Viral therapy: Prospects for protease inhibitors

Korant, Bruce D.; Towatari, Takae; Ivanoff, Lucinda A.; Pettewa, Steven Y.; Brzin, Jože; Lenarčič, Brigita; Türk, Vito

doi:10.1002/jcb.240320202

Cited by 52 publications

(32 citation statements)

References 8 publications

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“…Table I shows the inhibition of the viral CPE by various cysteine proteinase inhibitors. OC-I and OC-II are apparently potent antiviral agents against poliovirus at a concentration of 8 nmol/ml, similar to the inhibitory effect of egg white cystatin reported previously [6]. The truncated oryzacystatin-I mutant, tOC-I, is also effective.…”

Section: Febs Le'frerssupporting

confidence: 83%

“…If internalized, therefore, cystatins, a family of proteinaceous cysteine proteinase inhibitors, might be excepted to inhibit the replication of picornaviruses in infected cells. In fact, egg white cystatin has been shown to exhibit this type of inhibitory action [6]. Recently, cystatin C, which exists in human blood, tears and bone marrow, has also been reported to have an antiviral effect against herpesvirus [7].…”

Section: Introductionmentioning

confidence: 99%

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Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells

et al. 1992

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Poliovirus, a picornavirus family member, requires the processing of its poly-protein by its own cystein¢ protcinasc for replication. Oryzacystatin-I and oryza~statin-lI, proteinaceous cysteine proteinase inhibitors (cystatins) of rice seed orisin, were found to inhibit the replication of poliovirus effectively in infected Veto cells in vitro. Truncated oryzacystatin-I, which lacks the NH.,-terminal 25 amino acid residues of the intact protein, is an even more effective inhibitor, eliciting its effect at concentrations of less than 0.25 nmol/ml. The low molecular weight cysteine proteinase inhibitors, E-64, E-64C and loxistatin, showed no anti-viral effect at any concentration investigated.

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Section: Febs Le'frerssupporting

confidence: 83%

Section: Introductionmentioning

confidence: 99%

Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells

et al. 1992

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“…High concentrations of stefin A selectively localized Table 1 Inhibition constants (Ki,,,) [23,24]. There is an abundance of stefin A mRNA in chemically induced mouse skin papillomas but a decrease in mRNA with progression to carcinomas [8].…”

Section: Discussionmentioning

confidence: 99%

Bacterial expression of human cysteine proteinase inhibitor stefin A

et al. 1989

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Stefin A, a cysteine proteinase inhibitor of the cyst&in superfamily, has been found to be most abundant in epidermal cells. In order to determine its ~llular function, we have expressed human stefln A in ~cherich~ coli using plasmid expression vectors under the control of bacteriophage T7 RNA polymerase. The heat-stable, antibody-~sitive bacterial product was isolated using a papain-Sharon affinity column and was shown to inhibit two cysteine proteinases, papain and human cathepsin B. Recombinant stefin A may have commercial and therapeutic potential in situations requiring inhibition of cysteine proteinase activities, and in cosmetics, as an ingredient in skin creams.

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“…Sphingosine and Hl histone in the epidermis have been reported to have antimicrobial and antifungal activities [17,18]. However, proteinase inhibitors have also been reported to have antiviral, antimicrobial, and antifungal activities [5][6][7]19,20]. Moreover, it is well known that Staphylococcus aureus is increased on the skin surface of the lesions of atopic dermatitis.…”

Section: I3i!xxdonmentioning

confidence: 99%

“…Korant et al [5,6] reported that egg white cystatin inhibited the cysteine proteinase of the picoma virus and inhibited the processing of the virus precursor protein. It was found that the replication of Herpes simplex was blocked by cystatin C [7].…”

Section: Introductionmentioning

confidence: 99%

Inhibition of growth and cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin α in skin cornified envelope

Takahashi¹,

Tezuka²,

Katunuma³

1994

FEBS Letters

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The activity of a cysteine proteinase purified from Staphylococcus aureus V8 (SAVI) was inhibited by phosphorylated cystatin a (Pqstatin a) and by purified corn&d envelope protein of newborn rat, a conjugated form of P-cyst&in a. Immunohistochemical analysis demonstrated a marked decrease in P-cystatin a content in conrifled envelope treated with sphingosine. The inhibition of papain activity by proteins from sphingosine-treated skin was much weaker than that exerted by proteins from the untreated skin. The suppression of SAVI colony formation inoculated on the sphingosin~treated skin was examined. Colony formation on the sphingosine-treated skin was enhanced compared to that on normal skin. These findings suggest that P-cystatin a in the corn&d envelope may have a bacteriostatic barrier function against bacterial infection, such as that with SAVS.

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Viral therapy: Prospects for protease inhibitors

Cited by 52 publications

References 8 publications

Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells

Inhibitory effect of oryzacystatins and a truncation mutant on the replication of poliovirus in infected Vero cells

Bacterial expression of human cysteine proteinase inhibitor stefin A

Inhibition of growth and cysteine proteinase activity of Staphylococcus aureus V8 by phosphorylated cystatin α in skin cornified envelope

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