Evidence for specific, high‐affinity binding sites for a proteinaceous elicitor in tobacco plasma membrane

Wendehenne, David; Binet, Marie‐Noëlle; Blein, Jean‐Pierre; Ricci, Pierre; Pugin, Alain

doi:10.1016/0014-5793(95)01108-q

Cited by 100 publications

(67 citation statements)

References 21 publications

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“…Displacement experiments demonstrate that the specific binding sites for LTP1 and cryptogein are identical, and that the LTP1-interaction with the binding sites is reversible [59], as for cryptogein [34]. Thus, LTP1 binding sites exhibit all the characteristics of putative receptors.…”

Section: Ltps Bind With the Elicitin Receptorsmentioning

confidence: 90%

Section: Elicitin Receptorsmentioning

confidence: 99%

“…In addition, although the cryptogein binding curves could be analyzed as hyperbolic curves [34,36,40], that of wheat LTP1 presented a sigmoidal shape. This shape suggests that the LTP binding site is oligomeric, the molecular interaction involving positive cooperativity.…”

Section: Ltps Bind With the Elicitin Receptorsmentioning

confidence: 99%

“…Further experiments using either tobacco cell suspensions or plants showed that the cryptogein binding sites are located on the plasma membranes [34]. The binding is saturable, reversible, specific with an apparent Kd of 2nM (well correlated with concentrations required for biological activities in vivo), and with a very low number of sites (about 100-200 fmoles/mg plasmalemma proteins), suggesting that these sites could be the biological receptors for elicitins [34].These receptors are postulated to be glycoproteins since plasma membranes treated with proteases and N-glycosidase F are not able to bind cryptogein anymore [35,36]. The molecular mass of the elicitin receptors has been tentatively approached by cross-link and radiation-inactivation experiments.…”

mentioning

confidence: 99%

“…However, although the formation of a sterol-elicitin complex is a requisite step in elicitin recognition by receptors [56], we still have no indication on the importance of lipid-LTP complexes formation for binding to specific sites and/or for triggering cell responses. Moreover, the nature of extracellular or membrane putative ligands for LTP1 remains to be elucidated, since these proteins do not capture phytosterols as elicitins do.In addition, although the cryptogein binding curves could be analyzed as hyperbolic curves [34,36,40], that of wheat LTP1 presented a sigmoidal shape. This shape suggests that the LTP binding site is oligomeric, the molecular interaction involving positive cooperativity.…”

mentioning

confidence: 99%

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Involvement of lipid-protein complexes in plant-microorganism interactions

Blein¹

2002

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Summary : Increasing concerns about the environmental impact of modern agricultural have prompted research for alternate practices to pesticide treatments, notably using plant defense mechanisms. Thus, isolation and characterization of plant defense elicitors have been the main step of studies in many groups. Moreover, in the global concept of interactions between organisms and their environment, a major concern is to discriminate recognition between exogenous and endogenous signals, notably during pathogenic or allergenic interactions involving small proteins, such as elicitins or lipid transfer proteins (LTPs). Elicitins and lipid transfer proteins (LTP) are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defense mechanisms, the biological function of LTPs is still an enigma. They are ubiquitous plant proteins able to load and transfer hydrophobic molecules such as fatty acids or phospholipids. Among them, LTPs1 (type 1 lipid transfer proteins) constitute a multigenic family of secreted plant lipid binding proteins that are constitutively expressed in specific tissues and/or induced in response to biotic and abiotic stress (for reviews [1][2][3][4]). Their biological function is still unknown, even if some data provide arguments for a role of these proteins in the assembly of extracellular hydrophobic polymers (i.e., cutin and suberin) [2,4] and/or in plant defense against fungal pathogens [1,3]. Beside their involvement in plant defense, LTPs1 are also known to be pan-allergens of plant-derived foods [5]. Finally, the discovery of the sterol carrier-properties of elicitins has opened new perspectives dealing with the relationship between this function and the elicitor activity of these small cystein-rich proteins. Nevertheless, this elicitor activity is restrained to few plant species, and thus does not appear in accordance with a universal lipid transfer function. These considerations required a reassessment of the precise role of elicitins for both fungi and plants [6].Résumé : La stimulation des mécanismes naturels de défense des plantes représente une stratégie alternative à l'utilisation de la lutte chimique en phytoprotection. Dans ce contexte, les élicitines, qui sont de petites protéines sécrétées par des Phytophthora et des Pythium, induisent une réaction de type hypersensible chez des plantes comme le tabac. Ces plantes deviennent résistantes à l'agression de leurs agents pathogènes. La récente découverte que les élicitines sont des protéines de transfert de stérols a apporté une vue nouvelle sur l'activité moléculaire des élicitines. Élicitines et protéines de transfert de lipides (LTP) sont capables de charger et de transporter des molécules lipidiques et partagent des caractères communs tant au plan structural que fonctionnel mais, tandis que les élicitines sont connues pour leur activité élicitrice de réaction de défense chez les plantes, l'activité biologique des LTP reste inconnue. Cependant, ...

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Section: Ltps Bind With the Elicitin Receptorsmentioning

confidence: 90%

Section: Elicitin Receptorsmentioning

confidence: 99%