Ribotoxin restrictocin manifests anti-HIV-1 activity through its specific ribonuclease activity

Yadav, Santosh Kumar; Batra, Janendra K.

doi:10.1016/j.ijbiomac.2015.01.062

Cited by 7 publications

(7 citation statements)

References 27 publications

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“…RNase H had been developed as drug target for blocking virus replication5152. Our results demonstrated that hTRIR immunoprecipitated with hTR and digested T7 transcribed hTR in vitro .…”

Section: Discussionmentioning

confidence: 99%

Identification of an RNase that preferentially cleaves A/G nucleotides

Xie

Chen

Zhang

et al. 2017

Sci Rep

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Ribonucleases play an important role in the RNA metabolism which is critical for the localization, stability and function of mature RNA transcripts. More and more ribonucleases were discovered in recent years with the progress of technology. In the present study, we found that the uncharacterized C19orf43, a novel interacting protein of human telomerase RNA (hTR), digested T7 transcribed RNA, total cellular RNA and RNA oligos but not DNA. Thus we named this new RNase as hTRIR (human telomerase RNA interacting RNase). Genetic analysis showed that hTRIR is conserved among eukaryotic species and widely expressed in different cell lines. The RNase activity of hTRIR works in a broad temperature and pH range while divalent cations are not required. The conserved C-terminus of C19orf43 is necessary for its activity. Finally, we found that hTRIR cleaves all four unpaired RNA nucleotides from 5′ end or 3′ end with higher efficiency for purine bases, which suggested that hTRIR is an exoribonuclease. Taken together, our study showed the first evidence of the novel function of hTRIR in vitro, which provides clue to study the regulatory mechanism of hTR homeostasis in vivo.

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“…RNase H had been developed as drug target for blocking virus replication5152. Our results demonstrated that hTRIR immunoprecipitated with hTR and digested T7 transcribed hTR in vitro .…”

Section: Discussionmentioning

confidence: 99%

Identification of an RNase that preferentially cleaves A/G nucleotides

Xie

Chen

Zhang

et al. 2017

Sci Rep

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“…Hopefully more drugs will be isolated from fungi in the future and exploited to the welfare of mankind. (Orlandi et al, 1988;Rao et al, 2015;Yadav and Batra, 2015) α-sarcin from Aspergillus giganteus AVTWTCLNDQKNPKTNKYETKRLL α-sarcin immunotoxin IMTXA33αS on SW1222 cells (IC 50 = 30 nM) and LIM1215 cells (IC 50 = 70 nM) It inhibited growth of SW1222 in mice (Sacco et al, 1983;Tomé-Amat et al, 2015) …”

Section: Resultsmentioning

confidence: 99%

“…The fungal ribosome-inactivating protein restrictocin produced by Aspergillus restrictus recognized domains within the HIV-1 genome and its anti-HIV-1 activity was attributed to its specific ribonucleolytic activity (Yadav and Batra 2015). It recognized and cleaved a single phosphodiester bond specifically in a GAGA tetranucleotide located in a conserved stem and loop structure in ribosomal RNA (Nayak et al 2001).…”

Section: Fungal Proteins and Peptides With Antiviral Activitymentioning

confidence: 99%

Fungal proteinaceous compounds with multiple biological activities

Cheung

Wong

et al. 2016

Appl Microbiol Biotechnol

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Fungi comprise organisms like molds, yeasts and mushrooms. They have been used as food or medicine for a long time. A large number of fungal proteins or peptides with diverse biological activities are considered as antibacterial, antifungal, antiviral and anticancer agents. They encompass proteases, ribosome inactivating proteins, defensins, hemolysins, lectins, laccases, ribonucleases, immunomodulatory proteins, and polysaccharopeptides. The target of the present review is to update the status of the various bioactivities of these fungal proteins and peptides and discuss their therapeutic potential.

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“…Finally, it should be noted that some bacterial and fungal enzymes targeting the sarcin-ricin loop have also been reported to possess antiviral activity [2,[67][68][69][70][71][72][73].…”

Section: Citotoxicity Of Ripsmentioning

confidence: 99%

Antiviral Activity of Ribosome-Inactivating Proteins

Citores

Iglesias

Ferreras

2021

Toxins

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Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases from plants (EC 3.2.2.22) that inactivate ribosomes thus inhibiting protein synthesis. The antiviral properties of RIPs have been investigated for more than four decades. However, interest in these proteins is rising due to the emergence of infectious diseases caused by new viruses and the difficulty in treating viral infections. On the other hand, there is a growing need to control crop diseases without resorting to the use of phytosanitary products which are very harmful to the environment and in this respect, RIPs have been shown as a promising tool that can be used to obtain transgenic plants resistant to viruses. The way in which RIPs exert their antiviral effect continues to be the subject of intense research and several mechanisms of action have been proposed. The purpose of this review is to examine the research studies that deal with this matter, placing special emphasis on the most recent findings.

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Ribotoxin restrictocin manifests anti-HIV-1 activity through its specific ribonuclease activity

Cited by 7 publications

References 27 publications

Identification of an RNase that preferentially cleaves A/G nucleotides

Identification of an RNase that preferentially cleaves A/G nucleotides

Fungal proteinaceous compounds with multiple biological activities

Antiviral Activity of Ribosome-Inactivating Proteins

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