Mode of antiviral activity of water soluble components isolated fromElfvingia applanata on vesicular stomatitis virus

2001 ◽  
Vol 24 (1) ◽  
pp. 74-78 ◽  
Author(s):  
Seong Kug Eo ◽  
Young So Kim ◽  
Ki Wan Oh ◽  
Chong Kil Lee ◽  
Young Nam Lee ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Vesicular Stomatitis Virus ◽  
Water Soluble ◽  
Vesicular Stomatitis ◽  
Soluble Components

scholarly journals Vesicular Stomatitis Virus Transcription Is Inhibited by TRIM69 in the Interferon-Induced Antiviral State

2019 ◽  
Vol 93 (24) ◽  
Author(s):  
Tonya Kueck ◽  
Louis-Marie Bloyet ◽  
Elena Cassella ◽  
Trinity Zang ◽  
Fabian Schmidt ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Vesicular Stomatitis Virus ◽  
Rna Synthesis ◽  
Inhibition Mechanism ◽  
Target Sequence ◽  
Messenger Rnas ◽  
Antiviral Protein ◽  
Viral Mrnas ◽  
Antiviral State ◽  
Vesicular Stomatitis

ABSTRACT Interferons (IFNs) induce the expression of interferon-stimulated genes (ISGs), many of which are responsible for the cellular antiviral state in which the replication of numerous viruses is blocked. How the majority of individual ISGs inhibit the replication of particular viruses is unknown. We conducted a loss-of-function screen to identify genes required for the activity of alpha interferon (IFN-α) against vesicular stomatitis virus, Indiana serotype (VSVIND), a prototype negative-strand RNA virus. Our screen revealed that TRIM69, a member of the tripartite motif (TRIM) family of proteins, is a VSVIND inhibitor. TRIM69 potently inhibited VSVIND replication through a previously undescribed transcriptional inhibition mechanism. Specifically, TRIM69 physically associates with the VSVIND phosphoprotein (P), requiring a specific peptide target sequence encoded therein. P is a cofactor for the viral polymerase and is required for viral RNA synthesis, as well as the assembly of replication compartments. By targeting P, TRIM69 inhibits pioneer transcription of the incoming virion-associated minus-strand RNA, thereby preventing the synthesis of viral mRNAs, and consequently impedes all downstream events in the VSVIND replication cycle. Unlike some TRIM proteins, TRIM69 does not inhibit viral replication by inducing degradation of target viral proteins. Rather, higher-order TRIM69 multimerization is required for its antiviral activity, suggesting that TRIM69 functions by sequestration or anatomical disruption of the viral machinery required for VSVIND RNA synthesis. IMPORTANCE Interferons are important antiviral cytokines that work by inducing hundreds of host genes whose products inhibit the replication of many viruses. While the antiviral activity of interferon has long been known, the identities and mechanisms of action of most interferon-induced antiviral proteins remain to be discovered. We identified gene products that are important for the antiviral activity of interferon against vesicular stomatitis virus (VSV), a model virus that whose genome consists of a single RNA molecule with negative-sense polarity. We found that a particular antiviral protein, TRIM69, functions by a previously undescribed molecular mechanism. Specifically, TRIM69 interacts with and inhibits the function of a particular phosphoprotein (P) component of the viral transcription machinery, preventing the synthesis of viral messenger RNAs.

scholarly journals A Monomeric GTPase-Negative MxA Mutant with Antiviral Activity

2000 ◽  
Vol 74 (17) ◽  
pp. 8202-8206 ◽  
Author(s):  
Christian Janzen ◽  
Georg Kochs ◽  
Otto Haller
Keyword(s):  
Antiviral Activity ◽  
Vesicular Stomatitis Virus ◽  
Vero Cells ◽  
Virus Multiplication ◽  
Gtpase Activity ◽  
Wild Type ◽  
Gtp Hydrolysis ◽  
Intracellular Pool ◽  
Antiviral Function ◽  
Vesicular Stomatitis

ABSTRACT MxA is a large, interferon-induced GTPase with antiviral activity against RNA viruses. It forms large oligomers, but whether oligomerization and GTPase activity are important for antiviral function is not known. The mutant protein MxA(L612K) carries a lysine-for-leucine substitution at position 612 and fails to form oligomers. Here we show that monomeric MxA(L612K) lacks detectable GTPase activity but is capable of inhibiting Thogoto virus in transiently transfected Vero cells or in a Thogoto virus minireplicon system. Likewise, MxA(L612K) inhibited vesicular stomatitis virus multiplication. These findings indicate that MxA monomers are antivirally active and suggest that GTP hydrolysis may not be required for antiviral activity. MxA(L612K) is rapidly degraded in cells, whereas wild-type MxA is stable. We propose that high-molecular-weight MxA oligomers represent a stable intracellular pool from which active MxA monomers are recruited.

In vitro antiviral activity of dehydroepiandrosterone and its synthetic derivatives against vesicular stomatitis virus

2009 ◽  
Vol 182 (2) ◽  
pp. 327-335 ◽  
Author(s):  
Carina Romanutti ◽  
Andrea C. Bruttomesso ◽  
Viviana Castilla ◽  
Juan A. Bisceglia ◽  
Lydia R. Galagovsky ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Vesicular Stomatitis Virus ◽  
Vesicular Stomatitis ◽  
Synthetic Derivatives

scholarly journals Vesicular stomatitis virus transcription is inhibited by TRIM69 in the interferon-induced antiviral state

2019 ◽  
Author(s):  
Tonya Kueck ◽  
Louis-Marie Bloyet ◽  
Elena Cassella ◽  
Trinity Zang ◽  
Fabian Schmidt ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Vesicular Stomatitis Virus ◽  
Rna Synthesis ◽  
Inhibition Mechanism ◽  
Target Sequence ◽  
Messenger Rnas ◽  
Antiviral Protein ◽  
Viral Mrnas ◽  
Antiviral State ◽  
Vesicular Stomatitis

ABSTRACTInterferons (IFNs) induce the expression of many interferon stimulated genes (ISGs), many of which are responsible for the cellular ‘antiviral state’ in which the replication of numerous viruses is blocked. How the majority of individual ISGs inhibit the replication of particular viruses is unknown. We conducted a loss-of-function screen to identify genes required for the activity of IFNαagainst vesicular stomatitis virus, Indiana serotype (VSVIND), a prototype negative strand RNA virus. Our screen revealed that TRIM69, a member of tripartite motif family of proteins, is a VSVINDinhibitor. TRIM69 potently inhibited VSVINDreplication through a previously undescribed transcriptional inhibition mechanism. Specifically, TRIM69 physically associates with the VSVINDphosphoprotein (P), requiring a specific peptide target sequence encoded therein. P is a cofactor for the viral polymerase, and is required for viral RNA synthesis as well as the assembly of replication compartments. By targeting P, TRIM69 inhibits pioneer transcription of the incoming virion-associated minus strand RNA, thereby preventing the synthesis of viral mRNAs, and consequently impedes all downstream events in the VSVINDreplication cycle. Unlike some TRIM proteins, TRIM69 does not inhibit viral replication by inducing degradation of target viral proteins. Rather, higher-order TRIM69 multimerization is required for its antiviral activity, suggesting that TRIM69 functions by sequestration or anatomical disruption of the viral machinery required for VSVINDRNA synthesis.SIGNIFICANCE STATEMENTInterferons are important antiviral cytokines that work by inducing hundreds of host genes whose products inhibit replication of many viruses. While the antiviral activity of interferon has long been known, the identities and mechanisms of action of most interferon-induced antiviral proteins remain to be discovered. We identified gene products that are important for the antiviral activity of interferon against vesicular stomatitis virus (VSV) a model virus that whose genome consists a single RNA molecule with negative sense polarity. We found that a particular antiviral protein, TRIM69, functions by a previously undescribed molecular mechanism. Specifically, TRIM69 interacts with, and inhibits the function, of a particular phosphoprotein (P) component the viral transcription machinery, preventing the synthesis of viral messenger RNAs.

Antiviral activity of antisense oligonucleotides linked to poly(L-lysine):targets on genomic RNA and/or mRNA of Vesicular Stomatitis Virus

1989 ◽  
Vol 8 (5) ◽  
pp. 825-828 ◽  
Author(s):  
Jean-Paul Leonetti ◽  
Genevieve Degols ◽  
Pierre Milhaud ◽  
Corinne Gagnor ◽  
Marc Lemaitre ◽  
...  
Keyword(s):  
Antiviral Activity ◽  
Vesicular Stomatitis Virus ◽  
Antisense Oligonucleotides ◽  
Genomic Rna ◽  
Vesicular Stomatitis

Synthesis and antiviral activity of stereoisomeric eritadenines

1982 ◽  
Vol 47 (5) ◽  
pp. 1392-1407 ◽  
Author(s):  
Antonín Holý ◽  
Ivan Votruba ◽  
Erik De Clercq
Keyword(s):  
Antiviral Activity ◽  
Acid Hydrolysis ◽  
Vesicular Stomatitis Virus ◽  
Sodium Borohydride ◽  
Osmium Tetroxide ◽  
Sodium Periodate ◽  
Parainfluenza Virus ◽  
Racemic Mixture ◽  
Isopropylidene Derivative ◽  
Vesicular Stomatitis

D-Eritadenine (Ia) and L-eritadenine (IIa) were prepared from 5-(adenin-9-yl)-5-deoxyaldofuranoses or enantiomeric 2,3-disubstituted erythronolactones (VIIIb, c, XIV). Oxidation of methyl 2,3-O-isopropylidene-D-ribofuranoside (IX) with periodate in the presence of ruthenium, followed by acid hydrolysis and reduction with sodium borohydride, afforded L-ribonolactone (XI). Its 2,3-O-isopropylidene derivative was subjected to alkaline hydrolysis, followed by oxidation with periodate, reduction with sodium borohydride and reaction with cyclohexanone to give 2,3-O-cyclohexylidene-L-erythronolactone (XIV). Condensation of [U-14C]-adenine with VIIIb, followed by acid hydrolysis, afforded [U-14C-adenine]-D-eritadenine. The threo-eritadenines III and IV were prepared by oxidation of 1-(adenin-9-yl)-1-deoxy-2,3-O-isopropylidenethreitols XVI and XVII with sodium periodate in the presence of ruthenium, followed by acid hydrolysis. Reaction of 9-(2,2-diethoxyethyl)adenine (XIX) with malonic acid gave 4-(adenin-9-yl)-3-butenoic acid (XXI); its methyl ester XXII, prepared by treatment with methanol, was isomerized with triethylamine to give methyl 4-(adenin-9-yl)-2-butenoate (XXIII). Hydroxylation of XXIII with osmium tetroxide afforded the racemic mixture of D- and L-threo-eritadenine (III+ IV). Eritadenines Ia and IIa were active against vaccinia, measles and vesicular stomatitis virus. Eritadenine Ia was also effective against reo- and parainfluenza virus. In general, the antiviral activity of the eritadenines decreased in the order D-erythro (Ia) > L-erythro (IIa) > D- and L-threo (III, IV).

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