The Potyviridae family comprises several genera of plant‐infecting single‐stranded positive‐sense RNA viruses, with flexible and filamentous virion particles. Currently, eight genera are recognised within the family, including the large genus Potyvirus with near 150 aphid‐transmitted viruses. The rest of genera, Brambyvirus, Bymovirus, Ipomovirus, Macluravirus, Poacevirus, Rymovirus and Tritimovirus, are differentiated by their genome composition and structure (two RNA molecules for bymoviruses, one for the rest of genera), by the vector organisms responsible of their dissemination and by genome sequence similarity. Globally very important as pathogens, they also have drawn the attention of the research community for years to study aspects such as taxonomy, evolution, virion structure, functional characterisation of viral proteins, diagnosis, control, interaction with hosts and vectors and even biotechnological applications. Recent advances concerning viruses within the family are being presented.

Key Concepts

  • Members of the family Potyviridae are positive‐strand RNA viruses infecting plants, with genomes directly translated in large polyproteins that are proteolytically processed by virus‐encoded proteinases.
  • The family Potyviridae is the largest group of RNA plant viruses. It consists of eight genera, seven of them including viruses with monopartite genomes and a genus that includes viruses with bipartite genomes.
  • Virus particles of members of the family Potyviridae are flexuous rods formed by multiple subunits of a single capsid protein.
  • The replication of viruses of the family Potyviridae takes place in virus‐induced membranous structures. Membrane vesicles induced by viral proteins, likely including replication complexes, move cell‐to‐cell during infection.
  • Viruses of the family Potyviridae may cause a large range of macroscopic symptoms, which in many cases result in serious diseases of crops with high socio‐economical relevance. A very distinctive microscopic feature of Potyviridae infections is the accumulation of pinwheel‐shaped cylindrical inclusions.
  • Members of the family Potyviridae usually can be transmitted by mechanical means; however, in nature, these viruses are vector‐transmitted by specific types of arthropods or plasmodiophorids, depending on the genera.
  • Some viruses in the family Potyviridae have restricted host ranges. However, many other members of the family are able to infect numerous plant species, and alternative hosts can greatly affect the incidence and epidemiology of these viruses.
  • The large number of viruses in the family illustrates their evolutive success with different driving forces operating during speciation, including host adaptation and recombination events when more than one virus infect the same host plant.
  • Both engineered vectors based on members of the family Potyviridae and genetic elements derived from them have been exploited as tools of biotechnological utility.
  • From both economic and scientific standpoints, the family Potyviridae can be considered in any top list, as evidenced by the fast‐growing numbers of hits in general or scientific literature Internet search engines.

Keywords: phytopathology; plant diseases; plant viruses; potyvirus; RNA viruses

Figure 1. Thin section of the cytoplasm of a Nicotiana benthamiana plant cell infected with Plum pox virus, showing ‘pinwheel’ inclusions. Reproduced with permission of D. López‐Abella, CIB‐CSIC (Madrid, Spain). Bar equals 200 nm.
Figure 2. Structure of potyvirus particles. (a) Cryo‐electron micrograph of a detail of the flexuous particles of soybean mosaic virus (SMV) (bar equals 25 nm). (d) Outside view of the modelisation of SMV particle structure by iterative helical real‐space reconstruction, along with transversal (b) and longitudinal (d) sections at the same scale [bar in (b) equals 5 nm, and also applies to (c) and (d)]. The virion presents a central hole surrounded by compact and well‐defined CP sub‐units disposed with its longest dimension diverging radially from the centre. The helical symmetry of the particle is estimated to be 8.8 sub‐units of CP per turn. Reproduced with permission of Amy Kendall and Gerald Stubbs, Vandervilt University, Nashville, Tennessee, USA.
Figure 3. Genomic maps of viruses in the family Potyviridae. (a) Below the scale in kilobases, the genomic ssRNA of a member of the genus potyvirus is shown as a solid line, with the covalently linked VPg protein depicted as a solid circle at the 5′‐end, and the poly A tail at the 3′‐end indicated by An. ORFs are shown as boxes divided in individual gene products with their names above. Vertical lines with arrowheads pointing downward mark the proteolytic cleavage sites, and the three proteinases responsible for the polyprotein processing are identified with the corresponding colour‐coded arrowheads inside the boxes. The pipo ORF is shown by a box that follows P3N (N‐terminal portion of P3) after the expected frameshifting point, generating a P3N+PIPO product. A similar organisation of gene products corresponds to brambyvirus, macluravirus, poacevirus, rymovirus, and tritimovirus and to two ipomoviruses, Sweet potato mild mottle virus (SPMMV) and Tomato mild mottle virus (ToMMV). (b) Variant of the previous organisation corresponding to a bymovirus, with the two separate RNA segments, RNA1 and RNA2. (c) Genomic organisation of ipomoviruses, with the type member SPMMV (upper panel), and variants with two proteases P1a + P1b and absence of HCPro (centre panel), as in Cucumber vein yellowing virus (CVYV), or with a single P1, absence of HCPro and presence of the HAM1h extra product between NIb and CP (bottom panel), as in Cassava brown streak virus (CBSV). Other variants not shown in the figure include the presence of a putative pispo ORF in the P1 region of several sweet potato‐infecting potyviruses (Li et al., 2012, Virus Genes 45, 118–125) and the presence of a conserved AlkB domain within the P1 of the brambyvirus Blackberry virus Y (Susaimuthu et al., 2008, Virus Res 131, 145–151).


Adams MJ, Antoniw JF and Fauquet CM (2005) Molecular criteria for genus and species discrimination within the family Potyviridae. Archives of Virology 150: 459–479.

Adams MJ, Antoniw JF and Mullins JG (2001) Plant virus transmission by plasmodiophorid fungi is associated with distinctive transmembrane regions of virus‐encoded proteins. Archives of Virology 146: 1139–1153.

Aranda M and Maule A (1998) Virus‐induced host gene shutoff in animals and plants. Virology 243: 261–267.

Atreya CD and Pirone TP (1993) Mutational analysis of the helper component‐proteinase gene of a potyvirus: effects of amino acid substitutions, deletions, and gene replacement on virulence and aphid transmissibility. Proceedings of the National Academy of Sciences of the United States of America 90: 11919–11923.

Ballut L, Drucker M, Pugniere M, et al. (2005) HcPro, a multifunctional protein encoded by a plant RNA virus, targets the 20S proteasome and affects its enzymic activities. The Journal of General Virology 86: 2595–2603.

Bedoya L, Martínez F, Rubio L and Daròs JA (2010) Simultaneous equimolar expression of multiple proteins in plants from a disarmed potyvirus vector. Journal of Biotechnology 150: 268–275.

Blanc S, Lopez‐Moya JJ, Wang R, et al. (1997) A specific interaction between coat protein and helper component correlates with aphid transmission of a potyvirus. Virology 231: 141–147.

Carbonell A, Maliogka VI, Pérez JJ, et al. (2013) Diverse amino acid changes at specific positions in the N‐terminal region of the coat protein allow Plum pox virus to adapt to new hosts. Molecular Plant‐Microbe Interactions 26: 1211–1224.

Carrington JC and Freed DD (1990) Cap‐independent enhancement of translation by a plant potyvirus 5′ nontranslated region. Journal of Virology 64: 1590–1597.

Chung BY, Miller WA, Atkins JF and Firth AE (2008) An overlapping essential gene in the Potyviridae. Proceedings of the National Academy of Sciences of the United States of America 105: 5897–5902.

Del Toro F, Tena Fernández F, Tilsner J, et al. (2014) Potato virus Y HCPro localization at distinct, dynamically related and environment‐influenced structures in the cell cytoplasm. Molecular Plant‐Microbe Interactions 27: 1331–1343.

Desbiez C, Chandeysson C and Lecoq H (2014) A short motif in the N‐terminal part of the coat protein is a host‐specific determinant of systemic infectivity for two potyviruses. Molecular Plant Pathology 15: 217–221.

Dogimont C, Chovelon V, Pauquet J, Boualem A and Bendahmane A (2014) The Vat locus encodes for a CC‐NBS‐LRR protein that confers resistance to Aphis gossypii infestation and A. gossypii‐mediated virus resistance. The Plant Journal 80: 993–1004.

Dolja VV, Haldeman R, Robertson NL, Dougherty WG and Carrington JC (1994) Distinct functions of capsid protein in assembly and movement of tobacco etch potyvirus in plants. The EMBO Journal 13: 1482–1491.

Dolja VV, McBride HJ and Carrington JC (1992) Tagging of plant potyvirus replication and movement by insertion of beta‐glucuronidase into the viral polyprotein. Proceedings of the National Academy of Sciences of the United States of America 89: 10208–10212.

Dujovny G, Valli A, Calvo M and García JA (2009) A temperature‐controlled amplicon system derived from Plum pox potyvirus. Plant Biotechnology Journal 7: 49–58.

Gabrenaite‐Verkhovskaya R, Andreev IA, Kalinina NO, et al. (2008) Cylindrical inclusion protein of Potato virus A is associated with a subpopulation of particles isolated from infected plants. The Journal of General Virology 89: 829–838.

Giner A, Lakatos L, García‐Chapa M, López‐Moya JJ and Burgyán J (2010) Viral protein inhibits RISC activity by argonaute binding through conserved WG/GW motifs. PLoS Pathogens 6: e1000996.

Grangeon R, Jiang J, Wan J, et al. (2013) 6K2‐induced vesicles can move cell to cell during Turnip mosaic virus infection. Frontiers in Microbiology 4: 351.

Haldeman‐Cahill R, Daròs JA and Carrington JC (1998) Secondary structures in the capsid protein coding sequence and 3′ nontranslated region involved in amplification of the Tobacco etch virus genome. Journal of Virology 72: 4072–4079.

Hisa Y, Suzuki H, Atsumi G, et al. (2014) P3N‐PIPO of Clover yellow vein virus exacerbates symptoms in pea infected with White clover mosaic virus and is implicated in viral synergism. Virology 449: 200–206.

Hong Y and Hunt AG (1996) RNA polymerase activity catalyzed by a potyvirus‐encoded RNA‐dependent RNA polymerase. Virology 226: 146–151.

Jiang J and Laliberté JF (2011) The genome‐linked protein VPg of plant viruses‐a protein with many partners. Current Opinion in Virology 1: 347–354.

Kasschau KD, Xie Z, Allen E, et al. (2003) P1/HC‐Pro, a viral suppressor of RNA silencing, interferes with Arabidopsis development and miRNA function. Developmental Cell 4: 205–217.

Kelloniemi J, Mäkinen K and Valkonen JPT (2008) Three heterologous proteins simultaneously expressed from a chimeric potyvirus: infectivity, stability and the correlation of genome and virion lengths. Virus Research 135: 282–291.

Kendall A, McDonald M, Bian W, et al. (2008) Structure of flexible filamentous plant viruses. Journal of Virology 82: 9546–9554.

Mallory AC, Parks G, Endres MW, et al. (2002) The amplicon‐plus system for high‐level expression of transgenes in plants. Nature Biotechnology 20: 622–625.

Martínez F and Daròs JA (2014) Tobacco etch virus protein P1 traffics to the nucleolus and associates with the host 60S ribosomal subunits during infection. Journal of Virology 88: 10725–10737.

Mathur C and Savithri HS (2012) Novel ATPase activity of the polyprotein intermediate, Viral Protein genome‐linked‐Nuclear Inclusion‐a protease, of Pepper vein banding potyvirus. Biochemical and Biophysical Research Communications 427: 113–118.

Mbanzibwa DR, Tian Y, Mukasa SB and Valkonen JP (2009) Cassava brown streak virus (Potyviridae) encodes a putative Maf/HAM1 pyrophosphatase implicated in reduction of mutations and a P1 proteinase that suppresses RNA silencing but contains no HC‐Pro. Journal of Virology 83: 6934–6940.

McDonald M, Kendall A, Bian W, et al. (2010) Architecture of the potyviruses. Virology 405: 309–313.

Moreno A, Tjallingii WF, Fernandez‐Mata G and Fereres A (2012) Differences in the mechanism of inoculation between a semi‐persistent and a non‐persistent aphid‐transmitted plant virus. The Journal of General Virology 93: 662–667.

Moury B, Fabre F and Senoussi R (2007) Estimation of the number of virus particles transmitted by an insect vector. Proceedings of the National Academy of Sciences of the United States of America 104: 17891–17896.

Pérez JJ, Udeshi ND, Shabanowitz J, et al. (2013) O‐GlcNAc modification of the coat protein of the potyvirus Plum pox virus enhances viral infection. Virology 442: 122–131.

Pruss G, Ge X, Shi XM, Carrington JC and Bowman Vance V (1997) Plant viral synergism: the potyviral genome encodes a broad‐range pathogenicity enhancer that transactivates replication of heterologous viruses. The Plant Cell 9: 859–868.

Rajamäki ML, Streng J and Valkonen JPT (2014) Silencing suppressor protein VPg of a potyvirus interacts with the plant silencing‐related protein SGS3. Molecular Plant‐Microbe Interactions 27: 1199–1210.

Rakitina DV, Kantidze OL, Leshchiner AD, et al. (2005) Coat proteins of two filamentous plant viruses display NTPase activity in vitro. FEBS Letters 579: 4955–4960.

Rojas MR, Zerbini FM, Allison RF, Gilbertson RL and Lucas WJ (1997) Capsid protein and helper component‐proteinase function as potyvirus cell‐to‐cell movement proteins. Virology 237: 283–295.

Ruiz‐Ferrer V, Boskovic J, Alfonso C, et al. (2005) Structural analysis of tobacco etch potyvirus HC‐pro oligomers involved in aphid transmission. Journal of Virology 79: 3758–3765.

Schaad MC, Haldeman‐Cahill R, Cronin S and Carrington JC (1996) Analysis of the VPg‐proteinase (NIa) encoded by tobacco etch potyvirus: effects of mutations on subcellular transport, proteolytic processing, and genome amplification. Journal of Virology 70: 7039–7048.

Seo JK, Vo Phan MS, Kang SH, Choi HS and Kim KH (2013) The charged residues in the surface‐exposed C‐terminus of the Soybean mosaic virus coat protein are critical for cell‐to‐cell movement. Virology 446: 95–101.

Stenger DC, Hein GL and French R (2006) Nested deletion analysis of Wheat streak mosaic virus HC‐Pro: Mapping of domains affecting polyprotein processing and eriophyid mite transmission. Virology 350: 465–474.

Sun L, Andika IB, Shen J, Yang D and Chen J (2014) The P2 of Wheat yellow mosaic virus rearranges the endoplasmic reticulum and recruits other viral proteins into replication‐associated inclusion bodies. Molecular Plant Pathology 15: 466–478.

Tatineni S, Qu F, Li R, Morris TJ and French R (2012) Triticum mosaic poacevirus enlists P1 rather than HC‐Pro to suppress RNA silencing‐mediated host defense. Virology 433: 104–115.

Torrance L, Andreev IA, Gabrenaite‐Verhovskaya R, et al. (2006) An unusual structure at one end of potato potyvirus particles. Journal of Molecular Biology 357: 1–8.

Valli A, Gallo A, Calvo M, Pérez JJ and García JA (2014) A novel role of the potyviral helper component proteinase contributes to enhance the yield of viral particles. Journal of Virology 88: 9808–9818.

Valli A, Martín‐Hernández AM, López‐Moya JJ and García JA (2006) RNA silencing suppression by a second copy of the P1 serine protease of Cucumber vein yellowing ipomovirus, a member of the family Potyviridae that lacks the cysteine protease HCPro. Journal of Virology 80: 10055–10063.

Wei T, Zhang C, Hong J, et al. (2010) Formation of complexes at plasmodesmata for potyvirus intercellular movement is mediated by the viral protein P3N‐PIPO. PLoS Pathogens 6: e1000962.

Xiong R and Wang A (2013) SCE1, the SUMO‐conjugating enzyme in plants that interacts with NIb, the RNA‐dependent RNA polymerase of Turnip mosaic virus, is required for viral infection. Journal of Virology 87: 4704–4715.

Young BA, Stenger DC, Qu F, et al. (2012) Tritimovirus P1 functions as a suppressor of RNA silencing and an enhancer of disease symptoms. Virus Research 163: 672–677.

Zeenko V and Gallie DR (2005) Cap‐independent translation of Tobacco etch virus is conferred by an RNA pseudoknot in the 5′‐leader. The Journal of Biological Chemistry 280: 26813–26824.

Further Reading

Elena SF and Rodrigo G (2012) Towards an integrated molecular model of plant‐virus interactions. Current Opinion in Virology 2: 719–724.

Gibbs A and Ohshima K (2010) Potyviruses and the digital revolution. Annual Review of Phytopathology 48: 205–223.

Ivanov KI, Eskelin K, Lohmus A and Mäkinen K (2014) Molecular and cellular mechanisms underlying potyvirus infection. The Journal of General Virology 95: 1415–1429.

Mäkinen K and Hafren A (2014) Intracellular coordination of potyviral RNA functions in infection. Frontiers in Plant Science 5: 110.

Pirone TP and Blanc S (1996) Helper‐dependent vector transmission of plant viruses. Annual Review of Phytopathology 34: 227–247.

Revers F, Le Gall O, Candresse T and Maule AJ (1999) New advances in understanding the molecular biology of plant/potyvirus interactions. Molecular Plant‐Microbe Interactions 12: 367–376.

Riechmann JL, Laín S and García JA (1992) Highlights and prospects of potyvirus molecular biology. The Journal of General Virology 73: 1–16.

Simón‐Mateo C and García JA (2011) Antiviral strategies in plants based on RNA silencing. Biochimica et Biophysica Acta 1809: 722–731.

Sorel M, Garcia JA and German‐Retana S (2014) The Potyviridae cylindrical inclusion helicase: a key multipartner and multifunctional protein. Molecular Plant‐Microbe Interactions 27: 215–226.

Truniger V and Aranda MA (2009) Recessive resistance to plant viruses. Advances in Virus Research 75: 119–159.

Contact Editor close
Submit a note to the editor about this article by filling in the form below.

* Required Field

How to Cite close
Valli, Adrián, García, Juan A, and López‐Moya, Juan J(May 2015) Potyviridae. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0000755.pub3]