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PubMed2000

Quantification of lectin in freshwater prawn (Macrobrachium rosenbergii ) hemolymph by ELISA.

An enzyme-linked immunoabsorbent assay was developed to quantify the lectin present in the hemolymph of the freshwater prawn Macrobrachium rosenbergii. This method involves the use of murine monoclonal IgG1 with kappa light chain (designated as 3G1) antibodies raised against the purified lectin, the assay that we developed recognized as little as 30 ng/ml of lectin, and was used to measure the lectin concentration in animals at different maturation stages. The highest concentration of lectin was identified in the hemolymph from post-larval prawns and the lowest in molt stage adult animals. The hemagglutination activity of the lectin was four-fold higher in adult than in juvenile specimens, although in all cases N-acetylated sugar residues, such as N-acetyl-D-glucosamine, N-acetyl-D-galactosamine, and N-acetyl-D-neuraminic acid were inhibitors of the lectin activity, suggesting that lectin plays a role in the transport of N-acetylated sugar in juvenile prawns. Our results indicate that lectin concentration and hemagglutinating activity could be influenced by developmental conditions of the freshwater prawn.

Acetylgalactosamine↗
PubMed1997

D-galactoside-specific lectins from the body wall of an echiuroid (Urechis unicinctus) and two annelids (Neanthes japonica and Marphysa sanguinea).

Lectins recognizing D-galactosides were purified from the body wall of an echiuroid; Urechis unicinctus and two annelids; Neanthes japonica and Marphysa sanguinea, with single step lactosyl-agarose affinity column chromatography. SDS-PAGE under reduced and non-reduced conditions showed that U. unicinctus lectin had a major (36 kDa) and two minor (40 and 14 kDa) proteins, and that N. japonica lectin and M. sanguinea lectin had single 33 and 35 kDa proteins, respectively. Lectins were solubilized in the presence of lactose from tissues, and all polypeptides were shown to have sugar binding activity. The antisera raised against U. unicinctus lectin and N. japonica lectin crossreacted with each other but did not crossreact with bull frog (Rana catesbeiana) egg galectin-1 or a D-galactoside-specific lectin purified from sea urchin (Anthocidaris crassispina) eggs. These echiuroid and annelid lectins are immunologically similar, but distinct from members of the vertebrate galectin family.

Animals↗
PubMed1999

Enhancement of anti-Aeromonas salmonicida activity in Atlantic salmon (Salmo salar) macrophages by a mannose-binding lectin.

We investigated the effects of a calcium-dependent mannose-binding lectin isolated from the serum of Atlantic salmon on Aeromonas salmonicida viability and the anti-A. salmonicida activity of Atlantic salmon macrophages. In the absence of other factors, binding of this lectin at concentrations of 0.8, 4.0 and 20.0 ng ml(-1) to virulent A. salmonicida failed to significantly reduce (P> 0.05) cell viability. However, binding of the lectin to A. salmonicida did result in significant (P < or = 0.05) dose-dependent increases in phagocytosis, and bactericidal activity. Significant increases (P < or = 0.05) were also observed in phagocyte respiratory burst activity within the lectin concentration range of 4.0-20.0 ng ml(-1) but the stimulation was not dose dependent at these lectin concentrations. At the lowest lectin concentration tested (0.32 ng ml(-1)), a significant decrease (P < or = 0.05) in respiratory burst was observed. The structure and activity of this lectin are similar to that of mammalian mannose-binding lectins, which are known to play a pivotal role in innate immunity. The presence of this lectin may be an important defense mechanism against Gram-negative bacteria such as A. salmonicida.

Aeromonas↗
PubMed1999

Characterization of cell surface lectin-binding patterns of human airway epithelium.

Glycosylated structures on the cell surface have a role in cell adhesion, migration, and proliferation. Repair of the airway epithelium after injury requires each of these processes, but the normal cell surface glycosylation of non-mucin producing airway epithelial cells is unknown. We examined cell surface glycosylation in human airway epithelial cells in tissue sections and in human airway epithelial cell lines in culture. Thirty-eight lectin probes were used to determine specific carbohydrate residues by lectin-histochemistry. Galactose or galactosamine-specific lectins labeled basal epithelial cells, lectins specific for several different carbohydrate structures bound columnar epithelial cells, and fucose-specific lectins labeled all airway epithelial cells. The epithelial cell lines 1HAEo- and 16HBE14o- bound lectins that were specific to basal epithelial cells. Flow cytometry of these cell lines with selected lectins demonstrated that lectin binding was to cell surface carbohydrates, and revealed possible hidden tissue antigens on dispersed cultured cells. We demonstrate specific lectin-binding patterns on the surface of normal human airway epithelial cells. The expression of specific carbohydrate residues may be useful to type epithelial cells and as a tool to examine cell events involved in epithelial repair.

Cell Line, Transformed↗
PubMed2001

Different effects of lectins on the ligand binding of the NMDA receptors and sigma sites in rat brain hippocampus synaptic membranes.

The effects of the lectins concanavalin A, WGA, ricin, abrin, and the mistletoe lectins from Viscum album MLI, MLII, and MLIII on the binding of ligands of the NMDA and sigma receptors in rat hippocampus synaptic plasma membranes were investigated. Binding of [3H]MK-801, [3H]glutamate, [3H]5,7-DCKA, and [3H]glycine to the membranes was decreased by 40-60% after addition of galactose-specific lectins (mistletoe lectins MLI, MLII, ricin, abrin) at concentrations of 0.01 mg/ml, but was not affected by the glucose- and mannose-specific lectin Con A, an acetylglucosamine-specific lectin WGA, or an acetylgalactosamine-specific lectin MLIII. The binding of [3H]SKF 10047 was decreased only in the presence of MLIII and did not change after addition of the other lectins. It is suggested that lectin-sensitive ligand binding sites of sigma- and NMDA receptors are located separately, and that the carbohydrate side chains of the sigma receptor do not participate in the modulation of the NMDA-receptor.

Animals↗
PubMed1996

Lectin-bearing polymerized liposomes as potential oral vaccine carriers.

PURPOSE: The potential of using lectin-modified polymerized liposomes as Peyer's patch targeted oral delivery vehicles was examined. METHODS: Two types of lectins, Ulex Europaeus Agglutinin I (UEA I) and Wheat Germ Agglutinin (WGA), were modified with a hydrophobic anchor N-glutaryl-phosphotidylethanolamine (NGPE). The modified lectins were incorporated into liposome bilayers and the liposomes were subsequently stabilized through polymerization. The presence of the lectins on the liposome surfaces was first confirmed with X-ray photoelectron spectroscopy. Surface-immobilized lectins were then shown to retain their carbohydrate binding activities as well as specificities based on an in vitro aggregation assay. Finally, delivery efficiencies of lectin-bearing liposomes were determined in mice. RESULTS: About 10.5% UEA I liposomes and 5.8% WGA liposomes were taken up from the gastrointestinal tract. These numbers are significantly higher than the 3.2% observed in the case of lectin-free liposomes. At the same time, UEA I liposomes exhibited the most effective Peyer's patch targeting among the three, which directly correlated with the highest delivery efficiency observed. CONCLUSIONS: This establishes that lectin modification of liposomes can promote binding to Peyer's patches, which will give improved efficiency for Peyer's patch targeted delivery. All these point to the potential for these lectin-modified liposomes as novel vehicles for oral vaccination.

Drug Carriers↗
PubMed2001

Plant lectins: occurrence, biochemistry, functions and applications.

Growing insights into the many roles of glycoconjugates in biorecognition as ligands for lectins indicates a need to compare plant and animal lectins. Furthermore, the popularity of plant lectins as laboratory tools for glycan detection and characterization is an incentive to start this review with a brief introduction to landmarks in the history of lectinology. Based on carbohydrate recognition by lectins, initially described for concanavalin A in 1936, the chemical nature of the ABH-blood group system was unraveled, which was a key factor in introducing the term lectin in 1954. How these versatile probes are produced in plants and how they are swiftly and efficiently purified are outlined, and insights into the diversity of plant lectin structures are also given. The current status of understanding their functions calls for dividing them into external activities, such as harmful effects on aggressors, and internal roles, for example in the transport and assembly of appropriate ligands, or in the targeting of enzymatic activities. As stated above, attention is given to intriguing parallels in structural/functional aspects of plant and animal lectins as well as to explaining caveats and concerns regarding their application in crop protection or in tumor therapy by immunomodulation. Integrating the research from these two lectin superfamilies, the concepts are discussed on the role of information-bearing glycan epitopes and functional consequences of lectin binding as translation of the sugar code (functional glycomics).

Animals↗
PubMed2000

Endogenous lectins as cell surface transducers.

Interactions between cells or between cell and substratum involve specific receptors and their ligands. Among the various cell surface receptors identified during the last decades, the carbohydrate-binding proteins, e.g., lectins are of peculiar interest because glycolipids, glycoproteins and proteoglycans have been shown to interact with lectins on the surface of animal cells. Animal lectins are recognized as molecules playing important roles in a variety of biological processes through binding to glycoconjugates and lectin-like receptors such as selectins, sialoadhesins (CD22, CD33), natural killer receptors (NKR-P1, CD69 and CD94/NKG2), hyaluronate receptors (CD44, RHAMM, ICAM-1), B-cell associated antigen (CD23, CD72), beta2 leukocyte integrin (CD11b/CD18) or the well-known receptors for mannose, mannose-6-phosphate or asialoglycoprotein have been suggested to be able to mediate the transfer of information from the outside to the inside of the cell. This review focuses on the most recent advances in our understanding of the molecular basis of "outside-in" signaling mediated by lectins. Lectin-like receptors are involved in signal transduction in a great variety of ways; at the molecular level, they mimic in most of the cases the function of growth factor receptor either coupled to tyrosine kinase activity or to heterotrimeric G protein. They lead to a multiplicity of cellular events following their activation depending on factors such as cellular type, species and/or tissue. Nevertheless the potential of surface lectins as transducers is emphasized by the observation that in a few cases lectin-like receptors induce either novel signal transduction mechanism or new intracellular events with regards to what it has been observed as a consequence of growth factor receptor activation. This observation brings the idea that lectins may offer, as cell surface transducers, an alternative or additional signaling potential to cell.

Animals↗
PubMed2004

The identification of inducible cytoplasmic/nuclear carbohydrate-binding proteins urges to develop novel concepts about the role of plant lectins.

During the last few years compelling evidence has been presented for the occurrence of cytoplasmic/nuclear plant lectins that are not detectable in normal plants but are only induced upon application of well-defined stress conditions. Since both the regulation of the expression and the subcellular location indicate that these 'non-classical lectins' are good candidates to play a physiologically important role as mediators of specific protein-carbohydrate-interactions within the plant cell, a critical assessment is made of the impact of these findings on the development of novel concepts about the role of plant lectins. Based on an analysis of the biochemical, molecular and evolutionary data of a jasmonate-induced chitin-binding lectin from tobacco leaves and a salt/jasmonate-induced leaf lectin from rice it is concluded that these lectins most probably interact with endogenous glycans located within the cytoplasmic/nuclear compartment of the plant cell. Several working mechanisms are proposed to explain how these inducible lectins may fulfill an important regulatory or structural role in stressed cells. In addition, the question of the evolutionary relationship(s) between the newly discovered inducible lectins and their 'classical' constitutively expressed homologs is addressed. Evidence is presented that the 'non-classical lectins' represent the main evolutionary line and that some of their corresponding genes were used as templates for genes encoding storage protein-like 'classical' homologs.

Cell Nucleus↗
PubMed1999

Calcium-independent haemolysis via the lectin pathway of complement activation in the guinea-pig and other species*.

We previously reported that complement-dependent haemolysis of sheep erythrocytes (E) coated with mannan (M) and sensitized with human mannan-binding lectin (MBL) via the lectin pathway in man occurs in Mg-EGTA and requires alternative pathway amplification. Calcium was required for MBL binding to E-M, but once the E-M-MBL intermediate was formed, MBL was retained and haemolysis occurred in the absence of calcium. Comparable or greater lectin pathway haemolysis in the absence of calcium was observed upon incubation of E-M-MBL in guinea-pig, rat, dog and pig sera, and was further investigated in the guinea-pig, in which titres were much higher ( approximately 14-fold) than in man, and in contrast to humans, greater than classical pathway haemolytic activity. As in human serum, no lysis was observed in C4- or C2-deficient guinea-pig serum until purified C4 or C2, respectively, were restored. However, lectin pathway haemolytic activity in the guinea-pig did not require the alternative pathway. Removal (>98%) of factor D activity by three sequential passages through Sephadex G-75, resulting in serum which retained a normal classical pathway but no alternative pathway haemolytic activity, did not reduce the ability of guinea-pig serum to mediate haemolysis via the lectin pathway. Further, the C3-convertase formed via the lectin pathway (E-M-MBL-C4,2) lysed in C2-deficient guinea-pig but not human serum chelated with EDTA, a condition which precludes alternative pathway amplification. Thus, lectin pathway haemolysis occurs efficiently in guinea-pig serum, in the absence of calcium and without requirement for alternative pathway amplification. The guinea-pig provides a model for studying the assembly and haemolytic function of a lectin pathway which contrasts with the lectin pathway of man, and allows for comparisons that may help clarify the role of this pathway in complement biology.

Animals↗
PubMed2005

Thermodynamic, kinetic, and electron microscopy studies of concanavalin A and Dioclea grandiflora lectin cross-linked with synthetic divalent carbohydrates.

The jack bean lectin concanavalin A (ConA) and the Dioclea grandiflora lectin (DGL) are highly homologous Man/Glc-specific members of the Diocleinae subtribe. Both lectins bind, cross-link, and precipitate with carbohydrates possessing multiple terminal nonreducing Man residues. The present study investigates the binding and cross-linking interactions of ConA and DGL with a series of synthetic divalent carbohydrates that possess spacer groups with increasing flexibility and length between terminal alpha-mannopyranoside residues. Isothermal titration microcalorimetry was used to determine the thermodynamics of binding of the two lectins to the divalent analogs, and kinetic light scattering and electron microscopy studies were used to characterize the cross-linking interactions of the lectins with the carbohydrates. The results demonstrated that divalent analogs with flexible spacer groups between the two terminal Man residues possess higher affinities for the two lectins as compared with those with inflexible spacer groups. Furthermore, despite their high degree of homology, ConA and DGL exhibit differences in their kinetics of cross-linking and precipitation with the divalent analogs. Electron microscopy shows the loss of organized cross-linked lattices of the two lectins with analogs possessing increased distance between the terminal Man residues. The loss of lattice patterns with the analogs is distinct for each lectin. These results have important implications for the interactions of lectins with multivalent carbohydrate receptors in biological systems.

Calorimetry↗
PubMed2005

Characterization of a binary tandem domain F-type lectin from striped bass (Morone saxatilis).

Among other functions, lectins play an important role in the innate immune response of vertebrates and invertebrates by recognizing exposed glycans on the surface of potential pathogens. Despite the typically weak interaction of lectin domains with their carbohydrate ligands, they usually achieve high avidity through oligomeric structures or by the presence of tandem carbohydrate-binding domains along the polypeptide. The recently described structure of the fucose-binding European eel agglutinin revealed a novel lectin fold (the "F-type" fold), which is shared with other carbohydrate-binding proteins and apparently unrelated proteins from prokaryotes to vertebrates, and a unique fucose-binding sequence motif. Here we described the biochemical and molecular characterization of a unique fucose-binding lectin (MsaFBP32) isolated from serum of the striped bass (Morone saxatilis), composed of two tandem domains that exhibit the eel carbohydrate recognition sequence motif, which we designate F-type. We also described a novel lectin family ("F-type") constituted by a large number of proteins exhibiting greater multiples of the F-type motif, either tandemly arrayed or in mosaic combinations with other domains, including a putative transmembrane receptor, that suggests an extensive functional diversification of this lectin family. Among the tandem lectins, MsaFBP32 and other tandem binary homologues appear unique in that although their N-terminal domain shows close similarity to the fucose recognition domain of the eel agglutinin, their C-terminal domain exhibits changes that potentially could confer a distinct specificity for fucosylated ligands. In contrast with the amniotes, in which the F-type lectins appear conspicuously absent, the widespread gene duplication in the teleost fish suggests these F-type lectins acquired increasing evolutionary value within this taxon.

Amino Acid Sequence↗
PubMed2002

An in-vitro evaluation of lectin cytotoxicity using cell lines derived from the ocular surface.

Lectins are proteins or glycoproteins of non-immune origin capable of binding to one or more specific sugar residues. The potential for using lectins as a means of locating and "anchoring" a drug delivery system to a target site on a mucosal surface in order to promote controlled drug delivery and enhanced absorption has been described in previous work. Toxicity is evident for many lectins, and this study has investigated the cytotoxicity of lectins to cells derived from the cornea and conjunctiva. Cultures of transformed cell lines from the conjunctiva and cornea were exposed to solution of lectins, and the viability of these cells assessed by their ability to take up an MTT stain relative to the control. Clear evidence of lectin cytotoxicity was apparent for all of the lectins tested in this study, particularly at higher concentrations and over the longer (48 h) time period. This would raise issues with their potential use in targeted drug delivery systems. The lectins from Lycopersicon esculentum and Helix pomatia appeared to show the least cytotoxic activity and so could be considered the most promising. The lectins from Solanum tuberosum and Triticum vulgaris showed significant cytotoxicity, which contrasts with previous in-vivo studies. However, they might be considered for investigation as targeted therapeutic agents in the treatment of malignant diseases.

Antineoplastic Agents↗
PubMed1980

Purified lectin from skeletal muscle inhibits myotube formation in vitro.

A lactose-extractable lectin obtained from 14--16-d embryonic chick pectoral muscle and myotube muscle cultures by affinity chromatography inhibited myotube formation in culture. When applied to muscle cultures at 0.09 micrograms/ml, the purified lectin produced variable effects on the inhibition of myotube formation related to the time and length of application, suggesting that components of the culture medium and/or temperature produced inactivation. Hemagglutination assays showed that the lectin was inactivated by horse serum and by chick embryo extract but not by L-15 salt solution at 4 degrees C. Incubation in L-15 solution at 37 degrees C with or without 2 mM dithiothreitol resulted in inactivation in 2--3 h. To maximize the effect of the lectin on the inhibition of myotube formation, primary muscle cultures were grown in low [Ca+2] medium to inhibit fusion, and then [Ca+2] was increased to elicit fusion in the absence and presence of lectin with solution renewal every 2 h. Without lectin, myotube formation was normal, whereas, with lectin, it was inhibited by 93%. Continued incubation at 37 degrees C. without renewal of lectin resulted in myotube formation, suggesting reversibility by lectin inactivation.

Cell Adhesion↗
PubMed1980

Lectin receptors as markers for Trypanosoma cruzi. Developmental stages and a study of the interaction of wheat germ agglutinin with sialic acid residues on epimastigote cells.

Trypanosoma cruzi at various stages of maturation and differentiation have been isolated by conventional cellular fractionation procedures and characterized by cell surface markers using 30 highly purified lectins encompassing all known sugar specificities. Cell surface carbohydrates of the various T. cruzi stages were analyzed by agglutination and lectin-binding assays. Specific receptors for wheat germ agglutinin (WGA), Helix pomatia, Sophora japonica, and Bandeiraea simplicifolia lectin II were found only in culture epimastigotes, whereas peanut agglutinin (PNA) sites were present exclusively in amastigotes, those for Phaseolus vulgaris in bloodstream trypomastigotes and amastigotes, and for Wistaria floribunda hemagglutinin predominantly in culture forms of T. cruzi. The N-acetylgalactosamine (DGalNAc)-binding lectin from Bauhinia purpurea agglutinated and inhibited the movement of epimastigotes and bloodstream trypomastigotes, but it only inhibited--without agglutinating--culture trypomastigotes. Because both the agglutination and inhibition of movement were reversed by specific sugar haptens, Bauhinia purpurea sites were present in all the flagellated parasites. On the other hand, PNA sites were detectable on epimastigotes after the cells were treated with sialidase, whereas, at the same time, WGA receptors were completely removed and those for the other sialic acid-binding proteins, Aaptos papillata lectin II and Limulus polyphemus, were partially eliminated; moreover, the activity of Wistaria floribunda hemagglutinin, a DGalNAc-binding lectin, increased 4,000 times. Trypsinization and lyzozyme treatment of epimastigote cells did not significantly affect lectin agglutination or lectin binding. WGA reacted solely with sialic acid residues on epimastigote cell surface with an apparent association constant of 2 x 10(6) M-1, each epimastigote having an estimated average of 3 x 10(6) WGA sites, as determined by binding experiments and a minimum of 7.7 x 10(6) sialic acid residues, as calculated by colorimetric method after sialidase digestion. Evidences are presented that the sialyl residues are rapidly regenerated (in approximately 4 h) and that they, at least for the most part, are not adsorbed from the culture medium. The receptor for the D-mannose-binding lectins (concanavalin A [Con A] and Lens culinaris) must either be on the same carbohydrate moiety having the WGA site, or, if in a distinct molecule, both carrier molecules of Con A and WGA sites must be located close to each other in the plasma membrane of the parasite.

Animals↗
PubMed2004

A database analysis of jacalin-like lectins: sequence-structure-function relationships.

Lectins are known to be important for many biological processes, due to their ability to recognize cell surface carbohydrates with high specificity. Plant lectins have been model systems to study protein-carbohydrate recognition, because individually they exhibit high sensitivity and as a group large diversity in recognizing carbohydrate structures. Although extensive studies have been carried out for legume lectins that have led to interesting insights into the sequence determinants of sugar recognition in them, frameworks with such specific correlations are not available for other plant lectin families. This study reports a large-scale data acquisition and extensive analysis of sequences and structures of beta-prism-I or jacalin-related lectins (JRLs) and shows that hypervariability in the binding site loops generates carbohydrate recognition diversity, a strategy analogous to that in legume lectins. Analyses of the size, conformation, and sequence variability in key regions reveal the existence of a common theme, encoded as a set of structural features over a common scaffold, in defining specificity. This study also points to the remarkable range of domain architectures, often arising out of gene duplication events in lectins of this family. The data analyzed here also indicate a spectacular variety of quaternary associations possible in this family of lectins that have implications for glycan recognition. These results thus provide sequence-structure-function correlations, an understanding of the molecular basis of carbohydrate recognition by beta-prism-I lectins, and also a rationale for engineering specific recognition capabilities in relevant molecules.

Amino Acid Sequence↗
PubMed1981

Quantitative assay for lectin-induced cytoagglutination by means of an electronic particle-counting technique.

A method employing an electronic particle-counting technique was used to quantify lectin-induced agglutination of human granulocytes and lymphocytes with either concanavalin A or wheat germ agglutinin. The number and mean volume of single cells and aggregates in the presence of increasing concentrations of lectin were computed from 95% confidence intervals. Agglutination depended on both the number of free cells and the number and size of the cell clusters. Changes in these two variables were mutually independent of one another, and both were simultaneously determined. An index of agglutination that takes the effect of these two variables into account was defined as (formula: see text) VA equals mean volume of cell aggregates, NS equals number of single cells, NA equals number of cell aggregates, VS equals mean volume of single cells, rb equals r at a given lectin concentration, and ra equals r in the absence of lectin. For any combination of lectin and cell type, the agglutination curve, as described by zeta, consisted of two components: a) a flat region in which zeta remained constant with increasing lectin concentrations and b) a region in which zeta increased linearly as a function of the logarithm of lectin concentration. The shapes of these curves offered two parameters for quantitative comparison of agglutinability: 1)threshold concentration, defined as the minimum concentration of lectin (microgram/ml) required to bring about a measurable rise in zeta and 2) the concentration gradient, defined as the change in zeta for an increase of one log unit in the concentration of the lectin in the range beyond the threshold concentration. This method offers a high degree of quantification and provides reliable information that can be meaningfully correlated with cell surface characteristics.

Agglutination↗
PubMed2006

The presence of jasmonate-inducible lectin genes in some but not all Nicotiana species explains a marked intragenus difference in plant responses to hormone treatment.

Tobacco (Nicotiana tabacum L. cv Samsun NN) leaves accumulate a cytoplasmic/nuclear lectin, called Nictaba, in response to methyl jasmonate. To check whether, and if so to what extent, the specific induction of this lectin applies to related species, a collection of 19 Nicotiana species--covering 12 Nicotiana sections and eight Nicotiana tabacum cultivars--was screened for their capability to synthesize the jasmonate-inducible lectin. Protein analyses by agglutination assays and western blot confirmed that only nine out of the 19 species examined synthesize lectin after jasmonate treatment. Remarkably, all allotetraploid cultivars of the N. tabacum L. species tested express the lectin after jasmonate treatment. PCR analyses demonstrated that all responsive species possess one or more lectin genes, whereas no lectin gene(s) could be traced in the non-responding species. The number of introns present in the lectin genes varies between zero and two. Four tobacco species/cultivars contain both intronless Nictaba genes as well as lectin genes with introns. These findings provide the first firm evidence for a striking intragenus difference with respect to the activation of a well-defined jasmonate-inducible gene that can be correlated with the presence/absence of orthologous genes in the genomes of closely related species from a single plant genus. In addition, the differential response of closely related tobacco species illustrates that in the field of plant hormone research, care must be taken when extrapolating results obtained with a particular model system to other--even taxonomically closely related--species.

Acetates↗