Potato virus M
| Potato virus M | |
|---|---|
| Virus classification | |
| (unranked): | Virus |
| Realm: | Riboviria |
| Kingdom: | Orthornavirae |
| Phylum: | Kitrinoviricota |
| Class: | Alsuviricetes |
| Order: | Tymovirales |
| Family: | Betaflexiviridae |
| Genus: | Carlavirus |
| Species: | Carlavirus misolani
|
| Synonyms | |
| |
Potato virus M (PVM) is a plant pathogenic virus in the family Betaflexiviridae.[1] PVM can infect plants in the family Solanaceae, and it's an economically important pathogen of potato and pepino worldwide.[1][2]
Hosts and symptoms
PVM was first isolated from potatoes in 1923, in the United States. It was also identified from other New World plants, such as pepino, tomato and tobacco.[3]
PVM is naturally transmitted by aphids in a non-persistent manner, however poor cultural practices can cause up to 50% crop loss by mechanical means and infected seed tubers.[1][2]
PVM is detected in mixed infections of potatoes along with other viruses, but it can also cause damage in single infections.[2] In single infections of potato, PVM causes mild leaf symptoms, such as mottling, mosaic, crinkling and rolling of leaves, and necrosis, shoot and plant stunting.[1][2] In comparison to healthy tubers, PVM lowers the yield of starch by 0.96%, affects the size of starch granules, and increases amylose, ash and phosphate content in the affected tuber. [4]
PVM is less damaging in other hosts. In the common bean it causes necrotic spots and lesions. In tomato plants, it can cause the leaves to turn yellow. In the amaranth its symptoms are chlorotic rings and necrotic spots. In quinoa it can cause chlorotic lesions.[1]
Properties
PVM capsid is a rod-shaped or slightly curved filament with dimensions of 650 x 12 nm.[5]
PVM posesses a +ssRNA genome that is 8.5 kb in length. The RNA strand has a 5' cap and a 3' poly-A tail in order to resemble mature eukaryotic RNA.[1][6]
The RNA genome encodes six open reading frames (ORFs) that produce several viral proteins. ORF 1 encodes a replicase that has three domains: methyltransferase, helicase and RNA-dependent RNA polymerase. ORF 2, 3 and 4 overlap one another and are collectively referred to as the triple gene block. These proteins are involved in membrane binding, cell-to-cell movement of virions and RNA silencing. ORF 5 encodes the coat protein, and ORF 6 encodes a protein capable of binding with RNA and DNA and suppress RNA silencing.[1]
References
- ^ a b c d e f g Kumar, A; et al. (2023). "Genetic diversity of Potato virus M (PVM) in the major potato growing region in the Indo-Gangetic plain and characterization of a distinct strain of PVM occurring in India". Frontiers in Microbiology. 14 1265653. doi:10.3389/fmicb.2023.1265653. PMC 10701592. PMID 38075880.
- ^ a b c d Alexandrova, A; et al. (2022). "Virus Elimination from Naturally Infected Field Cultivars of Potato (Solanum tuberosum) by Transgenic RNA Interference". International Journal of Molecular Sciences. 23 (14): 8020. doi:10.3390/ijms23148020. PMC 9321115. PMID 35887367.
- ^ He, Z; et al. (2019). "Temporal analysis and adaptive evolution of the global population of potato virus M". Infection, Genetics and Evolution. 73: 167–174. Bibcode:2019InfGE..73..167H. doi:10.1016/j.meegid.2019.04.034. PMID 31054922.
- ^ Ospankulova, G; et al. (2023). "Effect of infection of potato plants by Potato virus Y (PVY), Potato virus S (PVS), and Potato virus M (PVM) on content and physicochemical properties of tuber starch". Food Science & Nutrition. 11 (7): 4002–4009. doi:10.1002/fsn3.3386. PMC 10345660. PMID 37457165.
- ^ Kalnciema, I; et al. (2018). "Potato Virus M-Like Nanoparticles: Construction and Characterization". Molecular Biotechnology. 57 (11–12): 982–992. doi:10.1007/s12033-015-9891-0. PMID 26346833.
- ^ Jaafar, ZA; et al. (2018). "Viral RNA structure‑based strategies to manipulate translation". Nature Reviews Microbiology. 17 (2): 110–123. doi:10.1038/s41579-018-0117-x. PMC 6452865. PMID 30514982.