Trypsin Action on the Growth of Sendai Virus in Tissue Culture Cells

Muramatsu, Michiko; Homma, M.

doi:10.1111/j.1348-0421.1980.tb00569.x

Cited by 59 publications

(2 citation statements)

References 28 publications

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“…2 C). For most paramyxoviruses, the cleavage activation event is believed to occur in the trans Golgi network, through the action of cellular furin-like proteases during F protein transport to the cellular surface ( Homma, 1971 , Homma and Ohuchi, 1973 , Muramatsu and Homma, 1980 , Scheid and Choppin, 1974 ). For Henipaviruses, the F 0 protein is recycled from the cell surface by endocytosis into endosomes, where it is cleaved by cathepsin L ( Diederich et al, 2005 , Pager et al, 2006 , Pager and Dutch, 2005 ).…”

Section: Cleavage By Cellular and Tissue Proteases Converts F Into Anmentioning

confidence: 99%

Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry

2015

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The Paramyxoviridae include some of the great and ubiquitous disease-causing viruses of humans and animals. In most paramyxoviruses, two viral membrane glycoproteins, fusion protein (F) and receptor binding protein (HN, H or G) mediate a concerted process of recognition of host cell surface molecules followed by fusion of viral and cellular membranes, resulting in viral nucleocapsid entry into the cytoplasm. The interactions between the F and HN, H or G viral glycoproteins and host molecules are critical in determining host range, virulence and spread of these viruses. Recently, atomic structures, together with biochemical and biophysical studies, have provided major insights into how these two viral glycoproteins successfully interact with host receptors on cellular membranes and initiate the membrane fusion process to gain entry into cells. These studies highlight the conserved core mechanisms of paramyxovirus entry that provide the fundamental basis for rational anti-viral drug design and vaccine development.

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Section: Cleavage By Cellular and Tissue Proteases Converts F Into Anmentioning

confidence: 99%

Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry

2015

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“…For most paramyxoviruses, the fusion protein is cleaved by cellular furin-like proteases in the trans Golgi network during cell surface trafficking or extracellular Clara cell-type tryptases present in the respiratory tract or embryonated egg allantoic fluid [115][116][117][118][119][120][121]. For HNVs, the premature F protein is endocytosed from the cell surface and cleaved by cathepsin L or cathepsin B in the endosome [122][123][124][125][126][127] and then re-cycled back to the cell surface.…”

Section: The Paramyxovirus Fusion Protein: the Energetic Facilitator mentioning

confidence: 99%

Differential Features of Fusion Activation within the Paramyxoviridae

Azarm

Lee

2020

Viruses

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Paramyxovirus (PMV) entry requires the coordinated action of two envelope glycoproteins, the receptor binding protein (RBP) and fusion protein (F). The sequence of events that occurs during the PMV entry process is tightly regulated. This regulation ensures entry will only initiate when the virion is in the vicinity of a target cell membrane. Here, we review recent structural and mechanistic studies to delineate the entry features that are shared and distinct amongst the Paramyxoviridae. In general, we observe overarching distinctions between the protein-using RBPs and the sialic acid- (SA-) using RBPs, including how their stalk domains differentially trigger F. Moreover, through sequence comparisons, we identify greater structural and functional conservation amongst the PMV fusion proteins, as compared to the RBPs. When examining the relative contributions to sequence conservation of the globular head versus stalk domains of the RBP, we observe that, for the protein-using PMVs, the stalk domains exhibit higher conservation and find the opposite trend is true for SA-using PMVs. A better understanding of conserved and distinct features that govern the entry of protein-using versus SA-using PMVs will inform the rational design of broader spectrum therapeutics that impede this process.

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An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo.

et al. 1990

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Host cell proteases responsible for activation of viral fusion glycoproteins are an important determinant for spread and tropism of various animal viruses. Exemplifying such proteases for the first time, we isolated an endoprotease from chick embryo, that activates para‐ and orthomyxovirus fusion glycoproteins by cleaving their precursor proteins at a specific, single arginine site. The protease is a calcium dependent serine protease consisting of two subunits, the 33 kd catalytic chain and the 23 kd chain possibly required for Ca2+ binding, and was found to be highly homologous, if not identical, to the blood clotting factor X(FX), a member of the prothrombin family. Its high efficiency and specificity in cleavage reactions was attributable to the properties characteristic of FX. Its role in vivo was strongly supported by cleavage inhibition in ovo highly selective for this virus group with a specific peptide inhibitor against FX.

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Trypsin Action on the Growth of Sendai Virus in Tissue Culture Cells

Cited by 59 publications

References 28 publications

Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry

Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry

Differential Features of Fusion Activation within the Paramyxoviridae

An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo.

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