The endopeptidase of the maize-affecting Marafivirus type member maize rayado fino virus doubles as a deubiquitinase

Patel, Ankoor; McBride, Jessica A.M.; Mark, Brian L.

doi:10.1016/j.jbc.2021.100957

Cited by 6 publications

(10 citation statements)

References 73 publications

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“…Comparison of the MRFV PRO 3D structure with known PRO 3D structures revealed turnip yellow mosaic virus (TYMV, family Tymovirus ) PRO as the closest structural homolog, followed by ovarian-tumor-domain-containing protein 3 (OTUD3) from Homo sapiens and OTUD1 from Saccharomyces cerevisiae . Additionally, deubiquitinating activity has been shown for BlVS, CSDaV, GsyV1, MRFV, OBDV, and OLV3 [ 106 ]. On the basis of their overall core fold, MRFV PRO and TYMV PRO seem to be more related to a viral out-specific ubiquitin hydrolase (DUB) than to papain-like proteases [ 107 , 108 ].…”

Section: Discussionmentioning

confidence: 99%

“…The tymovirus and marafivirus PRO can be classified as OTU-like cysteine proteases [ 109 , 110 ]. The MRFV cleavage site LVGA between PRO and HEL domains has been verified in the past, suggesting that this particular site in this location is highly likely to be active for other marafiviruses as well ( File S1 ) [ 106 ]. PRO cleavage sites for several marafiviruses, such as PGMV (INGG), SbMV (VNGG), DiMV2 (LTGS), and DiMV1 (LNGS), differ in either the first or last position ( File S1 ).…”

Section: Discussionmentioning

confidence: 99%

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Identification and Full Genome Analysis of the First Putative Virus of Sea Buckthorn (Hippophae rhamnoides L.)

et al. 2022

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The agricultural importance of sea buckthorn (SBT; Hippophae rhamnoides L.) is rapidly increasing. Several bacterial and fungal pathogens infecting SBT have been identified and characterized; however, the viral pathogens are not yet known. In this study, we identified, isolated, and sequenced a virus from a wild plantation of SBT for the first time. Sequence analysis of the obtained viral genome revealed high similarity with several viruses belonging to the genus Marafivirus. The genome of the new virus is 6989 nucleotides (nt) in length according to 5′, 3′ RACE (without polyA-tail), with 5′ and 3′ 133 and 109 nt long untranslated regions, respectively. The viral genome encoded two open reading frames (ORFs). ORF1 encoded a polyprotein of 1954 amino acids with the characteristic marafivirus non-structural protein domains—methyltransferase, Salyut domain, papain-like cysteine protease, helicase, and RNA-dependent RNA polymerase. ORF1 was separated from ORF2 by 6 nt, encoding the coat protein (CP) with typical signatures of minor and major forms. Both CP forms were cloned and expressed in a bacterial expression system. Only the major CP was able to self-assemble into 30 nm virus-like particles that resembled the native virus, thus demonstrating that minor CP is not essential for virion assembly.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification and Full Genome Analysis of the First Putative Virus of Sea Buckthorn (Hippophae rhamnoides L.)

et al. 2022

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“…Comparison of the MRFV PRO 3D structure with known PRO 3D structures revealed turnip yellow mosaic virus (TYMV, family Tymovirus ) PRO as the closest structural homolog, followed by ovarian tumor domain–containing protein 3 (OTUD3) from Homo sapiens and OTUD1 from Saccharomyces cerevisiae . Additionally, deubiquitinating activity has been shown for BLVS, CSDaV, GsyV1, MRFV, OBDV, and OLV3 [106]. Based on their overall core fold, MRFV PRO and TYMV PRO seem to be more related to a viral OTU specific ubiquitin hydrolase (DUB) than to papain-like proteases [107, 108].…”

Section: Discussionmentioning

confidence: 99%

“…The tymovirus and marafivirus PRO can be classified as OTU-like cysteine proteases [110]. The MRFV cleavage site LVGA between PRO and HEL domains has been verified in the past, suggesting that this particular site in this location is highly likely to be active for other marafiviruses as well (S1 File) [106]. PRO cleavage sites for several marafiviruses, such as PGMV (INGG), SbMV (VNGG), DiMV2 (LTGS), and DiMV1 (LNGS), differ in either the first or last position (S1 File).…”

Section: Discussionmentioning

confidence: 99%

Identification and full genome analysis of the first putative virus of sea buckthorn (Hippophae rhamnoidesL.)

Baļķe

Zeltina

Zrelovs

et al. 2022

Preprint

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The agricultural importance of sea buckthorn (Hippophae rhamnoides L.) is rapidly increasing. Several bacterial and fungal pathogens infecting sea buckthorn have been identified and characterized; however, the viral pathogens are not yet known. In this study, we identified, isolated, and sequenced a virus from a wild plantation of sea buckthorn for the first time. Sequence analysis of the obtained viral genome revealed high similarity with sequences of several viruses belonging to the genus Marafivirus, especially olive latent virus 3 (OLV-3). The genome of the new virus is 6,989 nucleotides (nt) in length according to 5′ and 3′ rapid amplification of cDNA ends (RACE) (without polyA-tail), with 5′ and 3′ untranslated regions being 133 and 109 nt long, respectively. The viral genome encoded two open reading frames (ORFs). ORF1 encoded a polyprotein of 1,954 amino acids (aa) with the characteristic marafivirus non-structural protein domains—methyltransferase, Salyut domain, papain-like cysteine protease, helicase, and RNA-dependent RNA polymerase. ORF1 was separated from ORF2 by a six nt and encoded the coat protein (CP). CP had typical signatures of minor (30.96 kDa) and major (21.18 kDa) forms. Both CP forms were cloned and expressed in a bacterial expression system, and only the major CP was able to self-assemble into 30 nm virus-like particles that resembled the native virus, thus demonstrating that minor CP is not essential for virion assembly. We suggest the newly discovered virus to be named as "Sea buckthorn marafivirus", abbreviated as "SBuMV".

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“…The various means range from inducing, inhibiting, or modifying the enzymes involved in the process, especially the E3 ligases. Some viruses such as turnip yellow mosaic virus (TYMV) and maize rayado fino virus (MRFV) can encode deubiquitinase enzymes (DUBs) to achieve a favorable environment for viral infection by inhibiting host defense mechanisms [ 45 , 46 ].…”

Section: Ubiquitin-proteasome System (Ups) Role Under Viral Infectionmentioning

confidence: 99%

The Ubiquitin–Proteasome System (UPS) and Viral Infection in Plants

Lobaina

Tarazi

Castorino

et al. 2022

Plants

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The ubiquitin–proteasome system (UPS) is crucial in maintaining cellular physiological balance. The UPS performs quality control and degrades proteins that have already fulfilled their regulatory purpose. The UPS is essential for cellular and organic homeostasis, and its functions regulate DNA repair, gene transcription, protein activation, and receptor trafficking. Besides that, the UPS protects cellular immunity and acts on the host’s defense system. In order to produce successful infections, viruses frequently need to manipulate the UPS to maintain the proper level of viral proteins and hijack defense mechanisms. This review highlights and updates the mechanisms and strategies used by plant viruses to subvert the defenses of their hosts. Proteins involved in these mechanisms are important clues for biotechnological approaches in viral resistance.

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The endopeptidase of the maize-affecting Marafivirus type member maize rayado fino virus doubles as a deubiquitinase

Cited by 6 publications

References 73 publications

Identification and Full Genome Analysis of the First Putative Virus of Sea Buckthorn (Hippophae rhamnoides L.)

Identification and Full Genome Analysis of the First Putative Virus of Sea Buckthorn (Hippophae rhamnoides L.)

Identification and full genome analysis of the first putative virus of sea buckthorn (Hippophae rhamnoidesL.)

The Ubiquitin–Proteasome System (UPS) and Viral Infection in Plants

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