Protein Profiling Analyses in Arbuscular Mycorrhizal Symbiosis

  • Ghislaine Recorbet
  • Eliane Dumas-Gaudot*


Because proteins are well known as key effectors of plant responses to environmental cues including recognition, signaling, transport, and defense reactions, interest has been paid to characterize those involved in the establishment and functioning of arbuscular mycorrhizal (AM) symbiosis. The recent development of high throughput techniques has enabled large-scale analyses of symbiosis-related proteins. Different proteomic strategies have been established depending on the symbiotic stage targeted and on the abundance of mycorrhizal material. In mature mycorrhiza, sub-cellular proteomic approaches have been developed in the model legume Medicago truncatula to target symbiosis-related membrane proteins eligible for nutrient transport and signaling between symbionts upon arbuscule formation. Modifications in the M. truncatula root proteome during early stages of AM symbiosis have also been investigated by comparing protein patterns of non-inoculated roots and roots synchronized for appressorium formation. Concomitantly, proteomic approaches have been developed on in vitro-grown mycorrhiza to identify extraradical fungal proteins along with endomycorrhizins. The genome sequencing programs launched for M. truncatula and Glomus intraradices are likely to provide additional knowledge about AM symbiosis-related proteins.


Arbuscular Mycorrhizal Mycorrhizal Root Appressorium Formation Actin Depolymerization Factor Root Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


  1. Amiour N, Recorbet G, Robert F, Gianinazzi S, Dumas-Gaudot E (2006) Mutations in DMI3. and SUNN modify the appressorium-responsive root proteome in arbuscular mycorrhiza Mol Plant Microbe Interact 19:988–997PubMedCrossRefGoogle Scholar
  2. Balestrini R, Lanfranco L (2006) Fungal and plant gene expression in arbuscular mycorrhizal symbiosis. Mycorrhiza 16:509–524PubMedCrossRefGoogle Scholar
  3. Benabdellah K, Azcon-Aguilar C, Ferrol N (1998) Soluble and membrane symbiosis-related polypeptides associated with the development of arbuscular mycorrhizas in tomato (Lycopersicon esculentum. ) New Phytol 140:135–143CrossRefGoogle Scholar
  4. Benabdellah K, Azcon-Aguilar C, Ferrol N (2000) Alterations in the plasma membrane polypeptide pattern of tomato roots (Lycopersicon esculentum. ) during the development of arbuscular mycorrhiza J Exp Bot 51:747–754PubMedCrossRefGoogle Scholar
  5. Bestel-Corre G, Dumas-Gaudot E, Poinsot V, Dieu M, Dierick J, van Tuinen D, Remacle J, Gianinazzi-Pearson V, Gianinazzi S (2002) Proteome analysis and identification of symbiosis-related proteins from Medicago truncatula. Gaertn. by two-dimensional electrophoresis and mass spectrometry. Electrophoresis 23:122–137PubMedCrossRefGoogle Scholar
  6. Bhat RA, Panstruga R (2005) Lipid rafts in plants. Planta 223:5–19PubMedCrossRefGoogle Scholar
  7. Blee E (2002) Impact of phyto-oxylipins in plant defense. Trends Plant Sci 7:315–321PubMedCrossRefGoogle Scholar
  8. Carvalho-Niebel F, Lescure N, Cullimore JV, Gamas P (1998) The Medicago truncatula MtAnn1. gene encoding an annexin is induced by Nod factors and during the symbiotic interaction with Rhizobium meliloti Mol Plant Microbe Interact 11:504–513CrossRefGoogle Scholar
  9. Catalano CM, Lane WS, Sherrier DJ (2004) Biochemical characterization of symbiosome membrane proteins from Medicago truncatula. root nodules Electrophoresis 25:519–531PubMedCrossRefGoogle Scholar
  10. Dumas-Gaudot E, Valot B, Bestel-Corre G, Recorbet G, St-Arnaud M, Fontaine B, Dieu, M Raes, M, Saravanan R Gianinazzi S (2004) Proteomics as a way to identify extra-radicular fungal proteins from Glomus intraradices. -RiT-DNA carrot root mycorrhizas FEMS Microbiol Ecol 48:401–411PubMedCrossRefGoogle Scholar
  11. El Yahyaoui F, Kuster H, Ben Amor B, Hohnjec N, Puhler A, Becker A, Gouzy J, Vernie T, Gough C, Niebel A, Godiard L, Gamas P (2004) Expression profiling in Medicago truncatula. identifies more than 750 genes differentially expressed during nodulation, including many potential regulators of the symbiotic program Plant Physiol 136:3159–3176PubMedCrossRefGoogle Scholar
  12. Fester T, Strack D (2002) A mycorrhiza-responsive protein in wheat roots. Mycorrhiza 12:219–222PubMedCrossRefGoogle Scholar
  13. García-Garrido JM, Ocampo JA (2002). Regulation of the plant defence response in arbuscular mycorrhizal symbiosis. J Exp Bot 53:1377–1386PubMedCrossRefGoogle Scholar
  14. Genre A, Chabaud M, Timmers T, Bonfante P, Barker DG (2005) Arbuscular mycorrhizal fungi elicit a novel intracellular apparatus in Medicago truncatula. root epidermal cells before infection Plant Cell 17:3489–3499PubMedCrossRefGoogle Scholar
  15. Gianinazzi-Pearson V, Arnould C, Oufattole M, Arango M, Gianinazzi S (2000) Differential activation of H+. -ATPase genes by an arbuscular mycorrhizal fungus in root cells of transgenic tobacco Planta 211:609–613PubMedCrossRefGoogle Scholar
  16. Harrison M, Dixon RA (1993) Isoflavonoid accumulation and expression of defense gene transcripts during the establishment of vesicular-arbuscular mycorrhizal associations in roots of Medicago truncatula. Mol Plant Microbe Interact 6:643–654CrossRefGoogle Scholar
  17. He F, Emmet MR, Håkansson K, Hendrikson CL, Marshall A (2004) Theoretical and experimental prospects for protein identification based solely on accurate mass measurement. J Proteome Res 3:61–67PubMedCrossRefGoogle Scholar
  18. Hohnjec N, Vieweg A, Puhler A, Becker A, Kuster H (2005) Overlaps in the transcriptional profiles of Medicago truncatula. roots inoculated with two different Glomus fungi provide insights into the genetic program activated during arbuscular mycorrhiza Plant Physiol 137:1283–1301PubMedCrossRefGoogle Scholar
  19. Journet EP, van Tuinen D, Gouzy J, Crespeau H, Carreau V, Farmer MJ, Niebel A, Chiex T, Saillon O, Chatagnier O, Godiard L, Micheli F, Kahn D, Gianinazzi-Pearson V, Gamas P (2002) Exploring root symbiotic programs in the model legume Medicago trunctula. using EST analysis Nuc Acids Res 15:5579–5592CrossRefGoogle Scholar
  20. Krajinski F, Hause B, Gianinazzi-Pearson V, Franken P (2002) Mtha1. , a plasma membrane H+-ATPase gene from Medicago truncatula, shows arbuscule-specific induced expression in mycorrhizal tissue Plant Biol 4:754–761CrossRefGoogle Scholar
  21. Liska AJ, Popov A, Sunyaev S, Coughlin P, Habermann B, Shevchenko A, Bork P, Eric Karsenti E, Shevchenko A (2004) Homology-based functional proteomics by mass spectrometry: application to the Xenopus. microtubule-associated proteome Proteomics 4:S2707–2721CrossRefGoogle Scholar
  22. Manthey K, Krajinski F, Hohnjec N, Firnhaber C, Puhler A, Perlick AM, Kuster H (2004) Transcriptome profiling in root nodules and arbuscular mycorrhiza identifies a collection of novel genes induced during Medicago truncatula. root endosymbioses Mol Plant Microbe Interact 17:1063–1077PubMedCrossRefGoogle Scholar
  23. Martin F, Tuskan GA, DiFazio SP, Lammers P, Newcombe G, Podila GK (2004) Symbiotic sequencing for the Populus. mesocosm New Phytol 161:330–335CrossRefGoogle Scholar
  24. O’Connell RJ, Panstruga R (2006) Tête a tête inside a plant cell: establishing compatibility between plants and biotrophic fungi and oomycetes. New Phytol 171:699–718PubMedCrossRefGoogle Scholar
  25. Panstruga R (2003) Establishing compatibility between plants and obligate biotrophic pathogens. Curr Opin Plant Biol 6:320–326PubMedCrossRefGoogle Scholar
  26. Parniske M (2000) Intracellular accommodation of microbes by plants: a common developmental program for symbiosis and disease? Curr Opin Plant Biol 3:320–328PubMedCrossRefGoogle Scholar
  27. Penheiter AR, Duff SM, Sarath G (1997) Soybean root nodule acid phosphatase. Plant Physiol 114:597–604PubMedCrossRefGoogle Scholar
  28. Rossignol M, Peltier JB, Mock HP, Matros A, Maldonado AM, Jorrín J (2006) Plant proteome analysis: a 2004–2006 update. Proteomics 6:5529–5548PubMedCrossRefGoogle Scholar
  29. Saalbach G, Erik P, Wienkoop S (2002) Characterisation by proteomics of peribacteroid space and peribacteroid membrane preparations from pea (Pisum sativum. ) symbiosomes Proteomics 2:325–337PubMedCrossRefGoogle Scholar
  30. Schulze-Lefert P, Panstruga R (2003) Establishment of biotrophy by parasitic fungi and reprogramming of host cells for disease resistance. Ann Rev Phytopathol 41:641–667CrossRefGoogle Scholar
  31. Thurston, G Regan S, Rampitsch C, Xing T (2005) Proteomic and phosphoproteomic approaches to understand plant–pathogen interactions. Physiol Mol Plant Pathol 66:3–11CrossRefGoogle Scholar
  32. Tucker SL, Talbot NJ (2001) Surface attachment and pre-penetration stage development by plant pathogenic fungi. Ann Rev Phytopathol 39:385–417CrossRefGoogle Scholar
  33. Valot B, Dumas-Gaudot E, Gianinazzi S (2004) Sub-cellular proteomic analysis of a Medicago truncatula. root fraction Phytochemistry 65:1721–1732PubMedCrossRefGoogle Scholar
  34. Valot B, Dieu M, Recorbet G, Raes M, Gianinazzi S, Dumas-Gaudot E (2005) Identification of membrane-associated proteins regulated by the arbuscular mycorrhizal symbiosis. Plant Mol Biol 59:565–580PubMedCrossRefGoogle Scholar
  35. Valot B, Negroni L, Zivy M, Gianinazzi S, Dumas-Gaudot E (2006) A mass spectrometric approach to identify arbuscular mycorrhiza-related proteins in root plasma membrane fractions. Proteomics 6:S145–155PubMedCrossRefGoogle Scholar
  36. Weidmann S, Sanchez L, Descombin J, Chatagnier O, Gianinazzi S, Gianinazzi-Pearson V (2004) Fungal elicitation of signal transduction-related plant genes precedes mycorrhiza establishment and requires the dmi3. gene in Medicago truncatula Mol Plant Microbe Interact 17:1385–1393PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2009

Authors and Affiliations

  • Ghislaine Recorbet
    • 1
  • Eliane Dumas-Gaudot*
    • 1
  1. 1.UMR 1088 INRA/CNRS 5184/UB Plante-Microbe-EnvironnementINRA/CMSEFrance

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