Interaction between Movement Proteins of Hibiscus green spot virus

Atabekova, Anastasia K.; Lazareva, Ekaterina A.; Lezzhov, Alexander A.; Solovieva, Anna D.; Golyshev, Sergey A.; Skulachev, Boris I.; Solovyev, Ilya D.; Savitsky, Alexander P.; Heinlein, Manfred; Morozov, Sergey Y.; Solovyev, Andrey G.

doi:10.3390/v14122742

Cited by 3 publications

(6 citation statements)

References 38 publications

(70 reference statements)

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“…Samples collected at 3 dpi were subjected to immunogold labeling for BMB2 detection, with the exception of the use of GFP-specific antibodies. Similar to BMB2, GFP-BMB1-specific labeling was strongly associated with PAMBs and distributed throughout these structures ( Figure 6 A), consistent with the recently demonstrated interaction between BMB1 and BMB2 in PAMBs [ 39 ]. Analysis of cell wall regions adjacent to PAMBs revealed that immunogold labeling was typically not associated with the PD channels ( Figure 6 A) and was occasionally found at the PD entrance ( Figure 6 B).…”

Section: Resultssupporting

confidence: 88%

“…with BMB1 and directs BMB1 to PAMBs, the PD interior, and neighboring cells [23,39]. The function of BMB2 in virus cell-to-cell transport depends on its ability to increase the permeability of the PD channels [24].…”

Section: Visualization Of Pambs By Airyscan Confocal Microscopymentioning

confidence: 99%

“…As shown by inhibitory analyses, the mechanism of BMB2 intracellular transport to PAMBs is based on a lateral translocation in the plane of the ER membranes rather than on a secretory pathway [ 38 ]. In plant cells, BMB2 interacts with BMB1 and directs BMB1 to PAMBs, the PD interior, and neighboring cells [ 23 , 39 ]. The function of BMB2 in virus cell-to-cell transport depends on its ability to increase the permeability of the PD channels [ 24 ].…”

Section: Introductionmentioning

confidence: 99%

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Fine Structure of Plasmodesmata-Associated Membrane Bodies Formed by Viral Movement Protein

Atabekova,

Golyshev,

Lezzhov

et al. 2023

Plants

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Cell-to-cell transport of plant viruses through plasmodesmata (PD) requires viral movement proteins (MPs) often associated with cell membranes. The genome of the Hibiscus green spot virus encodes two MPs, BMB1 and BMB2, which enable virus cell-to-cell transport. BMB2 is known to localize to PD-associated membrane bodies (PAMBs), which are derived from the endoplasmic reticulum (ER) structures, and to direct BMB1 to PAMBs. This paper reports the fine structure of PAMBs. Immunogold labeling confirms the previously observed localization of BMB1 and BMB2 to PAMBs. EM tomography data show that the ER-derived structures in PAMBs are mostly cisterns interconnected by numerous intermembrane contacts that likely stabilize PAMBs. These contacts predominantly involve the rims of the cisterns rather than their flat surfaces. Using FRET-FLIM (Förster resonance energy transfer between fluorophores detected by fluorescence-lifetime imaging microscopy) and chemical cross-linking, BMB2 is shown to self-interact and form high-molecular-weight complexes. As BMB2 has been shown to have an affinity for highly curved membranes at cisternal rims, the interaction of BMB2 molecules located at rims of adjacent cisterns is suggested to be involved in the formation of intermembrane contacts in PAMBs.

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Section: Resultssupporting

confidence: 88%

Section: Visualization Of Pambs By Airyscan Confocal Microscopymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Fine Structure of Plasmodesmata-Associated Membrane Bodies Formed by Viral Movement Protein

Atabekova,

Golyshev,

Lezzhov

et al. 2023

Plants

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“…This protein promotes the generation of membrane bodies in the vicinity of PD, increasing its size-exclusion limit (59). BMB1 interacts in vitro and in vivo with BMB2, which is essential for BMB2-directed targeting of BMB1 to PD-associated membrane bodies and probably provides intra-and intercellular transports of vRNPs (8,59).…”

Section: Cell-to-cell Movement Of Kitavirusesmentioning

confidence: 99%

Kitaviruses: A Window to Atypical Plant Viruses Causing Nonsystemic Diseases

Ramos-González

Arena

Tassi

et al. 2023

Annu. Rev. Phytopathol.

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Kitaviridae is a family of plant-infecting viruses that have multiple positive-sense, single-stranded RNA genomic segments. Kitaviruses are assigned into the genera Cilevirus, Higrevirus, and Blunervirus, mainly on the basis of the diversity of their genomic organization. Cell-to-cell movement of most kitaviruses is provided by the 30K family of proteins or the binary movement block, considered an alternative movement module among plant viruses. Kitaviruses stand out for producing conspicuously unusual locally restricted infections and showing deficient or nonsystemic movement likely resulting from incompatible or suboptimal interactions with their hosts. Transmission of kitaviruses is mediated by mites of many species of the genus Brevipalpus and at least one species of eriophyids. Kitavirus genomes encode numerous orphan open reading frames but RNA-dependent RNA polymerase and the transmembrane helix-containing protein, generically called SP24, typify a close phylogenetic link with arthropod viruses. Kitaviruses infect a large range of host plants and cause diseases of economic concern in crops such as citrus, tomato, passion fruit, tea, and blueberry. Expected final online publication date for the Annual Review of Phytopathology, Volume 61 is September 2023. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.

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“…The latter branch contains exclusively monopartite viruses and, in particular, includes Goji berry chlorosis virus (GBCV), which encodes six polypeptides and has no close relatives with similar genome organization [8]. Four additional benyvirus-like members of this brunch are predicted to encode a binary movement block (BMB), which is also found in multipartite viruses of the family Kitaviridae [7,[9][10][11] (Figure 1). In the course of recent studies on the phylogeny of benyvirus-like RNA polymerases, we found that phylogenetically close monopartite viruses include a new, previously In the course of recent studies on the phylogeny of benyvirus-like RNA polymerases, we found that phylogenetically close monopartite viruses include a new, previously un-described group of viruses related to members of the family Benyviridae.…”

Section: Introductionmentioning

confidence: 99%

Predicted Membrane-Associated Domains in Proteins Encoded by Novel Monopartite Plant RNA Viruses Related to Members of the Family Benyviridae

Morozov,

Lezzhov,

Solovyev

2023

IJMS

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As a continuation of our previous work, in this paper, we examine in greater detail the genome organization and some protein properties of the members of a potential group named Reclovirids and belonging to Benyviridae-related viruses. It can be proposed that the single-component Reclovirid genomes encode previously undiscovered transport genes. Indeed, analysis of the coding potential of these novel viral genomes reveals one or more cistrons ranging in size from 40 to 80 to about 600 codons, located in the 3′-terminal region of the genomic RNA, encoding proteins with predicted hydrophobic segments that are structurally diverse among Reclovirids and have no analogues in other plant RNA viruses. Additionally, in many cases, the possible methyltransferase domain of Reclovirid replicases is preceded by membrane-embedded protein segments that are not present in annotated members of the Benyviridae family. These observations suggest a general association of most Reclovirid proteins with cell membranes.

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Interaction between Movement Proteins of Hibiscus green spot virus

Cited by 3 publications

References 38 publications

Fine Structure of Plasmodesmata-Associated Membrane Bodies Formed by Viral Movement Protein

Fine Structure of Plasmodesmata-Associated Membrane Bodies Formed by Viral Movement Protein

Kitaviruses: A Window to Atypical Plant Viruses Causing Nonsystemic Diseases

Predicted Membrane-Associated Domains in Proteins Encoded by Novel Monopartite Plant RNA Viruses Related to Members of the Family Benyviridae

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