scholarly journals Similarities in Seed and Aphid Transmission Among Soybean mosaic virus Isolates

Plant Disease ◽  
2007 ◽  
Vol 91 (5) ◽  
pp. 546-550 ◽  
Author(s):  
Leslie L. Domier ◽  
Todd A. Steinlage ◽  
Houston A. Hobbs ◽  
Yi Wang ◽  
Gabriel Herrera-Rodriguez ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Field Experiments ◽  
Soybean Mosaic Virus ◽  
Aphid Transmission ◽  
Amino Acid Sequences ◽  
Mechanical Transmission ◽  
Soybean Plant ◽  
Loss Of Function ◽  
Strain Specificity ◽  
Plant Introductions

Soybean mosaic virus (SMV) is an aphid- and seed-transmitted virus that infects soybean (Glycine max) plants and causes significant yield losses. Seed-borne infections are the primary sources of inoculum for SMV infections. The strain specificity of SMV transmission through seed and SMV-induced seed-coat mottling were investigated in field experiments. Six soybean plant introductions (PIs) were inoculated with eight SMV strains and isolates. Transmission of SMV through seed ranged from 0 to 43%, and isolate-by-soybean line interactions occurred in both transmission rates and percentages of mottled seeds. For example, SMV 746 was transmitted through 43% of seed in PI 229324, but was not transmitted through seed of PIs 68522, 68671, or 86449. In contrast, SMV 413 was transmitted through seed from all PIs. SMVs that were transmitted poorly by the Asian soybean aphid, Aphis glycines, also were transmitted poorly through seed. No predicted amino acid sequences within the helper-component protease or coat protein coding regions differentiated the two groups of SMV strains. The loss of aphid and seed transmissibility by repeated mechanical transmission suggests that constant selection pressure is needed to maintain the regions of the SMV genome controlling the two phenotypes from genetic drift and loss of function.

scholarly journals Role of Soybean mosaic virus–Encoded Proteins in Seed and Aphid Transmission in Soybean

2013 ◽  
Vol 103 (9) ◽  
pp. 941-948 ◽  
Author(s):  
Sushma Jossey ◽  
Houston A. Hobbs ◽  
Leslie L. Domier
Keyword(s):  
Mosaic Virus ◽  
Seed Quality ◽  
Soybean Mosaic Virus ◽  
Seed Transmission ◽  
Aphid Transmission ◽  
Plant Introduction ◽  
Sequence Motif ◽  
Coding Region ◽  
Encoded Proteins ◽  
Seed Transmissibility

Soybean mosaic virus (SMV) is seed and aphid transmitted and can cause significant reductions in yield and seed quality in soybean (Glycine max). The roles in seed and aphid transmission of selected SMV-encoded proteins were investigated by constructing mutants in and chimeric recombinants between SMV 413 (efficiently aphid and seed transmitted) and an isolate of SMV G2 (not aphid or seed transmitted). As previously reported, the DAG amino acid sequence motif near the amino terminus of the coat protein (CP) was the major determinant in differences in aphid transmissibility of the two SMV isolates, and helper component proteinase (HC-Pro) played a secondary role. Seed transmission of SMV was influenced by P1, HC-Pro, and CP. Replacement of the P1 coding region of SMV 413 with that of SMV G2 significantly enhanced seed transmissibility of SMV 413. Substitution in SMV 413 of the two amino acids that varied in the CPs of the two isolates with those from SMV G2, G to D in the DAG motif and Q to P near the carboxyl terminus, significantly reduced seed transmission. The Q-to-P substitution in SMV 413 also abolished virus-induced seed-coat mottling in plant introduction 68671. This is the first report associating P1, CP, and the DAG motif with seed transmission of a potyvirus and suggests that HC-Pro interactions with CP are important for multiple functions in the virus infection cycle.

scholarly journals Multiple Loci Condition Seed Transmission of Soybean mosaic virus (SMV) and SMV-Induced Seed Coat Mottling in Soybean

2011 ◽  
Vol 101 (6) ◽  
pp. 750-756 ◽  
Author(s):  
Leslie L. Domier ◽  
Houston A. Hobbs ◽  
Nancy K. McCoppin ◽  
Charles R. Bowen ◽  
Todd A. Steinlage ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Seed Coat ◽  
Soybean Mosaic Virus ◽  
Seed Transmission ◽  
Primary Sources ◽  
Posttranscriptional Gene Silencing ◽  
Plant Introductions ◽  
Multiple Loci ◽  
Soybean Plants ◽  
Simple Sequence

Infection of soybean plants with Soybean mosaic virus (SMV), which is transmitted by aphids and through seed, can cause significant reductions in seed production and quality. Because seedborne infections are the primary sources of inoculum for SMV infections in North America, host-plant resistance to seed transmission can limit the pool of plants that can serve as sources of inoculum. To examine the inheritance of SMV seed transmission in soybean, crosses were made between plant introductions (PIs) with high (PI88799), moderate (PI60279), and low (PI548391) rates of transmission of SMV through seed. In four F2 populations, SMV seed transmission segregated as if conditioned by two or more genes. Consequently, a recombinant inbred line population was derived from a cross between PIs 88799 and 548391 and evaluated for segregation of SMV seed transmission, seed coat mottling, and simple sequence repeat markers. Chromosomal regions on linkage groups C1 and C2 were significantly associated with both transmission of isolate SMV 413 through seed and SMV-induced seed coat mottling, and explained ≈42.8 and 46.4% of the variability in these two traits, respectively. Chromosomal regions associated with seed transmission and seed coat mottling contained homologues of Arabidopsis genes DCL3 and RDR6, which encode enzymes involved in RNA-mediated transcriptional and posttranscriptional gene silencing.

scholarly journals Importance of the C-terminal domain of soybean mosaic virus coat protein for subunit interactions

2006 ◽  
Vol 87 (1) ◽  
pp. 225-229 ◽  
Author(s):  
Sung-Hwan Kang ◽  
Won-Seok Lim ◽  
Sung-Hyun Hwang ◽  
Jin-Woo Park ◽  
Hong-Soo Choi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Mosaic Virus ◽  
Virus Assembly ◽  
Soybean Mosaic Virus ◽  
Cell Movement ◽  
Aphid Transmission ◽  
Terminal Region ◽  
Virus Coat ◽  
Two Hybrid

The potyvirus coat protein (CP) is involved in aphid transmission, cell-to-cell movement and virus assembly, not only by binding to viral RNA, but also by self-interaction or interactions with other factors. In this study, a number of CP mutants of Soybean mosaic virus (SMV) containing deletions and site-directed mutations were generated and cloned into yeast two-hybrid vectors. Interaction was confirmed by the expression of reporter genes, including HIS3, ADE2 and MEL1, in yeast strain AH109. Deletion of the C-terminal region of the CP caused loss of the CP–CP self-interaction ability detected in CP mutants with the C-terminal region. Alanine substitution at the amino acid positions R190, E191, E212, R245, H246 and R249 disrupted CP–CP interaction, whereas substitutions at the amino acid positions R188, D189, D198, K205, K218 and D250 did not. These results indicate that the C-terminal region of SMV CP may contain a domain(s) or amino acids required for CP–CP interaction and virus assembly.

scholarly journals Optimizing the PBS1 Decoy System to Confer Resistance to Potyvirus Infection in Arabidopsis and Soybean

2020 ◽  
Vol 33 (7) ◽  
pp. 932-944 ◽  
Author(s):  
Sarah E. Pottinger ◽  
Aurelie Bak ◽  
Alexandra Margets ◽  
Matthew Helm ◽  
Lucas Tang ◽  
...  
Keyword(s):  
Cell Death ◽  
Plasma Membrane ◽  
Mosaic Virus ◽  
Pseudomonas Syringae ◽  
Soybean Mosaic Virus ◽  
Aphid Transmission ◽  
Defense Responses ◽  
Cell Death Response ◽  
Dependent Cell ◽  
Nia Protease

The Arabidopsis resistance protein RPS5 is activated by proteolytic cleavage of the protein kinase PBS1 by the Pseudomonas syringae effector protease AvrPphB. We have previously shown that replacing seven amino acids at the cleavage site of PBS1 with a motif cleaved by the NIa protease of turnip mosaic virus (TuMV) enables RPS5 activation upon TuMV infection. However, this engineered resistance conferred a trailing necrosis phenotype indicative of a cell-death response too slow to contain the virus. We theorized this could result from a positional mismatch within the cell between PBS1TuMV, RPS5, and the NIa protease. To test this, we relocalized PBS1TuMV and RPS5 to cellular sites of NIa accumulation. These experiments revealed that relocation of RPS5 away from the plasma membrane compromised RPS5-dependent cell death in Nicotiana benthamiana, even though PBS1 was efficiently cleaved. As an alternative approach, we tested whether overexpression of plasma membrane–localized PBS1TuMV could enhance RPS5 activation by TuMV. Significantly, overexpressing the PBS1TuMV decoy protein conferred complete resistance to TuMV when delivered by either agrobacterium or by aphid transmission, showing that RPS5-mediated defense responses are effective against bacterial and viral pathogens. Lastly, we have now extended this PBS1 decoy approach to soybean by modifying a soybean PBS1 ortholog to be cleaved by the NIa protease of soybean mosaic virus (SMV). Transgenic overexpression of this soybean PBS1 decoy conferred immunity to SMV, demonstrating that we can use endogenous PBS1 proteins in crop plants to engineer economically relevant disease resistant traits.

scholarly journals The Relationship Between Aphis glycines and Soybean mosaic virus Incidence in Different Pest Management Systems

Plant Disease ◽  
2005 ◽  
Vol 89 (9) ◽  
pp. 926-934 ◽  
Author(s):  
M. E. Lee Burrows ◽  
C. M. Boerboom ◽  
J. M. Gaska ◽  
C. R. Grau
Keyword(s):  
Mosaic Virus ◽  
Field Experiments ◽  
Seed Quality ◽  
Soybean Mosaic Virus ◽  
Aphis Glycines ◽  
Management Systems ◽  
Insecticide Treatment ◽  
Virus Incidence ◽  
The Relationship ◽  
Herbicide Glyphosate

The soybean aphid, Aphis glycines, causes yield loss and transmits viruses such as Soybean mosaic virus (SMV) in soybean (Glycine max). Field experiments were designed to monitor the landing rate of A. glycines and transmission of SMV to soybean grown in six crop management environments. Management systems evaluated were the application of postemergence insecticide or no insecticide, and within each insecticide treatment no herbicide, glyphosate, or imazamox application. In 2001, early-season incidence of SMV was 2%, which increased to 80% within 18 days after the beginning of the A. glycines flight. In 2002, the incidence of SMV was 1% prior to the arrival of A. glycines, and increased to 44% within 21 days. The landing rate of A. glycines was fivefold higher in 2001 than in 2002. The incidence of SMV was lower in insecticide-treated plots in 2002, but no effect of insecticide was seen in 2001. Imazamox slowed the progression of SMV incidence, but the final incidence of SMV-infected plants was the same. Glyphosate had no consistent effect on SMV incidence. Yield was higher in the insecticide-treated plots in 2002, but not 2001. Insecticide and herbicide application had no substantial effects on seed quality.

scholarly journals Optimizing the PBS1 Decoy System to Confer Resistance to Potyvirus Infection in Arabidopsis and Soybean

2020 ◽  
Author(s):  
Sarah E. Pottinger ◽  
Aurelie Bak ◽  
Alexandra Margets ◽  
Matthew Helm ◽  
Lucas Tang ◽  
...  
Keyword(s):  
Cell Death ◽  
Plasma Membrane ◽  
Mosaic Virus ◽  
Pseudomonas Syringae ◽  
Soybean Mosaic Virus ◽  
Aphid Transmission ◽  
Defense Responses ◽  
Cell Death Response ◽  
Dependent Cell ◽  
Nia Protease

ABSTRACTThe Arabidopsis resistance protein RPS5 is activated by proteolytic cleavage of the protein kinase PBS1 by the Pseudomonas syringae effector protease AvrPphB. We have previously shown that replacing seven amino acids at the cleavage site of PBS1 with a motif cleaved by the NIa protease of turnip mosaic virus (TuMV) enables RPS5 activation upon TuMV infection. However, this engineered resistance conferred a trailing necrosis phenotype indicative of a cell death response too slow to contain the virus. We theorized this could result from a positional mismatch within the cell between PBS1TuMV, RPS5 and the NIa protease. To test this, we re-localized PBS1TuMV and RPS5 to cellular sites of NIa accumulation. These experiments revealed that relocation of RPS5 away from the plasma membrane compromised RPS5-dependent cell death in N. benthamiana, even though PBS1 was efficiently cleaved. As an alternative approach, we tested whether overexpression of plasma membrane-localized PBS1TuMV would enhance RPS5 activation by TuMV. Significantly, over-expressing the PBS1TuMV decoy protein conferred complete resistance to TuMV when delivered by either Agrobacterium or by aphid transmission, showing that RPS5-mediated defense responses are effective against bacterial and viral pathogens. Lastly, we have now extended this PBS1 decoy approach to soybean by modifying a soybean PBS1 ortholog to be cleaved by the NIa protease of soybean mosaic virus (SMV). Transgenic overexpression of this soybean PBS1 decoy conferred immunity to SMV, demonstrating that we can use endogenous PBS1 proteins in crop plants to engineer economically relevant disease resistant traits.

scholarly journals The HC-Pro and P3 Cistrons of an Avirulent Soybean mosaic virus Are Recognized by Different Resistance Genes at the Complex Rsv1 Locus

2013 ◽  
Vol 26 (2) ◽  
pp. 203-215 ◽  
Author(s):  
R.-H. Wen ◽  
B. Khatabi ◽  
T. Ashfield ◽  
M. A. Saghai Maroof ◽  
M. R. Hajimorad
Keyword(s):  
Mosaic Virus ◽  
Resistance Genes ◽  
Soybean Mosaic Virus ◽  
Plant Introduction ◽  
Soybean Plant ◽  
Leucine Rich Repeat ◽  
Extreme Resistance ◽  
Helper Component ◽  
Inoculation Site ◽  
Helper Component Proteinase

The complex Rsv1 locus in soybean plant introduction (PI) ‘PI96983’ confers extreme resistance (ER) against Soybean mosaic virus (SMV) strain N but not SMV-G7 and SMV-G7d. Both the SMV helper-component proteinase (HC-Pro) and P3 cistrons can serve as avirulence factors recognized by Rsv1. To understand the genetics underlying recognition of the two cistrons, we have utilized two soybean lines (L800 and L943) derived from crosses between PI96983 (Rsv1) and Lee68 (rsv1) with distinct recombination events within the Rsv1 locus. L800 contains a single PI96983-derived member (3gG2) of an Rsv1-associated subfamily of nucleotide-binding leucine-rich repeat (NB-LRR) genes. In contrast, although L943 lacks 3gG2, it contains a suite of five other NB-LRR genes belonging to the same family. L800 confers ER against SMV-N whereas L943 allows limited replication at the inoculation site. SMV-N-derived chimeras containing HC-Pro from SMV-G7 or SMV-G7d gained virulence on L943 but not on L800 whereas those with P3 replacement gained virulence on L800 but not on L943. In reciprocal experiments, SMV-G7- and SMV-G7d-derived chimeras with HC-Pro replacement from SMV-N lost virulence on L943 but retained virulence on L800 whereas those with P3 replacement lost virulence on L800 while remaining virulent on L943. These data demonstrate that distinct resistance genes at the Rsv1 locus, likely belonging to the NB-LRR class, mediate recognition of HC-Pro and P3.

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