Structural requirements of the rIn·rCn complex for Induction of human interferon

Carter, W.A.; Pitha, Paula M.; Marshall, Lewis W.; Tazawa, Ichiro; Tazawa, Setsuko; Ts’o, Paul O. P.

doi:10.1016/0022-2836(72)90560-8

Cited by 129 publications

(54 citation statements)

References 26 publications

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“…However, at that time the mechanisms by which cells recognize dsRNA and produce IFN remained elusive. Later, several studies suggested that human cells recognize particular spatial and steric organization of dsRNA via putative cell membrane receptors and produce type I IFN, IFN-α/β (6,10,15). Among synthetic dsRNA, polyriboinosinic: polyribocytidylic acid, poly(I:C), was found to be the most potent IFN inducer.…”

Section: Introductionmentioning

confidence: 99%

Toll‐Like Receptor 3: A Link between Toll‐Like Receptor, Interferon and Viruses

Matsumoto

Funami

Oshiumi

et al. 2004

Microbiology and Immunology

174

133

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Section: Introductionmentioning

confidence: 99%

Toll‐Like Receptor 3: A Link between Toll‐Like Receptor, Interferon and Viruses

Matsumoto

Funami

Oshiumi

et al. 2004

Microbiology and Immunology

174

133

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“…These findings tend to support the notions that, as an interferon inducer, (I), . (C), tolerates large reductions in size for (C),, but not for (I), [28,29], and that in the interferon-induction process of (I), . (C),, (I), plays a more decisive role than (C), [30].…”

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confidence: 99%

Degradation of Poly(inosinic acid) · poly(cytidylic acid) [(I)_n· (C_n)] by Human Plasma

Clercq

1979

European Journal of Biochemistry

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The double‐helical RNA interferon inducer, poly(inosinic acid) · poly(cytidylic acid) [(I)n· (C)n], is rapidly degraded by nucleases present in human plasma (serum). When incubated at 37°C with 50% human plasma, (I)n· (C)n (10 μg/ml) showed a half‐life of 6 min, [as assessed by residual acid insoluble radioactivity of an (I)n· (C)n preparation which was 3H‐labelled in the (C)n component]. Sucrose velocity analysis revealed that human plasma nucleases specifically hydrolyzed the (C)n strand of (I)n· (C)n, as assessed with (I)n· (C)n preparations that were 3H‐labelled in either (I)n or (C)n. The plasma nucleases that were responsible for the degradation of (I)n· (C)n resembled pancreatic ribonuclease A rather than T1 ribonuclease in substrate specificity. (I)n· (C)n became completely inactive as an inerferon inducer when it was incubated with 50% human plasma or serum. However, its interferon‐inducing capacity was fully restored if (C)n but not (I)n was added to the host cells, after these had been exposed to the inactivated (I)n· (C)n. That the inactivating effect of human plasma on the interferon‐inducing potency of (I)n· (C)n could solely be attributed to hydrolysis of the (C)n strand was further supported by the finding that two analogues of (I)n· (C)n, which had become more resistant to degradation by pancreatic ribonuclease by virtue of some substitutions in the (C)n strand, i.e. a bromine at C‐5, (I)n· (br5C)n, or a sulfur at C‐2, (I)n· (s2C)n, were not inactivated in the presence of 50% human plasma (or serum).

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“…(C), is more tolerant to substitutions at C-2' of the (I), strand than it is to similar modifications of the (C), strand. However other modifications, such as strand interruption by unpaired bases or bond breakage, are better tolerated by the (C), strand than by the (I),, strand [32].…”

Section: Discussionmentioning

confidence: 99%

Interferon Induction by a 2′‐Modified Double‐Helical RNA, Poly(2′‐azido‐2′‐deoxyinosinic acid) · polycytidylic acid

Clercq

Torrence

Stollar

et al. 1978

European Journal of Biochemistry

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Although the presence of free 2'-hydroxyl groups in both strands of a double-stranded RNA complex has been recognized as one of the major requisites for the interferon-inducing activity of double-stranded RNAs, we have found a particular analogue of (I), . (C), in which the 2'-hydroxyls of the purine nucleotide strand were replaced by azido groups, (dInj), . (C),, to be highly effective in inducing interferon. Various other 2'-azido analogues of (I), .

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Structural requirements of the rIn·rCn complex for Induction of human interferon

Cited by 129 publications

References 26 publications

Toll‐Like Receptor 3: A Link between Toll‐Like Receptor, Interferon and Viruses

Toll‐Like Receptor 3: A Link between Toll‐Like Receptor, Interferon and Viruses

Degradation of Poly(inosinic acid) · poly(cytidylic acid) [(I)_n· (C_n)] by Human Plasma

Interferon Induction by a 2′‐Modified Double‐Helical RNA, Poly(2′‐azido‐2′‐deoxyinosinic acid) · polycytidylic acid

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Structural requirements of the rIn·rCn complex for Induction of human interferon

Cited by 129 publications

References 26 publications

Toll‐Like Receptor 3: A Link between Toll‐Like Receptor, Interferon and Viruses

Toll‐Like Receptor 3: A Link between Toll‐Like Receptor, Interferon and Viruses

Degradation of Poly(inosinic acid) · poly(cytidylic acid) [(I)n· (Cn)] by Human Plasma

Interferon Induction by a 2′‐Modified Double‐Helical RNA, Poly(2′‐azido‐2′‐deoxyinosinic acid) · polycytidylic acid

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Degradation of Poly(inosinic acid) · poly(cytidylic acid) [(I)_n· (C_n)] by Human Plasma