Erratum: ICTV Virus Taxonomy Profile: Potyviridae

Wylie, Stephen J.; Adams, Mike; Chalam, Celia; Kreuze, Jan; López‐Moya, Juan José; Ohshima, Kazusato; Praveen, Shelly; Rabenstein, Frank; Stenger, Drake C.; Wang, Aiming; Zerbini, F. Murilo

doi:10.1099/jgv.0.000960

Cited by 29 publications

(9 citation statements)

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“…The high identity obtained in BlastN identification of CABMV (88 to 98%) and BCMV-BlCM (97 to 98%) is in agreement with the ICTV Potyvirus species demarcation (<76% nucleotide identity in the coat protein) (Wylie et al, 2017).…”

Section: Discussionsupporting

confidence: 54%

Molecular characterization of virus isolates from genus Potyvirus infecting Vigna subterranea in Burkina Faso

Konaté¹,

Ouédraogo²,

Néya³

et al. 2017

Afr. J. Biotechnol.

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Bambara groundnut (Vigna subterranea) is an African legume with a great nutritional, economic and social potential. However, one of the main constraints to this crop is viral diseases which reduced yields. Indeed, approximately 12 viruses have been reported to infect bambara groundnut. Among these, only four were reported from Burkina Faso, namely, cowpea aphid-borne mosaic virus (CABMV), bean common mosaic virus strain-blackeye cowpea mosaic (BCMV-BlCM), peanut mottle virus (PeMoV), and cowpea mottle virus (CPMoV). This study was carried out in order to identify and characterize the main viruses occurring in bambara groundnut from Burkina Faso using serological and molecular tests. 140 plants were sampled in the three agro-climatic zones of Burkina Faso. Both Potyvirus CABMV and BCMV-BlCM were identified in 8.57% of the samples when double antibody sandwich enzyme-linked immunosorbent assay (DAS-ELISA) test was used and 14.29% of the samples when reverse transcription-polymerase chain reaction (RT-PCR) test was used. Phylogenetic tree based on 476 nt in coat protein showed that all Burkina Faso CABMV isolates clustered together with Uganda isolate (KT726938). However, two groups were distinguished within these isolates. Burkina Faso BCMVBlCM isolates are strengthly clustered with BCMV and BlCMV group. This study reports the first molecular characterization of CABMV and BCMV-BlCM infecting Bambara groundnut in Burkina Faso.

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Section: Discussionsupporting

confidence: 54%

Molecular characterization of virus isolates from genus Potyvirus infecting Vigna subterranea in Burkina Faso

Konaté¹,

Ouédraogo²,

Néya³

et al. 2017

Afr. J. Biotechnol.

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“…These chymotrypsin-like proteases are encoded by viruses of the “picorna-like supergroup”, which, although infecting a variety of eukaryotic hosts, are grouped together based on the common origin of their RdRps [1,4,36]. Notable chymotrypsin-like viral proteases include the archetype 3C cysteine proteases (3C-Pro) of animal and human viruses in the family Picornaviridae [36,37] and the related 3C-like proteases (3CL-Pros) of plant viruses in the families Secoviridae [38] and Potyviridae [39] (Figure 1A). Serine proteases of plant viruses in the family Solemoviridae, and in the genera Polerovirus and Enamovirus also adopt a chymotrypsin-like fold.…”

Section: Chymotrypsin-like Serine and Cysteine Proteasesmentioning

confidence: 99%

“…The family Potyviridae is the largest and most economically important family of plant (+)-strand RNA viruses [39]. Although often referred to as “picorna-like” viruses because of the signature RdRps and 3CL-Pros that they encode, viruses in the family Potyviridae (potyvirids) differ from members of the order Picornavirales by their capsid structure and by the nature of the helicase and VPg [22,39] (Figure 1A). The 3CL-Pro of potyvirids is referred to as the NIa protease, an abbreviation for nuclear inclusion protein a.…”

Section: Chymotrypsin-like Serine and Cysteine Proteasesmentioning

confidence: 99%

“…The 3CL-Pro of potyvirids is referred to as the NIa protease, an abbreviation for nuclear inclusion protein a. Although potyvirids encode other proteases (Figure 1A), the NIa protease is responsible for most of the viral polyprotein cleavage events and it can act in cis or in trans , depending on the cleavage site [39,51]. The NIa protease of tobacco etch virus (TEV, genus Potyvirus ) is well characterized.…”

Section: Chymotrypsin-like Serine and Cysteine Proteasesmentioning

confidence: 99%

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Expanding Repertoire of Plant Positive-Strand RNA Virus Proteases

Mann

Sanfaçon

2019

Viruses

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Many plant viruses express their proteins through a polyprotein strategy, requiring the acquisition of protease domains to regulate the release of functional mature proteins and/or intermediate polyproteins. Positive-strand RNA viruses constitute the vast majority of plant viruses and they are diverse in their genomic organization and protein expression strategies. Until recently, proteases encoded by positive-strand RNA viruses were described as belonging to two categories: (1) chymotrypsin-like cysteine and serine proteases and (2) papain-like cysteine protease. However, the functional characterization of plant virus cysteine and serine proteases has highlighted their diversity in terms of biological activities, cleavage site specificities, regulatory mechanisms, and three-dimensional structures. The recent discovery of a plant picorna-like virus glutamic protease with possible structural similarities with fungal and bacterial glutamic proteases also revealed new unexpected sources of protease domains. We discuss the variety of plant positive-strand RNA virus protease domains. We also highlight possible evolution scenarios of these viral proteases, including evidence for the exchange of protease domains amongst unrelated viruses.

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“…Potyviruses account for ∼30% of the currently known plant viruses and include many agriculturally and economically important viruses, such as Turnip mosaic virus (TuMV), Soybean mosaic virus (SMV), Plum pox virus (PPV), and Potato virus Y (PVY) ( 17 , 18 , 20 ). Potyviruses have a positive-strand, ∼10-kb RNA genome that encodes a large polyprotein precursor and a small open reading frame (ORF) resulting from RNA polymerase slippage in the P3 coding sequence ( 17 ).…”

Section: Introductionmentioning

confidence: 99%

Dynamin-Like Proteins of Endocytosis in Plants Are Coopted by Potyviruses To Enhance Virus Infection

Cui

Chen

et al. 2018

J Virol

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It is well known that animal viruses enter host cells via endocytosis, whereas plant viruses require physical assistance, such as human and insect activities, to penetrate the host cell to establish their infection. In this study, we report that the endocytosis pathway is also involved in virus infection in plants. We show that plant potyviruses recruit endocytosis dynamin-like proteins to support their infection. Depletion of them by knockout of the corresponding genes suppresses virus replication, whereas overexpression of them enhances virus replication and intercellular movement. We also demonstrate that the dynamin-like proteins interact with several viral proteins that are essential for virus replication and cell-to-cell movement. We further show that treatment of a dynamin-specific inhibitor disrupts endocytosis and inhibits virus replication and intercellular movement. Therefore, the dynamin-like proteins are novel host factors of potyviruses. The corresponding genes may be manipulated using advanced biotechnology to control potyviral diseases.

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Erratum: ICTV Virus Taxonomy Profile: Potyviridae

Cited by 29 publications

References 0 publications

Molecular characterization of virus isolates from genus Potyvirus infecting Vigna subterranea in Burkina Faso

Molecular characterization of virus isolates from genus Potyvirus infecting Vigna subterranea in Burkina Faso

Expanding Repertoire of Plant Positive-Strand RNA Virus Proteases

Dynamin-Like Proteins of Endocytosis in Plants Are Coopted by Potyviruses To Enhance Virus Infection

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