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Journal articles on the topic 'Plant proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 June 2025

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1

Chakraborty, Biswanath. "Plant Defense Proteins." NBU Journal of Plant Sciences 2, no. 1 (2008): 1–12. http://dx.doi.org/10.55734/nbujps.2007.v02i01.001.

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Plants are compelled to withstand stresses of all kinds, be it biotic, abiotic or anthropogenic as a consequence of their immobility. The initial infection process involving adhesion/recognition events between plants and fungal pathogens is essential for the establishment of pathogenesis. The extracellular matrix (ECM) is a biologically active part of the cell surface composed of a complex mixture of macromolecules that, in addition to serving a structural function, profoundly affect the cellular physiology of the organism. During the past two decades it has become evident that the cell wall is a dynamic organization that is essential for cell division, enlargement and differentiation as well as responding to biotic and abiotic stress. ECM is also the source of signals for cell recognition within the same or between different organisms. Cell walls are natural composite structures, mostly made up of high molecular weight polysaccharides, proteins and lignins. Lignins are only found in specific cell types. Arabidopsis thaliana cell wall proteins (CWP) that can be involved in modifications of cell wall components, wall structure and signaling as well as interactions with plasma membrane proteins at the cell surface has been reviewed.

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2

Shewry, P. R. "Plant Storage Proteins." Biological Reviews 70, no. 3 (August 1995): 375–426. http://dx.doi.org/10.1111/j.1469-185x.1995.tb01195.x.

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3

Graumann, Katja, and David E. Evans. "Plant SUN domain proteins." Plant Signaling & Behavior 5, no. 2 (February 2010): 154–56. http://dx.doi.org/10.4161/psb.5.2.10458.

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4

Cassab, Gladys I. "PLANT CELL WALL PROTEINS." Annual Review of Plant Physiology and Plant Molecular Biology 49, no. 1 (June 1998): 281–309. http://dx.doi.org/10.1146/annurev.arplant.49.1.281.

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5

Vercesi, Aníbal Eugênio, Jiri Borecký, Ivan de Godoy Maia, Paulo Arruda, Iolanda Midea Cuccovia, and Hernan Chaimovich. "PLANT UNCOUPLING MITOCHONDRIAL PROTEINS." Annual Review of Plant Biology 57, no. 1 (June 2006): 383–404. http://dx.doi.org/10.1146/annurev.arplant.57.032905.105335.

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6

Grimes, Howard D., and R. William Breidenbach. "Plant Plasma Membrane Proteins." Plant Physiology 85, no. 4 (December 1, 1987): 1048–54. http://dx.doi.org/10.1104/pp.85.4.1048.

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7

Grimes, Howard D., Raymond M. Slay, and Thomas K. Hodges. "Plant Plasma Membrane Proteins." Plant Physiology 88, no. 2 (October 1, 1988): 444–49. http://dx.doi.org/10.1104/pp.88.2.444.

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8

Kandasamy, Muthugapatti K., Roger B. Deal, Elizabeth C. McKinney, and Richard B. Meagher. "Plant actin-related proteins." Trends in Plant Science 9, no. 4 (April 2004): 196–202. http://dx.doi.org/10.1016/j.tplants.2004.02.004.

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9

Kaas, Quentin, and David J. Craik. "NMR of plant proteins." Progress in Nuclear Magnetic Resonance Spectroscopy 71 (May 2013): 1–34. http://dx.doi.org/10.1016/j.pnmrs.2013.01.003.

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10

Deom, C. Michael, Moshe Lapidot, and Roger N. Beachy. "Plant virus movement proteins." Cell 69, no. 2 (April 1992): 221–24. http://dx.doi.org/10.1016/0092-8674(92)90403-y.

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11

Goodall, Greg, Jonathan Levy, Maria Mieszczak, and Witold Filipowicz. "Plant RNA-binding proteins." Molecular Biology Reports 14, no. 2-3 (1990): 137. http://dx.doi.org/10.1007/bf00360447.

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12

Urrutia, Maria E., John G. Duman, and Charles A. Knight. "Plant thermal hysteresis proteins." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1121, no. 1-2 (May 1992): 199–206. http://dx.doi.org/10.1016/0167-4838(92)90355-h.

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13

Kuchar, M. "Plant telomere-binding proteins." Biologia plantarum 50, no. 1 (March 1, 2006): 1–7. http://dx.doi.org/10.1007/s10535-005-0067-9.

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14

Kawakami, Shigeki, and Yuichiro Watanabe. "Plant viruses. Movement proteins of plant viruses." Uirusu 49, no. 2 (1999): 107–18. http://dx.doi.org/10.2222/jsv.49.107.

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15

Curticăpean, Manuela-Claudia. "Plant Aquaporins." Acta Biologica Marisiensis 2, no. 2 (December 1, 2019): 36–48. http://dx.doi.org/10.2478/abmj-2019-0009.

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Abstract This mini-review briefly presents the main types of plant aquaporins, highlighting their importance for different plant species and for plant cellular functions. Aquaporins (AQPs), families of water channel proteins (WCPs) are transmembrane proteins that are present in prokaryotes, animals, plants, and humans. The plant aquaporins are part of the Major Intrinsic Proteins (MIPs) family which resides in the following plant organs: roots, stems, leaves, flowers, fruits, and seeds. According to the sub-cellular localization, to their sequence homologies and to their phylogenetic distribution, plant aquaporins have been divided in five subgroups: (a) plasma membrane intrinsic proteins (PIPs); (b) tonoplast intrinsic proteins (TIPs); (c) Nodulin26-like intrinsic membrane proteins (NIPs); (d) small basic intrinsic proteins (SIPs) and (e) uncharacterized intrinsic proteins (XIPs). Different subclasses of the plant aquaporins allow several types of transport using: water, glycerol, urea, hydrogen peroxide, organic acids, ethanol, methanol, arsenite, lactic acid, and gaseous compounds. Plant aquaporins have a significant role in cell response to cold stress, photosynthesis, plant growth, cell elongation, reproduction, and seed germination.

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16

Lawit, Shai J., Heidi M. Wych, Deping Xu, Suman Kundu, and Dwight T. Tomes. "Maize DELLA Proteins dwarf plant8 and dwarf plant9 as Modulators of Plant Development." Plant and Cell Physiology 51, no. 11 (October 11, 2010): 1854–68. http://dx.doi.org/10.1093/pcp/pcq153.

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17

BURNS, ROBERT A. "Protease Inhibitors in Processed Plant Foods." Journal of Food Protection 50, no. 2 (February 1, 1987): 161–66. http://dx.doi.org/10.4315/0362-028x-50.2.161.

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Plants contain a wide variety of protein protease inhibitors. However, most is known about the serine protease (trypsin and chymotrypsin) inhibitors found in legumes, particularly soybeans. These inhibitors in unheated legume protein (a) impair the protein's nutritional quality, (b) induce pancreatic hyper-trophy in some but not all experimental animals, (c) enhance the action of chemical pancreatic carcinogens in Wistar rats but not hamsters or mice, (d) are reported to be carcinogenic to the pancreas of Wistar rats and (e) inhibit certain experimental tumors in rats, mice and hamsters. The physiological significance of the low residual protease inhibitor levels in commercially processed plant proteins and human foods prepared from such proteins remains to be resolved. Plant proteins prepared for human consumption, however, contain low levels of pro-tease inhibitor activity which are of no nutritional concern in animals or humans.

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18

Marangon, Matteo, Simone Vincenzi, and Andrea Curioni. "Wine Fining with Plant Proteins." Molecules 24, no. 11 (June 11, 2019): 2186. http://dx.doi.org/10.3390/molecules24112186.

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Fining treatments involve the addition of a substance or a mixture to wine, and are generally carried out in order to clarify, stabilize or modify the wine’s organoleptic characteristics. Usually these fining agents will bind the target compound(s) to form insoluble aggregates that are subsequently removed from the wine. The main reasons to perform wine fining treatments are to carry out wine clarification, stabilization and to remove phenolic compounds imparting unwanted sensory characteristics on the wine, which is an operation that often relies on the use of animal proteins, such as casein, gelatin, egg and fish proteins. However, due to the allergenic potential of these animal proteins, there is an increasing interest in developing alternative solutions including the use of fining proteins extracted from plants (e.g., proteins from cereals, grape seeds, potatoes, legumes, etc.), and non-proteinaceous plant-based substances (e.g., cell wall polysaccharides and pomace materials). In this article, the state of the art alternative fining agents of plant origins are reviewed for the first time, including considerations of their organoleptic and technological effects on wine, and of the allergenic risks that they can pose for consumers.

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19

Ma, Kai Kai, Maija Greis, Jiakai Lu, Alissa A. Nolden, David Julian McClements, and Amanda J. Kinchla. "Functional Performance of Plant Proteins." Foods 11, no. 4 (February 18, 2022): 594. http://dx.doi.org/10.3390/foods11040594.

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Increasingly, consumers are moving towards a more plant-based diet. However, some consumers are avoiding common plant proteins such as soy and gluten due to their potential allergenicity. Therefore, alternative protein sources are being explored as functional ingredients in foods, including pea, chickpea, and other legume proteins. The factors affecting the functional performance of plant proteins are outlined, including cultivars, genotypes, extraction and drying methods, protein level, and preparation methods (commercial versus laboratory). Current methods to characterize protein functionality are highlighted, including water and oil holding capacity, protein solubility, emulsifying, foaming, and gelling properties. We propose a series of analytical tests to better predict plant protein performance in foods. Representative applications are discussed to demonstrate how the functional attributes of plant proteins affect the physicochemical properties of plant-based foods. Increasing the protein content of plant protein ingredients enhances their water and oil holding capacity and foaming stability. Industrially produced plant proteins often have lower solubility and worse functionality than laboratory-produced ones due to protein denaturation and aggregation during commercial isolation processes. To better predict the functional performance of plant proteins, it would be useful to use computer modeling approaches, such as quantitative structural activity relationships (QSAR).

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20

Barbosa, Mayck Silva, Bruna da Silva Souza, Ana Clara Silva Sales, Jhoana D’arc Lopes de Sousa, Francisca Dayane Soares da Silva, Maria Gabriela Araújo Mendes, Káritta Raquel Lustoza da Costa, Taiane Maria de Oliveira, Tatiane Caroline Daboit, and Jefferson Soares de Oliveira. "Antifungal Proteins from Plant Latex." Current Protein & Peptide Science 21, no. 5 (June 2, 2020): 497–506. http://dx.doi.org/10.2174/1389203720666191119101756.

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Latex, a milky fluid found in several plants, is widely used for many purposes, and its proteins have been investigated by researchers. Many studies have shown that latex produced by some plant species is a natural source of biologically active compounds, and many of the hydrolytic enzymes are related to health benefits. Research on the characterization and industrial and pharmaceutical utility of latex has progressed in recent years. Latex proteins are associated with plants’ defense mechanisms, against attacks by fungi. In this respect, there are several biotechnological applications of antifungal proteins. Some findings reveal that antifungal proteins inhibit fungi by interrupting the synthesis of fungal cell walls or rupturing the membrane. Moreover, both phytopathogenic and clinical fungal strains are susceptible to latex proteins. The present review describes some important features of proteins isolated from plant latex which presented in vitro antifungal activities: protein classification, function, molecular weight, isoelectric point, as well as the fungal species that are inhibited by them. We also discuss their mechanisms of action.

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21

Evrard, Jean-Luc, Laurent Pieuchot, Jan W. Vos, Isabelle Vernos, and Anne-Catherine Schmit. "Plant TPX2 and related proteins." Plant Signaling & Behavior 4, no. 1 (January 2009): 69–72. http://dx.doi.org/10.4161/psb.4.1.7409.

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22

Talalaev, O. S. "Plant small heat shock proteins." Biopolymers and Cell 21, no. 5 (September 20, 2005): 392–99. http://dx.doi.org/10.7124/bc.000701.

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23

Thakur, Nitasha, and Neelam Sharma. "Plant Lectin as defense proteins." Biotech Today : An International Journal of Biological Sciences 5, no. 1 (2015): 25. http://dx.doi.org/10.5958/2322-0996.2015.00004.6.

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24

Moffatt, Barbara, Vanya Ewart, and Ann Eastman. "Cold comfort: plant antifreeze proteins." Physiologia Plantarum 126, no. 1 (January 2006): 5–16. http://dx.doi.org/10.1111/j.1399-3054.2006.00618.x.

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25

Aguilera-Alvarado, G. Paulina, and Sobeida Sï¿½nchez-Nieto. "Plant Hexokinases are Multifaceted Proteins." Plant and Cell Physiology 58, no. 7 (April 25, 2017): 1151–60. http://dx.doi.org/10.1093/pcp/pcx062.

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26

Helm, Ricki M. "Allergy to Plant Seed Proteins." Journal of New Seeds 3, no. 3 (October 26, 2001): 37–60. http://dx.doi.org/10.1300/j153v03n03_02.

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27

Day, Peter R. "The biology of plant proteins." Critical Reviews in Food Science and Nutrition 36, sup001 (November 1996): 39–47. http://dx.doi.org/10.1080/10408399609527758.

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28

Hwang, Hee-Youn, and Seong-Hee Bhoo. "Photoperiodic Proteins in Plant Cells." Journal of Applied Biological Chemistry 53, no. 3 (September 30, 2010): 121–25. http://dx.doi.org/10.3839/jabc.2010.023.

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29

Peumans, W. J., and EJM Van Damme. "Lectins as Plant Defense Proteins." Plant Physiology 109, no. 2 (October 1, 1995): 347–52. http://dx.doi.org/10.1104/pp.109.2.347.

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30

Parate, Vishal R., and Ritika P. Chaudhari. "Study on Plant Based Proteins." International Journal of Innovations in Engineering and Science 9, no. 4 (August 5, 2024): 110–15. http://dx.doi.org/10.46335/ijies.2024.9.4.21.

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31

Bouché, Nicolas, Ayelet Yellin, Wayne A. Snedden, and Hillel Fromm. "PLANT-SPECIFIC CALMODULIN-BINDING PROTEINS." Annual Review of Plant Biology 56, no. 1 (June 2005): 435–66. http://dx.doi.org/10.1146/annurev.arplant.56.032604.144224.

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32

Prescott, Andrea. "Plant proteins — an engineer's perspective." Trends in Biotechnology 11, no. 2 (February 1993): 69–70. http://dx.doi.org/10.1016/0167-7799(93)90126-t.

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33

Jervis, L., and W. S. Pierpoint. "Purification technologies for plant proteins." Journal of Biotechnology 11, no. 2-3 (August 1989): 161–98. http://dx.doi.org/10.1016/0168-1656(89)90117-x.

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34

Van Engelen, F. "Extracellular proteins in plant embryogenesis." Trends in Genetics 8, no. 1 (1992): 66–70. http://dx.doi.org/10.1016/0168-9525(92)90046-7.

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35

Van Engelen, Fred A., and Sacco C. De Vries. "Extracellular proteins in plant embryogenesis." Trends in Genetics 8, no. 2 (February 1992): 66–70. http://dx.doi.org/10.1016/0168-9525(92)90352-5.

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36

Y. I. Takinami, Patricia. "Radiation, Plant Proteins and Sustainability." American Journal of Biological and Environmental Statistics 2, no. 4 (2016): 28. http://dx.doi.org/10.11648/j.ajbes.20160204.11.

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37

Hanke, G., C. Bowsher, M. N. Jones, I. Tetlow, and M. Emes. "Proteoliposomes and plant transport proteins." Journal of Experimental Botany 50, no. 341 (December 1, 1999): 1715–26. http://dx.doi.org/10.1093/jxb/50.341.1715.

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38

Moriyasu, Y., and M. Tazawa. "Plant vacuole degrades exogenous proteins." Protoplasma 130, no. 2-3 (June 1986): 214–15. http://dx.doi.org/10.1007/bf01276604.

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39

Ahsan, Nagib, Rashaun S. Wilson, and Jay J. Thelen. "Absolute Quantitation of Plant Proteins." Current Protocols in Plant Biology 3, no. 1 (March 2018): 1–13. http://dx.doi.org/10.1002/cppb.20064.

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40

Reddy, Narendra, and Yiqi Yang. "Thermoplastic films from plant proteins." Journal of Applied Polymer Science 130, no. 2 (May 27, 2013): 729–38. http://dx.doi.org/10.1002/app.39481.

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41

Jacques, Silke, Bart Ghesquière, Frank Van Breusegem, and Kris Gevaert. "Plant proteins under oxidative attack." PROTEOMICS 13, no. 6 (February 4, 2013): 932–40. http://dx.doi.org/10.1002/pmic.201200237.

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42

Kreuger, Marc, and Gerrit-Jan van Holst. "Arabinogalactan proteins and plant differentiation." Plant Molecular Biology 30, no. 6 (March 1996): 1077–86. http://dx.doi.org/10.1007/bf00019543.

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43

Bardani, Eirini, Paraskevi Kallemi, Martha Tselika, Konstantina Katsarou, and Kriton Kalantidis. "Spotlight on Plant Bromodomain Proteins." Biology 12, no. 8 (August 2, 2023): 1076. http://dx.doi.org/10.3390/biology12081076.

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Bromodomain-containing proteins (BRD-proteins) are the “readers” of histone lysine acetylation, translating chromatin state into gene expression. They act alone or as components of larger complexes and exhibit diverse functions to regulate gene expression; they participate in chromatin remodeling complexes, mediate histone modifications, serve as scaffolds to recruit transcriptional regulators or act themselves as transcriptional co-activators or repressors. Human BRD-proteins have been extensively studied and have gained interest as potential drug targets for various diseases, whereas in plants, this group of proteins is still not well investigated. In this review, we aimed to concentrate scientific knowledge on these chromatin “readers” with a focus on Arabidopsis. We organized plant BRD-proteins into groups based on their functions and domain architecture and summarized the published work regarding their interactions, activity and diverse functions. Overall, it seems that plant BRD-proteins are indispensable components and fine-tuners of the complex network plants have built to regulate development, flowering, hormone signaling and response to various biotic or abiotic stresses. This work will facilitate the understanding of their roles in plants and highlight BRD-proteins with yet undiscovered functions.

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44

Kader, Jean-Claude. "Lipid-transfer proteins: a puzzling family of plant proteins." Trends in Plant Science 2, no. 2 (February 1997): 66–70. http://dx.doi.org/10.1016/s1360-1385(97)82565-4.

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45

Watanabe, Yuichiro. "Special issue: Plant viruses. Movement proteins of plant viruses." Uirusu 44, no. 1 (1994): 11–17. http://dx.doi.org/10.2222/jsv.44.11.

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46

Kerksick, Chad M., Andrew Jagim, Anthony Hagele, and Ralf Jäger. "Plant Proteins and Exercise: What Role Can Plant Proteins Have in Promoting Adaptations to Exercise?" Nutrients 13, no. 6 (June 7, 2021): 1962. http://dx.doi.org/10.3390/nu13061962.

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Adequate dietary protein is important for many aspects of health with current evidence suggesting that exercising individuals need greater amounts of protein. When assessing protein quality, animal sources of protein routinely rank amongst the highest in quality, largely due to the higher levels of essential amino acids they possess in addition to exhibiting more favorable levels of digestibility and absorption patterns of the amino acids. In recent years, the inclusion of plant protein sources in the diet has grown and evidence continues to accumulate on the comparison of various plant protein sources and animal protein sources in their ability to stimulate muscle protein synthesis (MPS), heighten exercise training adaptations, and facilitate recovery from exercise. Without question, the most robust changes in MPS come from efficacious doses of a whey protein isolate, but several studies have highlighted the successful ability of different plant sources to significantly elevate resting rates of MPS. In terms of facilitating prolonged adaptations to exercise training, multiple studies have indicated that a dose of plant protein that offers enough essential amino acids, especially leucine, consumed over 8–12 weeks can stimulate similar adaptations as seen with animal protein sources. More research is needed to see if longer supplementation periods maintain equivalence between the protein sources. Several practices exist whereby the anabolic potential of a plant protein source can be improved and generally, more research is needed to best understand which practice (if any) offers notable advantages. In conclusion, as one considers the favorable health implications of increasing plant intake as well as environmental sustainability, the interest in consuming more plant proteins will continue to be present. The evidence base for plant proteins in exercising individuals has seen impressive growth with many of these findings now indicating that consumption of a plant protein source in an efficacious dose (typically larger than an animal protein) can instigate similar and favorable changes in amino acid update, MPS rates, and exercise training adaptations such as strength and body composition as well as recovery.

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47

İsmail, Karakaş. "Plants That Can be Used as Plant-Based Edible Vaccines; Current Situation and Recent Developments." Virology & Immunology Journal 6, no. 3 (November 4, 2022): 1–10. http://dx.doi.org/10.23880/vij-16000302.

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Among the purposes of genetic engineering technology applications in plants, improving product quality, increasing resistance to harmful organisms and improving agronomic properties, the most important one is the production of drugs, hormones and vaccines for humans and animals (for example, the use of potatoes in cholera vaccines). Today, the use of plants as bioreactors to obtain recombinant proteins from plants has been further developed and accelerated thanks to the developments in plant genetics, molecular biology and biotechnology. Appearing as a concept about a decade ago, plant bioreactors are genetically modified plants whose genomes have been manipulated to incorporate and express gene sequences of a number of useful proteins from different biological sources. Plant-derived bioreactor systems offer significant advantages over techniques used for other biological-based protein production. Easy and inexpensive production from plant tissues, providing appropriate post-translational modifications for the production of recombinant viral and bacterial antigens, and showing similar biological activity to recombinant vaccines obtained in microorganisms are important reasons that encourage the use of plant tissues in vaccine production. Edible vaccines, which create an immune response in the body against a foreign pathogen that causes disease, have a working mechanism that serves as both a nutritive and a vaccine that we consume in our daily lives. In the development of edible vaccines, the gene responsible for the production of the part of the foreign pathogen that causes the disease, that is, the antigen, which provides the immune response in the body, is transferred to the plants. With this technique, antigen production is carried out in plants. For example, thanks to today's advancing technology, enough hepatitis B antigens to vaccinate all of the world's approximately 133 million live births each year can be grown on a field of approximately two hundred hectares. In addition to these, edible vaccine technology also makes edible vaccines an interesting concept as secondgeneration vaccines, as they allow several antigens to approach M (microcoat) cells at the same time, by offering multicomponent vaccine proteins that are possible by crossing two plant lines.

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48

Narváez-Barragán, Delia A., Omar E. Tovar-Herrera, Lorenzo Segovia, Mario Serrano, and Claudia Martinez-Anaya. "Expansin-related proteins: biology, microbe–plant interactions and associated plant-defense responses." Microbiology 166, no. 11 (December 1, 2020): 1007–18. http://dx.doi.org/10.1099/mic.0.000984.

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Expansins, cerato-platanins and swollenins (which we will henceforth refer to as expansin-related proteins) are a group of microbial proteins involved in microbe-plant interactions. Although they share very low sequence similarity, some of their composing domains are near-identical at the structural level. Expansin-related proteins have their target in the plant cell wall, in which they act through a non-enzymatic, but still uncharacterized, mechanism. In most cases, mutagenesis of expansin-related genes affects plant colonization or plant pathogenesis of different bacterial and fungal species, and thus, in many cases they are considered virulence factors. Additionally, plant treatment with expansin-related proteins activate several plant defenses resulting in the priming and protection towards subsequent pathogen encounters. Plant-defence responses induced by these proteins are reminiscent of pattern-triggered immunity or hypersensitive response in some cases. Plant immunity to expansin-related proteins could be caused by the following: (i) protein detection by specific host-cell receptors, (ii) alterations to the cell-wall-barrier properties sensed by the host, (iii) displacement of cell-wall polysaccharides detected by the host. Expansin-related proteins may also target polysaccharides on the wall of the microbes that produced them under certain physiological instances. Here, we review biochemical, evolutionary and biological aspects of these relatively understudied proteins and different immune responses they induce in plant hosts.

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49

Maulik, A., A. I. Sarkar, S. Devi, and S. Basu. "Polygalacturonase-inhibiting proteins - leucine-rich repeat proteins in plant defence." Plant Biology 14 (November 1, 2011): 22–30. http://dx.doi.org/10.1111/j.1438-8677.2011.00501.x.

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50

Butkovic, Anamarija, Valerian V. Dolja, Eugene V. Koonin, and Mart Krupovic. "Plant virus movement proteins originated from jelly-roll capsid proteins." PLOS Biology 21, no. 6 (June 15, 2023): e3002157. http://dx.doi.org/10.1371/journal.pbio.3002157.

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Numerous, diverse plant viruses encode movement proteins (MPs) that aid the virus movement through plasmodesmata, the plant intercellular channels. MPs are essential for virus spread and propagation in distal tissues, and several unrelated MPs have been identified. The 30K superfamily of MPs (named after the molecular mass of tobacco mosaic virus (TMV) MP, the classical model of plant virology) is the largest and most diverse MP variety, represented in 16 virus families, but its evolutionary origin remained obscure. Here, we show that the core structural domain of the 30K MPs is homologous to the jelly-roll domain of the capsid proteins (CPs) of small RNA and DNA viruses, in particular, those infecting plants. The closest similarity was observed between the 30K MPs and the CPs of the viruses in the families Bromoviridae and Geminiviridae. We hypothesize that the MPs evolved via duplication or horizontal acquisition of the CP gene in a virus that infected an ancestor of vascular plants, followed by neofunctionalization of one of the paralogous CPs, potentially through the acquisition of unique N- and C-terminal regions. During the subsequent coevolution of viruses with diversifying vascular plants, the 30K MP genes underwent explosive horizontal spread among emergent RNA and DNA viruses, likely permitting viruses of insects and fungi that coinfected plants to expand their host ranges, molding the contemporary plant virome.

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