Antiviral effect of oryzacystatin, a proteinase inhibitor in rice, against herpes simplex virus type 1 in vitro and in vivo

Aoki, Hiizu; Akaike, Takaaki; K, Abe; Kuroda, Marcelo J.; Arai, Soichi; Okamura, R; Negi, Akira; Maeda, Hiroshi

doi:10.1128/aac.39.4.846

Cited by 56 publications

(39 citation statements)

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“…Oryzacystatins have been shown to be potent inhibitors of herpes simplex virus-1 (HSV-1) replication following virus adsorption to monkey kidney epithelial cells (Aoki et al, 1995). Significantly, daily administration for one week of 7.5 g of oryzacystatin I as eye drops to mice that had received a lethal eye innoculum of HSV-1 led to a 67% survival rate after 14 days, compared with 0% in the controls.…”

Section: (4) Antimicrobial and Antiviral Activitiesmentioning

confidence: 99%

Salivary (SD-Type)Cystatins:OverOneBillionYears in theMaking—But toWhatPurpose?

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

101

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The cystatin superfamily is comprised of a large group of ancestrally related proteins, most of which are potent inhibitors of cysteine peptidases (CPs). Human saliva contains relatively abundant proteins that are related ancestrally in sequence to the cystatin superfamily. These proteins are now commonly referred to as 'salivary cystatins', although this is something of a misnomer (see below). It has been several years since the publication of the last comprehensive reviews that focused on the salivary cystatins (Bobek and Levine, 1992;Henskens et al., 1996c). Since then, significant advances have been made regarding the gene organization, protein structure, and properties of human and rat proteins. Therefore, a major purpose of this article is to review this recent work. What is the function of the 'salivary cystatins'? Despite a great deal of research effort, we still do not have a definitive answer to this question. A major impediment is the lack of a disease to associate with a specific defect in a gene: Functionality must be inferred from circumstantial evidence. A central premise of this review is that clues to 'salivary cystatin' function are contained within their phylogenetic history, and that by looking at established or likely functions of their 'siblings' and 'cousins', one can assess the likelihood of this function(s) continuing into the 'salivary cystatins'. A comprehensive review of the large cystatin superfamily is beyond the scope of a single article. This review will aim to outline the main branches of the superfamily and the common elements of their structure and function, but will pay closest attention to the nearest relatives of the 'salivary cystatins'.(1) BACKGROUND Scission of peptide bonds is an essential reaction in living cells, and there is a considerable number of peptidases that catalyze this reaction with various degrees of specificity. CPs use a cysteine residue in the active site as the nucleophile in the reaction (see Dickinson, 2002, and references therein). Release of proteolytic enzymes outside of their normal compartment has the potential to cause serious degradation and pathology-an effect taken advantage of by pathogenic organisms from a wide range of phyla. Therefore, control of proteolytic enzyme activity is mandatory. Building upon a very early report (see Barrett et al., 1986, for a review of this earlier literature) of a bovine trypsin inhibitor in chicken egg white, a search for egg white inhibitors of plant proteinases (the CPs ficin and papain) identified a relatively small (12.7 kDa) protein that was a potent inhibitor (Ki = 10 nM). The term cystatin was coined for this protein, which was shown also to inhibit mammalian CPs of the papain superfamily, including cathepsins B, C, H, and L. Cystatins form 1:1 reversible complexes with CPs, in competition with the substrate, but in some cases the binding is so tight as to be physiologically irreversible. (2) THE CYSTATIN SUPERFAMILYExamination of mammalian tissues and serum revealed several CP inhibitors ranging in si...

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Section: (4) Antimicrobial and Antiviral Activitiesmentioning

confidence: 99%

Salivary (SD-Type)Cystatins:OverOneBillionYears in theMaking—But toWhatPurpose?

Dickinson

2002

Critical Reviews in Oral Biology & Medicine

101

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“…In addition to their other biological functions, cystatins have been shown to inhibit RNA virus-induced programmed cell death (Björklund et al, 1997). Moreover, the antiviral properties of cystatins (Björck et al, 1990;Aoki et al, 1995;Gu et al, 1995;Collins & Grubb, 1998) suggest that they may also inhibit cysteine proteases used by viruses during infection.…”

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confidence: 99%

The cysteine protease inhibitors cystatins inhibit herpes simplex virus type 1-induced apoptosis and virus yield in HEp-2 cells

Peri

Hukkanen

Nuutila

et al. 2007

Journal of General Virology

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The role of cystatins in herpes simplex virus (HSV)-induced apoptosis and viral replication has been studied. Human epithelial (HEp-2) cells infected with wild-type HSV-1 (F), with a deletion virus lacking the anti-apoptotic gene Us3 (R7041) or with a deletion virus lacking the anti-apoptotic genes Us3 and ICP4 (d120) were treated with cystatin A, C or D. Cells and culture media were studied at different time points for replicating HSV-1 and for apoptosis. Cystatins C and D inhibited the yield of replicative HSV-1 significantly in HEp-2 cells. In addition, cystatin D inhibited R7041 and d120 virus-induced apoptosis. Moreover, cystatin A inhibited R7041-induced apoptosis. These inhibitory effects of cystatins on virus replication and apoptosis are likely to be separate functions. Cystatin D treatment decreased cellular cathepsin B activity in HSV-1 infection, suggesting that cathepsin B is involved in virus-induced apoptosis.

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“…The antiviral eŠects of oryzacystatins have been reported. 14,15) The antiviral eŠects of Job's tears may also arise from an inhibition of virus proteinases. A cystatin from Job's tears might strongly inhibit the proliferation of viruses.…”

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confidence: 99%