Proteolytic cleavage by plasmin of the HA polypeptide of influenza virus: Host cell activation of serum plasminogen

Lazarowitz, Sondra G.; Goldberg, Andrew V.; Choppin, Purnell W.

doi:10.1016/0042-6822(73)90296-1

Cited by 156 publications

(86 citation statements)

References 29 publications

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“…Under normal conditions of virion maturation, hemagglutinin is cleaved into two polypeptides, followed by an increase in the infectivity of the virus [29]. The results presented here show that transglutaminase incorporates a labeled probe into a proteolytically sensitive region of hemagglutinin.…”

Section: Discussionmentioning

confidence: 64%

“…At the same time, increased labeling of hemagglutinin occurred, to an average of 3 mol [3H]putrescine/mol, suggesting the existence of internal labeling sites on the hemagglutinin polypeptide. It was shown by Lazarovitz et al [29] that hemagglutinin under normal conditions of maturation is cleaved into two peptides due to attack by plasmin. Other proteases, such as trypsin and chymotrypsin, can also generate similar peptides.…”

Section: Labeling Of Surface-membrane Proteinsmentioning

confidence: 99%

“…The membranes of the sarcoplasmic reticulum are known to contain a small number of well characterized proteins [30] and there- [29]. Protein applied 30-40 pgislot fore are well suited for transglutaminase labeling experiments.…”

Section: Labeling Of Intracellular Membranesmentioning

confidence: 99%

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The Use of Liver Transglutaminase for Protein Labeling

Iwanij

1977

European Journal of Biochemistry

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Guinea-pig transglutaminase catalyzes the formation of an amide bond between the y-carboxyl group of peptide-bound glutamine and a variety of amines, including fluorescent or spin-labeled derivatives. A systematic study was conducted with this enzyme in order to establish its usefulness as a protein-labeling technique. Transglutaminase-catalyzed amine incorporation was tested with isolated proteins, intact cells, membrane preparations, and virus particles. It was found that, due to its large molecular weight and its specificity, the transglutaminase reaction is limited to highly exposed glutamine residues. For example, proteins such as tubulin and a,-macroglobulin were modified while immunoglobulins (IgG) from a variety of sources were not, despite their high glutamine content. The peptide hormone glucagon was modified by transglutaminase, which resulted in the loss of hormonal activity.Most of the intact cells were not labeled with transglutaminase.

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Section: Discussionmentioning

confidence: 64%

Section: Labeling Of Surface-membrane Proteinsmentioning

confidence: 99%

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The Use of Liver Transglutaminase for Protein Labeling

Iwanij

1977

European Journal of Biochemistry

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“…The polypeptide of highest molecular weight, designated P, is present in small amounts and it appears to be associated with the viral ribonucleoprotein (33,34). The largest glycoprotein, designated HA, possesses hemagglutinin activity; under certain conditions it may be cleaved into two polypeptides designated HAI and HA,, although this cleavage is not essential for viral assembly (19,(35)(36)(37). The polypeptide subunit of the internal ribonucleoprotein is designated NP, and the other surface glycoprotein, the neuraminidase, is designated NA.…”

Section: Materials a N D Methodsmentioning

confidence: 99%

Assembly of lipid‐containing viruses

1974

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Enveloped viruses which form by budding a t the cell surface possess a membrane consisting of a lipid bilayer and a small number of virus-coded polypeptides. Since viral polypeptides become integral components of the plasma membrane during assembly, the process of synthesis and incorporation into membranes of these proteins may reflect the pathway of plasma membrane assembly. Electron microscopic studies have suggested that viral envelope proteins are incorporated into discrete, localized regions of the plasma membrane which serve as recognition sites for the viral nucleocapsid. In influenza virus-infected cells, viral polypeptides are associated with cytoplasmic membranes as well as the plasma membrane. The major envelope glycoprotein appears to be synthesized in rough endoplasmic reticulum, and to migrate to smooth membranes after synthesis. Glycosylation is initiated in rough membranes and progresses further in smooth membranes. Unlike the glycoproteins, the major nonglycosylated polypeptide appears t o be inserted directly into the plasma membrane. In the presence of 2-deoxyglucose o r high concentrations of glucosamine, aberrant viral glycoproteins are detected which appear t o be unglycosylated or partially glycosylated; these are associated with membranes and incorporated into virus particles of reduced infectivity. Therefore normal glycosylation is not essential for incorporation of viral glycoproteins into cellular membranes or virus particles, but is required for normal biological activity. The role of the viral neuraminidase in assembly and release has been studied using mutants defective in neuraminidase a t restrictive temperature. Under these conditions virus formation occurs, but the progeny form large aggregates a t the cell surface. Colloidal iron hydroxide staining indicates that such virus particles contain neuraminic acid, and these residues appear t o serve as receptors leading t o the extensive aggregation.

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“…This is further evidence that the activating enzyme in CAF is differentfrom chymotrypsin or elastase. Plasmin also cannot be the activating enzyme in CAF, since it was shown not to cleave the F glycoprotein of Sendai virus (25) although it cleaved the hemagglutinin polypeptide of the WSN strain of influenza virus (17)(18)(19).…”

Section: Discussionmentioning

confidence: 99%

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

Muramatsu¹,

Homma²

1980

Microbiology and Immunology

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A trypsin-like protease which is responsible for activation of Sendai virus was found in the chorioallantoic fluid (CAF) of embryonated chicken eggs. Treatment of the inactive form of Sendai virus, grown in LLC-MK2 cells, with CAF enhanced both hemolytic activity and infectivity for the cells. Soybean trypsin inhibitor restrained the enhancing activity of CAF. These results indicate that CAF contains a trypsin-like protease which activates the inactive form of Sendai virus.The activation was strongly inhibited by phenylmethylsulfonylfluoride, ethylenediaminetetraacetate, antipain, and leupeptin but not by tosyllysylchloromethylketone, suggesting that the activating enzyme in CAF is a protease similar to but not identical with trypsin. The inactive form of the virion was produced in ovo when the seed virus was inoculated along with antipain or leupeptin.In deembryonated chicken eggs in which CAF was substituted for a culture medium, multiple cycle growth occurred, but not when soybean trypsin inhibitor was present. These observations indicate that some activating enzyme, possibly the same one as found in CAF, was secreted from the chorioallantoic membrane.

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Proteolytic cleavage by plasmin of the HA polypeptide of influenza virus: Host cell activation of serum plasminogen

Cited by 156 publications

References 29 publications

The Use of Liver Transglutaminase for Protein Labeling

The Use of Liver Transglutaminase for Protein Labeling

Assembly of lipid‐containing viruses

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

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