The nine C-terminal residues of the grapevine fanleaf nepovirus movement protein are critical for systemic virus spread.

Belin, Christophe; Schmitt, Corinne; Gaire, Fabien; Walter, Bernard; Demangeat, Gérard; Pinck, L.

doi:10.1099/0022-1317-80-6-1347

Cited by 43 publications

(29 citation statements)

References 32 publications

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“…CP to encapsidate viral RNA was assessed under conditions that allows to distinguish RNase-protected, encapsidated viral RNA (P condition, PIPES buffer) from total, encapsidated, and nonencapsidated viral RNA (T condition, TLES buffer) as described previously (6). As expected, under T condition, progeny viral RNA was detected for all GFLV RNA1 and RNA2 combinations (Fig.…”

Section: Vol 84 2010 Coat Protein Determinants Of Gflv Transmissionmentioning

confidence: 94%

“…Plasmid pVec2ABC carrying a fulllength cDNA copy of GFLV-F13 RNA2 was used as a template to develop chimeric 2C CP genes (6). For cloning purposes, an Acc65I restriction site was introduced into pVec2ABC from positions 2678 to 2683 (nucleotide positions are given according to the GFLV-F13 RNA2 sequence, GenBank accession no.…”

Section: Methodsmentioning

confidence: 99%

“…CP is maintained for cell-to-cell movement (5,6). Mutations affecting regions R1 (nucleotides [nt] 2284 to 2302), R2 (nt 2609 to 2640), R4 (nt 2819 to 2842), and R5 (nt 2937 to 2965) of the GFLV 2C CP gene were produced by primer overlap extension mutagenesis (14), using the primers described in Table S1 in the supplemental material.…”

Section: Methodsmentioning

confidence: 99%

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A Stretch of 11 Amino Acids in the βB-βC Loop of the Coat Protein of Grapevine Fanleaf Virus Is Essential for Transmission by the Nematode Xiphinema index

Schellenberger

Andret-Link

Schmitt-Keichinger

et al. 2010

J Virol

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Grapevine fanleaf virus (GFLV) and Arabis mosaic virus (ArMV) from the genus Nepovirus, family Secoviridae, cause a severe degeneration of grapevines. GFLV and ArMV have a bipartite RNA genome and are transmitted specifically by the ectoparasitic nematodes Xiphinema index and Xiphinema diversicaudatum, respectively. The transmission specificity of both viruses maps to their respective RNA2-encoded coat protein (CP). To further delineate the GFLV CP determinants of transmission specificity, three-dimensional (3D) homology structure models of virions and CP subunits were constructed based on the crystal structure of Tobacco ringspot virus, the type member of the genus Nepovirus. The 3D models were examined to predict amino acids that are exposed at the external virion surface, highly conserved among GFLV isolates but divergent between GFLV and ArMV. Five short amino acid stretches that matched these topographical and sequence conservation criteria were selected and substituted in single and multiple combinations by their ArMV counterparts in a GFLV RNA2 cDNA clone. Among the 21 chimeric RNA2 molecules engineered, transcripts of only three of them induced systemic plant infection in the presence of GFLV RNA1. Nematode transmission assays of the three viable recombinant viruses showed that swapping a stretch of (i) 11 residues in the ␤B-␤C loop near the icosahedral 3-fold axis abolished transmission by X. index but was insufficient to restore transmission by X. diversicaudatum and (ii) 7 residues in the ␤E-␣B loop did not interfere with transmission by the two Xiphinema species. This study provides new insights into GFLV CP determinants of nematode transmission.

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Section: Vol 84 2010 Coat Protein Determinants Of Gflv Transmissionmentioning

confidence: 94%

Section: Methodsmentioning

confidence: 99%

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A Stretch of 11 Amino Acids in the βB-βC Loop of the Coat Protein of Grapevine Fanleaf Virus Is Essential for Transmission by the Nematode Xiphinema index

Schellenberger

Andret-Link

Schmitt-Keichinger

et al. 2010

J Virol

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“…These results suggest that in vivo only homologous virions can be moved from cell to cell by the viral transport tubule and that the MP is not able to assist the movement of virions even of related viruses. Little, but supportive, evidence is available for this hypothesis from a study performed by Belin et al (1999) on the nepovirus GFLV, showing that nine C-terminal residues of the 2B movement protein must be of the same virus origin as the 2C coat protein for successful systemic spread.…”

Section: Discussionmentioning

confidence: 99%

“…Indirect evidence for a specific interaction between the C terminus of the CPMV MP and virions was presented by Lekkerkerker et al (1996), who showed that a mutant virus encoding an MP lacking the C-terminal 18 amino acids (residues 313-331) was able to form tubules in protoplasts which did not contain virus particles, and the mutant was not able to spread systemically in plant tissue. Furthermore, for Grapevine fanleaf virus (GFLV), another member of the family Comoviridae, Belin et al (1999) found that the nine C-terminal amino acids of the MP must be of the same virus origin as the CP for successful systemic spread, and they also proposed a requirement for specific interactions between the movement protein (2B MP ) and the coat protein (2C CP ).…”

Section: Introductionmentioning

confidence: 99%

The C-terminal region of the movement protein of Cowpea mosaic virus is involved in binding to the large but not to the small coat protein

Carvalho

Wellink²,

Ribeiro

et al. 2003

Journal of General Virology

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Cowpea mosaic virus (CPMV) moves from cell to cell as virus particles which are translocated through a plasmodesmata-penetrating transport tubule made up of viral movement protein (MP) copies. To gain further insight into the roles of the viral MP and capsid proteins (CP) in virus movement, full-length and truncated forms of the MP were expressed in insect cells using the baculovirus expression system. Using ELISA and blot overlay assays, affinity purified MP was shown to bind specifically to intact CPMV virions and to the large CP, but not to the small CP. This binding was not observed with a C-terminal deletion mutant of the MP, although this mutant retained the capacity to bind to other MP molecules and to form tubules. These results suggest that the C-terminal 48 amino acids constitute the virion-binding domain of the MP.

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Involvement of RNA2-Encoded Proteins in the Specific Transmission of Grapevine Fanleaf Virus by Its Nematode Vector Xiphinema index

Belin¹,

Schmitt²,

Demangeat³

et al. 2001

Virology

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The nepovirus Grapevine fanleaf virus (GFLV) is specifically transmitted by the nematode Xiphinema index. To identify the RNA2-encoded proteins involved in X. index-mediated spread of GFLV, chimeric RNA2 constructs were engineered by replacing the 2A, 2B(MP), and/or 2C(CP) sequences of GFLV with their counterparts in Arabis mosaic virus (ArMV), a closely related nepovirus which is transmitted by Xiphinema diversicaudatum but not by X. index. Among the recombinant viruses obtained from transcripts of GFLV RNA1 and chimeric RNA2, only those which contained the 2C(CP) gene (504 aa) and 2B(MP) contiguous 9 C-terminal residues of GFLV were transmitted by X. index as efficiently as natural and synthetic wild-type GFLV, regardless of the origin of the 2A and 2B(MP) genes. As expected, ArMV was not transmitted probably because it is not retained by X. index. These results indicate that the determinants responsible for the specific spread of GFLV by X. index are located within the 513 C-terminal residues of the polyprotein encoded by RNA2.

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The nine C-terminal residues of the grapevine fanleaf nepovirus movement protein are critical for systemic virus spread.

Abstract: The grapevine fanleaf virus (GFLV)RNA2

Cited by 43 publications

References 32 publications

A Stretch of 11 Amino Acids in the βB-βC Loop of the Coat Protein of Grapevine Fanleaf Virus Is Essential for Transmission by the Nematode Xiphinema index

A Stretch of 11 Amino Acids in the βB-βC Loop of the Coat Protein of Grapevine Fanleaf Virus Is Essential for Transmission by the Nematode Xiphinema index

The C-terminal region of the movement protein of Cowpea mosaic virus is involved in binding to the large but not to the small coat protein

Involvement of RNA2-Encoded Proteins in the Specific Transmission of Grapevine Fanleaf Virus by Its Nematode Vector Xiphinema index

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