Isolation of factor Xa from chick embryo as the amniotic endoprotease responsible for paramyxovirus activation

@article{Gotoh1992IsolationOF,
  title={Isolation of factor Xa from chick embryo as the amniotic endoprotease responsible for paramyxovirus activation},
  author={Bin Gotoh and Fumi Yamauchi and T. Ogasawara and Yoshiyuki Nagai},
  journal={FEBS Letters},
  year={1992},
  volume={296}
}
In chick embryo, certain paramyxoviruses mainly target the chorioallantois and the allantoamnion and show no extensive further spreading in the other organs. This has been explained by the possible presence of an endoprotease activating the viral fusion glycoprotein precursor in the allantoic and the amniotic fluid, and its absence in other places or organs, We previously isolated such an endoprotease from the allantoic fluid and demonstrated its identity with the clotting factor Xa. Exactly… 
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  • Y. Nagai
  • Biology, Medicine
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  • 1995
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Pretreatment of mouse and human lung cell lines with the serine protease inhibitors AEBSF or p AB or a cocktail of both prior to infection with the H1N1 or the A/Seal/Massachusetts/1/80 virus resulted in a decrease in virus replication.
Mammalian subtilisin-related proteinases in cleavage activation of the paramyxovirus fusion glycoprotein: superiority of furin/PACE to PC2 or PC1/PC3
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The cleavage activity of the mammalian subtilisin-related proteinases furin/PACE, PC2, and PC1/PC3, which are thought to be responsible for proprotein processing in either the constitutivesecretory pathway or the regulated secretory pathway, are examined.
The Tween 80 Toxicity in Chicken Embryos and Effect on the Kinetics of Newcastle Disease Virus Replication
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At high concentrations of TW80, hemorrhage-induced mortality was observed in embryos at the early stages of incubation, indicating that its toxicity to the chicken embryos was dose-dependent.
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References

SHOWING 1-10 OF 22 REFERENCES
Primary structure of the virus activating protease: from chick embryo Its identity with the blood clotting factor Xa
TLDR
Cloned and sequenced a cDNA of the protease and show that it is encoded in a single gene as a preproform with all the functional and structural domains known to be characteristic of bovine or human FX, establishing the identity between the prote enzyme and FXa.
An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo.
TLDR
An endoprotease from chick embryo is isolated, that activates para‐ and orthomyxovirus fusion glycoproteins by cleaving their precursor proteins at a specific, single arginine site and was found to be highly homologous, if not identical, to the blood clotting factor X(FX), a member of the prothrombin family.
Activation of Sendai virus infectivity by an enzyme in chicken amniotic fluid.
TLDR
Treatment of Sendai virus with chicken amniotic fluid resulted in a 10(3)- to 10(4)-fold increase in infectivity, the development of haemolysing ability, and cleavage of the F glycoprotein, suggesting that SAE may be the natural proteolytic activator of Sendae virus in a soluble form.
Purification and properties of chicken prothrombin.
TLDR
Rabbit antibody to chicken prothrombin evidenced a single line by immunoelectrophoresis against purified antigen and chicken plasma as well as a stable dimer in some preparations.
Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus.
Abstract In search of a molecular basis underlying the variations in virulence observed with different strains of Newcastle disease virus, a comparative study has been carried out on the biosynthesis…
The spread of a pathogenic and an apathogenic strain of Newcastle disease virus in the chick embryo as depending on the protease sensitivity of the virus glycoproteins.
The pathogenic strain Italien and the apathogenic strain Ulster of Newcastle disease virus have been compared with respect to organ tropism and spread of infection in 11-day-old chick embryos. After…
Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus.
TLDR
The results indicate that the small glycoprotein of paramyxoviruses is biologically active and is involved in virus-induced hemolysis, cell fusion, and the initiation of infection, and provides a biochemical basis for previously observed host-dependent variation in infectivity, and in hemolyzing and cell-fusion induced by paramyxviruses.
Modulation of morphological differentiation of human neuroepithelial cells by serine proteases: independence from blood coagulation.
TLDR
Using the inhibitor di‐isopropylfluorophosphate (DIP), it is shown that abrogation of the proteolytic activity of thrombin also results in a loss (greater than 2000 fold) of differentiation reversal activity.
Protease activation mutants of sendai virus. Activation of biological properties by specific proteases.
TLDR
Findings with pa mutants support the previous conclusion based on results with wild type virus, that a host-dependent cleavage of the F 0 protein is required for the infectivity of Sendai virus and for activation of hemolyzing and cell-fusing activities.
Purification of the fusion protein of Sendai virus: analysis of the NH2-terminal sequence generated during precursor activation.
TLDR
Since these cleavages confer infectivity upon both Sendai and influenza viruses and the ability to induce cell-to-cell fusion upon Sendai virus, the hydrophobic NH2-terminal sequences on F1 and HA2 may play a role in fusion of viral and host-cell membranes.
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