ◽

Challenge Virus ◽

Neuraminidase Activity ◽

Definitive Evidence ◽

Viral Interference ◽

Human Parainfluenza Virus ◽

Type 3

ABSTRACT Viral interference is characterized by the resistance of infected cells to infection by a challenge virus. Mechanisms of viral interference have not been characterized for human parainfluenza virus type 3 (HPF3), and the possible role of the neuraminidase (receptor-destroying) enzyme of the hemagglutinin-neuraminidase (HN) glycoprotein has not been assessed. To determine whether continual HN expression results in depletion of the viral receptors and thus prevents entry and cell fusion, we tested whether cells expressing wild-type HPF3 HN are resistant to viral infection. Stable expression of wild-type HN-green fluorescent protein (GFP) on cell membranes in different amounts allowed us to establish a correlation between the level of HN expression, the level of neuraminidase activity, and the level of protection from HPF3 infection. Cells with the highest levels of HN expression and neuraminidase activity on the cell surface were most resistant to infection by HPF3. To determine whether this resistance is attributable to the viral neuraminidase, we used a cloned variant HPF3 HN that has two amino acid alterations in HN leading to the loss of detectable neuraminidase activity. Cells expressing the neuraminidase-deficient variant HN-GFP were not protected from infection, despite expressing HN on their surface at levels even higher than the wild-type cell clones. Our results demonstrate that the HPF3 HN-mediated interference effect can be attributed to the presence of an active neuraminidase enzyme activity and provide the first definitive evidence that the mechanism for attachment interference by a paramyxovirus is attributable to the viral neuraminidase.

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