Plant Proteins with Antiviral Activity Against Human Immunodeficiency Virus

Lee‐Huang, Sylvia; Chen, Hao-Chia; Kung, Hsiang‐Fu; Huang, Peng; Nara, Peter L.; Li, Bao-Qun; Huang, Peter H. T.; Huang, Hong; Huang, Paul L.

doi:10.1007/978-1-4615-3414-3_8

Cited by 4 publications

(7 citation statements)

References 27 publications

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“…This new topological activity on DNA, that was irreversible even in the presence of high concentrations of ethidium bromide (data not shown), is in agreement with the general depurination activity of RIPs [8], and could explain the antiviral action reported for some RIPs [29]. As a control, we used dianthin 30, the RIP from Dianthus caryophyllus [1], which has been reported among the RIPs to have the strongest topological activity on DNA [29]. Notably, nigritins seem to be at least as active as dianthin 30 and much more active than the recently described basic nigrin b [16].…”

Section: Resultssupporting

confidence: 83%

“…5b, nigritins trigger the conversion of supercoiled pBlueScript SK + DNA forms to both relaxed and linear forms. This new topological activity on DNA, that was irreversible even in the presence of high concentrations of ethidium bromide (data not shown), is in agreement with the general depurination activity of RIPs [8], and could explain the antiviral action reported for some RIPs [29]. As a control, we used dianthin 30, the RIP from Dianthus caryophyllus [1], which has been reported among the RIPs to have the strongest topological activity on DNA [29].…”

Section: Resultssupporting

confidence: 79%

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Constitutive and inducible type 1 ribosome‐inactivating proteins (RIPs) in elderberry (Sambucus nigra L.)

et al. 1998

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Two novel highly basic type 1 (single chain) ribosomeinactivating proteins (RIPs) with N-glycosidase activity have been found in elderberries (the fruits of Sambucus nigra L.). Mass spectrometry of these RIPs, which we named nigritins f1 and f2, gave M r values of 24 095 and 23 565, respectively. Both proteins strongly inhibited protein synthesis in rabbit reticulocyte lysates but were inactive against plant ribosomes. Both nigritins have a similar topological activity on pBlueScript SK + DNA as that displayed by dianthin 30. Nigritin f1 is a constitutive RIP since it is present in both green and mature intact elderberries at nearly the same proportion with respect to total fruit protein. By contrast, nigritin f2 is inducible and only appeared in mature intact elderberries. Elderberries also contain two isoforms of a basic nigrin equivalent to the recently found basic nigrin b in elder bark (De Benito et al., FEBS Letters 413 (1997) 85^91).Our results indicate that probably not all plant RIPs exert the same biological function and that this may be determined by the physiological state of the tissue.z 1998 Federation of European Biochemical Societies.

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Section: Resultssupporting

confidence: 83%

Section: Resultssupporting

confidence: 79%

Constitutive and inducible type 1 ribosome‐inactivating proteins (RIPs) in elderberry (Sambucus nigra L.)

et al. 1998

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“…In addition, GAP31 and other anti-HIV proteins also exhibit ribosome-inactivating activity that hydrolyzes a glycosidic linkage between the ribose and adenine-4324 or guanine-4323 of 28S rRNA and subsequently inhibits eukaryotic protein synthesis (6)(7)(8). The dual action against both DNA and RNA demonstrated here for these series of proteins may be related to the inhibition of both infection and replication of HIV-1 by these compounds (4,5). However, the mechanism underlying this unique dual function in the anti-HIV action of these plant proteins is still elusive.…”

mentioning

confidence: 89%

“…In the effective dose range, little cytotoxicity to normal human cells and no toxicity to experimental animals were observed (1)(2)(3)(4). N-terminal analyses of these proteins revealed 10-57% amino acid sequence homologies in the first 40-60 residues (3,4). Furthermore, a homology of 48% was found between residues 1-40 ofGAP31 and residues 659-698 of Drosophila DNA topoisomerase II.…”

mentioning

confidence: 98%

“…In search of antiviral agents, we have purified proteins of plant origins, MAP30, TAP29, GAP31, DAP30, and DAP32, which have been shown to inhibit both de novo HIV-1 infection and replication of the virus in already infected cells (1)(2)(3). In the effective dose range, little cytotoxicity to normal human cells and no toxicity to experimental animals were observed (1)(2)(3)(4). N-terminal analyses of these proteins revealed 10-57% amino acid sequence homologies in the first 40-60 residues (3,4).…”

mentioning

confidence: 99%

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Human immunodeficiency virus type 1 (HIV-1) inhibition, DNA-binding, RNA-binding, and ribosome inactivation activities in the N-terminal segments of the plant anti-HIV protein GAP31.

Lee‐Huang

Kung²,

Huang³

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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GAP31 (gelonium anti-HIV protein of 31 kDa) is an anti-HIV protein which we have identified and purified from a medicinal plant, Gelonium multiflorum. It is capable of inhibiting HIV-1 infection and replication. GAP31 also exhibits DNA topoisomerase inhibitor activity and RNA N-glycosidase activity. The ability of GAP31 to interrupt both DNA and RNA functions may be related to its multiple antiviral actions. To define the roles of these activities in the anti-HIV action of GAP31, a series of peptides corresponding to the N-terminal segment of GAP31 were synthesized and assayed for the aforementioned activities of the parent molecule. A

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