The occurrence of 2'-5' oligoadenylates in Escherichia coli

Trujillo, Maria A.; Roux, Damien; Fueri, Josette P.; Samuel, D.; Cailla, H.; Rickenberg, H.V.

doi:10.1111/j.1432-1033.1987.tb13594.x

Cited by 12 publications

(13 citation statements)

References 17 publications

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“…The dsRNA required to produce 2-5A may be derived from pathogen or host RNAs; indeed, certain host mRNAs contain secondary structure that is capable of activating OAS (28). In addition, 2-5A linkages have been reported in bacteria (29) and RNase-L expression in bacteria results in cell RNA degradation and antiproliferative activity (30), suggesting that bacteria may produce endogenous activators of RNase-L. The validation of specific RNase-L substrates will provide a sensitive readout of its activity and a more physiologic system in which to dissect the source(s) of RNase-L activators in cells.…”

Section: Resultsmentioning

confidence: 99%

An essential role for the antiviral endoribonuclease, RNase-L, in antibacterial immunity

Ezelle²,

Kang

et al. 2008

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

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Type I IFNs were discovered as the primary antiviral cytokines and are now known to serve critical functions in host defense against bacterial pathogens. Accordingly, established mediators of IFN antiviral activity may mediate previously unrecognized antibacterial functions. RNase-L is the terminal component of an RNA decay pathway that is an important mediator of IFN-induced antiviral activity. Here, we identify a role for RNase-L in the host antibacterial response. RNase-L ؊/؊ mice exhibited a dramatic increase in mortality after challenge with Bacillus anthracis and Escherichia coli; this increased susceptibility was due to a compromised immune response resulting in increased bacterial load. Investigation of the mechanisms of RNase-L antibacterial activity indicated that RNase-L is required for the optimal induction of proinflammatory cytokines that play essential roles in host defense from bacterial pathogens. RNase-L also regulated the expression of the endolysosomal protease, cathepsin-E, and endosome-associated activities, that function to eliminate internalized bacteria and may contribute to RNase-L antimicrobial action. Our results reveal a unique role for RNase-L in the antibacterial response that is mediated through multiple mechanisms. As a regulator of fundamental components of the innate immune response, RNase-L represents a viable therapeutic target to augment host defense against diverse microbial pathogens.cathepsin-E ͉ interferon ͉ 2Ј, 5Ј-oligoadenylate ͉ cytokine ͉ endosome

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Section: Resultsmentioning

confidence: 99%

An essential role for the antiviral endoribonuclease, RNase-L, in antibacterial immunity

Ezelle²,

Kang

et al. 2008

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

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“…The putative (2'-5')A,, synthetase was partially purified from tobacco and found to cross-react with human-(2'-5')A,, synthetase-reactive antibodies (Sela et a]., 1987). (2'-5')A, molecules were even detected in Escherichia coli (Trujillo et al, 1987) and in some other bacteria and yeasts (Laurence et al, 1984). However, this does not necessarily mean that the same pathway is involved in all cases.…”

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confidence: 99%

The (2′‐5′)Oligoadenylate Synthetase is Present in the Lowest Multicellular Organisms, the Marine Sponges

Kuusksalu

Pihlak

Müller

et al. 1995

European Journal of Biochemistry

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We have proved the presence of (2′‐5′)oligoadenylates [(2′‐5′)An] and oligoadenylate synthetase [(2′‐5′)An synthetase] in the marine sponge Geodia cydonium. (2′‐5′)An isolated from sponge crude extract competed with authentic (2′‐5′)An for binding to polyclonal antiserum against (2′‐5′)An. HPLC analysis revealed the presence of nucleotides eluting with molecular markers for (2′‐5′)A oligomers. The biological activity of sponge (2′‐5′)An was demonstrated by inhibiting the protein biosynthesis in rabbit reticulocyte lysate. The activity of the (2′‐5′)An synthetase, present in crude sponge extract, was found to be high compared to that in mammalian interferon‐treated cell extract. The (2′‐5′)An synthetase from sponge extract binds to poly(I) · poly(C) as does the mammalian enzyme. Western blot analysis with antibodies to recombinant rat 43‐kDa (2′‐5′)An synthetase revealed in sponge immunologically related proteins with molecular masses of approximately 110, 65, 61 and 34 kDa. We conclude, that the (2′‐5′)An system has evolved from receptors and enzymes involved in cell adhesion and/or growth control.

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“…Furthermore, the isolated RNA species were not a lariat because they would have produced a different junction after digestion (i.e., a threeway junction). Moreover, the possibility that a 2Ј,5Ј-linked oligo(A) might have comigrated with PLMVd is highly unlikely, as it has been shown that most oligonucleotides of this type are usually very small (i.e., ϳ10 nt) (34). Also, it would be surprising for such an oligonucleotide to include a C/U dinucleotide and, more importantly, for this C/U dinucleotide to be the only 2Ј,5Ј-linked dinucleotide that it contains.…”

Section: Figmentioning

confidence: 99%

Natural 2′,5′-Phosphodiester Bonds Found at the Ligation Sites of Peach Latent Mosaic Viroid

Côté

Lévesque

Perreault

2001

J Virol

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Peach latent mosaic viroid (PLMVd) is a circular RNA pathogen that replicates in a DNA-independent fashion via a rolling circle mechanism. PLMVd has been shown to self-ligate in vitro primarily via the formation of 2,5-phosphodiester bonds; however, in vivo the occurrence and necessity of this nonenzymatic mechanism are not evident. Here, we unequivocally report the presence of 2,5-phosphodiester bonds at the ligation site of circular PLMVd strands isolated from infected peach leaves. These bonds serve to close the linear conformers (i.e., intermediates), yielding circular ones. Furthermore, these bonds are shown to stabilize the replicational circular templates, resulting in a significant advantage in terms of viroid viability. Although the mechanism responsible for the formation of these 2,5-phosphodiester bonds remains to be elucidated, a hypothesis describing in vivo nonenzymatic self-ligation is proposed. Most significantly, our results clearly show that 2,5-phosphodiester bonds are still present in nature and that they are of biological importance.Viroids are the smallest nucleic acid-based pathogens known to date (see references 15 and 33 for reviews). They are small (ϳ300 nucleotides [nt]), single-stranded, circular RNAs that infect higher plants and cause significant losses in agriculture. Viroids have been classified into two groups (A and B) based primarily on whether or not they possess the five typical structural domains found in the group B viroids. Further division among the 27 group B members depends on the sequence and length of the conserved central regions (7,14,33). Viroids that do not possess any kind of sequence or structural similarity with group B viroids have been classified as belonging to group A. The latter group includes the avocado sunblotch viroid, the peach latent mosaic viroid (PLMVd), and the chrysanthenum chlorotic mottle viroid (7, 15). All group A viroids possess hammerhead self-cleaving motifs and are proposed to replicate in chloroplasts (8,11,23). This localization has received recent support from the identification of a chloroplastic RNA polymerase that has the ability to replicate avocado sunblotch viroid (26). In contrast, group B viroids are localized in the nucleus, and RNA polymerase II appears to be responsible for their replication (4,18,30).In infected cells, viroids replicate in a DNA-independent manner via a rolling circle mechanism that follows either a symmetric or an asymmetric mode (6,8,33,36). The replicational intermediates of PLMVd, a 338-nt group A viroid that is the causal agent of peach latent mosaic disease (19), were recently studied by Northern blot analysis (8). PLMVd has been shown to replicate in a symmetric mode involving the accumulation of both circular and linear monomeric strands of both polarities (see Fig. 1). No multimeric conformer (i.e., intermediate) has been detected, indicating that both strands self-cleave efficiently via their hammerhead sequences. Moreover, it has been observed that monomeric linear RNAs accumulate at a high level...

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The occurrence of 2'-5' oligoadenylates in Escherichia coli

Cited by 12 publications

References 17 publications

An essential role for the antiviral endoribonuclease, RNase-L, in antibacterial immunity

An essential role for the antiviral endoribonuclease, RNase-L, in antibacterial immunity

The (2′‐5′)Oligoadenylate Synthetase is Present in the Lowest Multicellular Organisms, the Marine Sponges

Natural 2′,5′-Phosphodiester Bonds Found at the Ligation Sites of Peach Latent Mosaic Viroid

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