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Author (down) Traissac, S.; Pascal, J.-P. url  openurl
  Title Birth and life of tree aggregates in tropical forest: Hypotheses on population dynamics of an aggregated shade-tolerant species Type Journal Article
  Year 2014 Publication Journal of Vegetation Science Abbreviated Journal J. Veg. Sci.  
  Volume 25 Issue 2 Pages 491-502  
  Keywords Clusters; Colonization strategy; Janzen-Connell; Spatial analysis; Spatial pattern; Vouacapoua americana  
  Abstract Questions: Several studies have described aggregated spatial patterns in tropical tree species. This study investigates aggregate dynamics of Vouacapoua americana (Aublet), a climax species whose spatial pattern is not simply related to light and soil conditions or to its short seed dispersal range. Location: Two rain forest sites: Nouragues and Paracou, in the Guiana Shield. Methods: We described the spatial pattern of tree locations and spatial autocorrelation of tree diameters, using statistics derived from Ripley's K. We particularly used methods to define analysis subplots according to local density or local mean diameter. We investigated relationships between spatial distributions of adults and saplings. Results: At both sites, populations of Vouacapoua demonstrated several nested levels of aggregation. Tree diameters were spatially autocorrelated, revealing the existence of clusters with similar diameters. In the largest aggregates, tree diameters declined from the centre to the edge. Regeneration was aggregated and occurred mainly at cluster edges and around rare isolated trees, and sapling densities and basal area of adults were negatively correlated. We show that long-distance dispersal events are rare. Conclusions: Environmental factors and seed dispersal only explain part of the observed spatial patterns. We provide two main hypotheses about Vouacapoua population dynamics. First, the lack of regeneration in aggregate centres results in the ageing of existing aggregates. We suggest that this lack of recruitment close to mature trees is due to a Janzen-Connell effect. However, aggregates can continue to grow along colonization fronts. Second, long-distance dispersal events allow the formation of new clusters and play a crucial role in the colonization process. We investigate aggregate dynamics of Vouacapoua americana (Aublet) whose spatial pattern is not simply related to environmental conditions or to its seed dispersal. Regeneration does not occur in centers of aggregate of adults. We suggest that rare long-distance dispersal events and density-dependence predation of seeds and seedlings play a crucial role in formation of new clusters and structuration of larger aggregates. © 2013 International Association for Vegetation Science.  
  Address Université Claude Bernard Lyon 1, 43 Boulevard 11 Novembre 1918, Villeurbanne, 69100, France  
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  ISSN 11009233 (Issn) ISBN Medium  
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  Notes Export Date: 10 March 2014; Source: Scopus; Coden: Jvese; Language of Original Document: English; Correspondence Address: Traissac, S.; AgroParisTech, UMR ECOlogie des Forêts de Guyane, Campus Agronomique, BP 709, Kourou, 97387, France; email: stephane.traissac@ecofog.gf Approved no  
  Call Number EcoFoG @ webmaster @ Serial 532  
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Author (down) Touré, S.; Nirma, C.; Falkowski, M.; Dusfour, I.; Boulogne, I.; Jahn-Oyac, A.; Coke, M.; Azam, D.; Girod, R.; Moriou, C.; Odonne, G.; Stien, D.; Houel, E.; Eparvier, V. url  openurl
  Title Aedes aegypti Larvicidal Sesquiterpene Alkaloids from Maytenus oblongata Type Journal Article
  Year 2017 Publication Journal of Natural Products Abbreviated Journal Journal of Natural Products  
  Volume 80 Issue 2 Pages 384-390  
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  Abstract Four new sesquiterpene alkaloids (1-4) with a β-dihydroagrofuran skeleton and a new triterpenoid (5) were isolated from an ethyl acetate extract of Maytenus oblongata stems. Their structures were elucidated using 1D and 2D NMR spectroscopy as well as MS and ECD experiments. The M. oblongata stem EtOAc extract and the pure compounds isolated were tested for larvicidal activity against Aedes aegypti under laboratory conditions, and compounds 2 and 3 were found to be active. © 2017 The American Chemical Society and American Society of Pharmacognosy.  
  Address Laboratoire de Biodiversité et Biotechnologies Microbiennes (LBBM), Sorbonne Universités, UPMC Univ. Paris 06, CNRS, Observatoire Océanologique, Banyuls-sur-Mer, France  
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  Notes Export Date: 13 March 2017 Approved no  
  Call Number EcoFoG @ webmaster @ Serial 743  
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Author (down) Touchard, A.;Dejean, A.;Orivel, J. pdf  doi
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  Title Intraspecific variations in the venom peptidome of the ant Odontomachus haematodus (Formicidae: Ponerinae) from French Guiana Type Journal Article
  Year 2015 Publication Journal of Hymenoptera Research Abbreviated Journal Journal of Hymenoptera Research  
  Volume 47 Issue Pages 87-101  
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  Abstract Ant venoms are complex cocktails of toxins employed to subdue prey and to protect the colony from predators and microbial pathogens. Although the extent of ant venom peptide diversity remains largely unexplored, previous studies have revealed the presence of numerous bioactive peptides in most stinging ant venoms. We investigated the venom peptidome of the ponerine ant Odontomachus haematodus using LC-MS analysis and then verified whether the division of labor in the colonies and their geographical location are correlated with differences in venom composition. Our results reveal that O. haematodus venom is comprised of 105 small linear peptides. The venom composition does not vary between the different castes (i.e., nurses, foragers and queens), but an intraspecific variation in peptide content was observed, particularly when the colonies are separated by large distances. Geographical variation appears to increase the venom peptide repertoire of this ant species, demonstrating its intraspecific venom plasticity.  
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  Call Number EcoFoG @ webmaster @ Serial 643  
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Author (down) Touchard, A.; Labrière, N.; Roux, O.; Petitclerc, F.; Orivel, J.; Escoubas, P.; Koh, J.M.S.; Nicholson, G.M.; Dejean, A. url  openurl
  Title Venom toxicity and composition in three Pseudomyrmex ant species having different nesting modes Type Journal Article
  Year 2014 Publication Toxicon Abbreviated Journal Toxicon  
  Volume 88 Issue Pages 67-76  
  Keywords Ant venoms; Ants; Arboreal and ground-nesting ants; Evolution; Peptides; Pseudomyrmex; ant venom; acute toxicity; animal experiment; ant; article; biochemical composition; controlled study; disulfide bond; high performance liquid chromatography; lethality; matrix assisted laser desorption ionization time of flight mass spectrometry; molecular weight; myrmecophyte; nesting; nonhuman; predator prey interaction; priority journal; Pseudomyrmex gracilis; Pseudomyrmex penetrator; Pseudomyrmex termitarius; species diversity; toxin analysis  
  Abstract We aimed to determine whether the nesting habits of ants have influenced their venom toxicity and composition. We focused on the genus Pseudomyrmex (Pseudomyrmecinae) comprising terrestrial and arboreal species, and, among the latter, plant-ants that are obligate inhabitants of myrmecophytes (i.e., plants sheltering ants in hollow structures). Contrary to our hypothesis, the venom of the ground-dwelling species, Pseudomyrmex termitarius, was as efficacious in paralyzing prey as the venoms of the arboreal and the plant-ant species, Pseudomyrmexpenetrator and Pseudomyrmexgracilis. The lethal potency of P. termitarius venom was equipotent with that of P. gracilis whereas the venom of P. penetrator was less potent. The MALDI-TOF MS analysis of each HPLC fraction of the venoms showed that P. termitarius venom is composed of 87 linear peptides, while both P. gracilis and P. penetrator venoms (23 and 26 peptides, respectively) possess peptides with disulfide bonds. Furthermore, P. penetrator venom contains three hetero- and homodimeric peptides consisting of two short peptidic chains linked together by two interchain disulfide bonds. The large number of peptides in P. termitarius venom is likely related to the large diversity of potential prey plus the antibacterial peptides required for nesting in the ground. Whereas predation involves only the prey and predator, P. penetrator venom has evolved in an environment where trees, defoliating insects, browsing mammals and ants live in equilibrium, likely explaining the diversity of the peptide structures. © 2014 Elsevier Ltd. All rights reserved.  
  Address Laboratoire Écologie Fonctionnelle et Environnement, 118 Route de Narbonne, 31062 Toulouse, France  
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  Publisher Elsevier Ltd Place of Publication Editor  
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  ISSN 18793150 (Issn) ISBN Medium  
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  Notes Export Date: 30 July 2014; Coden: Toxia; Correspondence Address: Labrière, N.; CNRS, UMR Ecologie des Forêts de Guyane (EcoFoG), Campus Agronomique, BP 316, 97379 Kourou cedex, France Approved no  
  Call Number EcoFoG @ webmaster @ Serial 553  
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Author (down) Touchard, A.; Koh, J.M.S.; Aili, S.R.; Dejean, A.; Nicholson, G.M.; Orivel, J.; Escoubas, P. url  openurl
  Title The complexity and structural diversity of ant venom peptidomes is revealed by mass spectrometry profiling Type Journal Article
  Year 2015 Publication Rapid Communications in Mass Spectrometry Abbreviated Journal Rapid Communications in Mass Spectrometry  
  Volume 29 Issue 5 Pages 385-396  
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  Abstract Rationale Compared with other animal venoms, ant venoms remain little explored. Ants have evolved complex venoms to rapidly immobilize arthropod prey and to protect their colonies from predators and pathogens. Many ants have retained peptide-rich venoms that are similar to those of other arthropod groups. Methods With the goal of conducting a broad and comprehensive survey of ant venom peptide diversity, we investigated the peptide composition of venoms from 82 stinging ant species from nine subfamilies using matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOFMS). We also conducted an in-depth investigation of eight venoms using reversed-phase high-performance liquid chromatography (RP-HPLC) separation coupled with offline MALDI-TOFMS. Results Our results reveal that the peptide compositions of ant venom peptidomes from both poneroid and formicoid ant clades comprise hundreds of small peptides (<4 kDa), while large peptides (>4 kDa) are also present in the venom of formicoids. Chemical reduction revealed the presence of disulfide-linked peptides in most ant subfamilies, including peptides structured by one, two or three disulfide bonds as well as dimeric peptides reticulated by three disulfide bonds. Conclusions The biochemical complexity of ant venoms, associated with an enormous ecological and taxonomic diversity, suggests that stinging ant venoms constitute a promising source of bioactive molecules that could be exploited in the search for novel drug and biopesticide leads. Copyright © 2015 John Wiley & Sons, Ltd. Copyright © 2015 John Wiley & Sons, Ltd.  
  Address VenomeTech, 473 Route des DolinesValbonne, France  
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  Notes Export Date: 24 April 2015 Approved no  
  Call Number EcoFoG @ webmaster @ Serial 599  
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Author (down) Touchard, A.; Dauvois, M.; Arguel, M.-J.; Petitclerc, F.; Leblanc, M.; Dejean, A.; Orivel, J.; Nicholson, G.M.; Escoubas, P. url  openurl
  Title Elucidation of the unexplored biodiversity of ant venom peptidomes via MALDI-TOF mass spectrometry and its application for chemotaxonomy Type Journal Article
  Year 2014 Publication Journal of Proteomics Abbreviated Journal J. Proteomics  
  Volume 105 Issue Pages 217-231  
  Keywords Ant venom; Chemotaxonomy; Maldi-Tof Ms; Peptide; Peptidome; Ponerinae; ant venom; cytochrome c oxidase; ant; article; biodiversity; chemotaxonomy; correlational study; DNA sequence; French Guiana; Hymenoptera; matrix assisted laser desorption ionization time of flight mass spectrometry; mitochondrial gene; nonhuman; Odontomachus biumbonatus; Odontomachus haematodus; Odontomachus hastatus; Odontomachus mayi; Odontomachus scalptus; Pachcondyla apicalis; Pachcondyla arhuaca; Pachcondyla commutata; Pachcondyla constricta; Pachcondyla crassinola; Pachcondyla goeldii; Pachcondyla inversa; Pachcondyla marginata; Pachcondyla procidua; Pachcondyla stigma; Pachcondyla verenae; Pachcondyla villosa; peptidomics; phylogeny; priority journal; Animalia; Formicidae; Hymenoptera; Odontomachus; Pachycondyla; Pachycondyla apicalis; Pachycondyla stigma; Ponerinae  
  Abstract The rise of integrative taxonomy, a multi-criteria approach used in characterizing species, fosters the development of new tools facilitating species delimitation. Mass spectrometric (MS) analysis of venom peptides from venomous animals has previously been demonstrated to be a valid method for identifying species. Here we aimed to develop a rapid chemotaxonomic tool for identifying ants based on venom peptide mass fingerprinting. The study focused on the biodiversity of ponerine ants (Hymenoptera: Formicidae: Ponerinae) in French Guiana. Initial experiments optimized the use of automated matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) to determine variations in the mass profiles of ant venoms using several MALDI matrices and additives. Data were then analyzed via a hierarchical cluster analysis to classify the venoms of 17 ant species. In addition, phylogenetic relationships were assessed and were highly correlated with methods using DNA sequencing of the mitochondrial gene cytochrome c oxidase subunit 1. By combining a molecular genetics approach with this chemotaxonomic approach, we were able to improve the accuracy of the taxonomic findings to reveal cryptic ant species within species complexes. This chemotaxonomic tool can therefore contribute to more rapid species identification and more accurate taxonomies. Biological significance: This is the first extensive study concerning the peptide analysis of the venom of both Pachycondyla and Odontomachus ants. We studied the venoms of 17 ant species from French Guiana that permitted us to fine-tune the venom analysis of ponerine ants via MALDI-TOF mass spectrometry. We explored the peptidomes of crude ant venom and demonstrated that venom peptides can be used in the identification of ant species. In addition, the application of this novel chemotaxonomic method combined with a parallel genetic approach using COI sequencing permitted us to reveal the presence of cryptic ants within both the Pachycondyla apicalis and Pachycondyla stigma species complexes. This adds a new dimension to the search for means of exploiting the enormous biodiversity of venomous ants as a source for novel therapeutic drugs or biopesticides. This article is part of a Special Issue entitled: Proteomics of non-model organisms. © 2014 Elsevier B.V.  
  Address Neurotoxin Research Group, School of Medical and Molecular Biosciences, University of Technology, Sydney, NSW, Australia  
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  Publisher Elsevier Place of Publication Editor  
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  ISSN 18767737 (Issn) ISBN Medium  
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  Notes Cited By (since 1996):1; Export Date: 30 July 2014; Correspondence Address: Touchard, A.; UMR-EcoFoG, Campus Agronomique, BP 316, 97379 Kourou Cedex, France; email: axel.touchard@ecofog.gf; Chemicals/CAS: cytochrome c oxidase, 72841-18-0, 9001-16-5 Approved no  
  Call Number EcoFoG @ webmaster @ Serial 555  
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Author (down) Touchard, A.; Brust, A.; Cardoso, F.C.; Chin, Y.K.-Y.; Herzig, V.; Jin, A.-H.; Dejean, A.; Alewood, P.F.; King, G.F.; Orivel, J.; Escoubas, P. url  doi
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  Title Isolation and characterization of a structurally unique β-hairpin venom peptide from the predatory ant Anochetus emarginatus Type Journal Article
  Year 2016 Publication Biochimica et Biophysica Acta – General Subjects Abbreviated Journal Biochimica et Biophysica Acta – General Subjects  
  Volume 1860 Issue 11 Pages 2553-2562  
  Keywords Anochetus; Ant venom; Disulfide-rich peptides; L-type calcium channels; Neurotoxin; Poneritoxins; U1-PONTX-Ae1a  
  Abstract Background Most ant venoms consist predominantly of small linear peptides, although some contain disulfide-linked peptides as minor components. However, in striking contrast to other ant species, some Anochetus venoms are composed primarily of disulfide-rich peptides. In this study, we investigated the venom of the ant Anochetus emarginatus with the aim of exploring these novel disulfide-rich peptides. Methods The venom peptidome was initially investigated using a combination of reversed-phase HPLC and mass spectrometry, then the amino acid sequences of the major peptides were determined using a combination of Edman degradation and de novo MS/MS sequencing. We focused on one of these peptides, U1-PONTX-Ae1a (Ae1a), because of its novel sequence, which we predicted would form a novel 3D fold. Ae1a was chemically synthesized using Fmoc chemistry and its 3D structure was elucidated using NMR spectroscopy. The peptide was then tested for insecticidal activity and its effect on a range of human ion channels. Results Seven peptides named poneritoxins (PONTXs) were isolated and sequenced. The three-dimensional structure of synthetic Ae1a revealed a novel, compact scaffold in which a C-terminal β-hairpin is connected to the N-terminal region via two disulfide bonds. Synthetic Ae1a reversibly paralyzed blowflies and inhibited human L-type voltage-gated calcium channels (CaV1). Conclusions Poneritoxins from Anochetus emarginatus venom are a novel class of toxins that are structurally unique among animal venoms. General significance This study demonstrates that Anochetus ant venoms are a rich source of novel ion channel modulating peptides, some of which might be useful leads for the development of biopesticides. © 2016  
  Address VenomeTech, 473 Route des Dolines, Valbonne, France  
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  Notes Export Date: 15 September 2016 Approved no  
  Call Number EcoFoG @ webmaster @ Serial 694  
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Author (down) Touchard, A.; Aili, S.R.; Téné, N.; Barassé, V.; Klopp, C.; Dejean, A.; Kini, R.M.; Mrinalini; Coquet, L.; Jouenne, T.; Lefranc, B.; Leprince, J.; Escoubas, P.; Nicholson, G.M.; Treilhou, M.; Bonnafé, E. url  doi
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  Title Venom Peptide Repertoire of the European Myrmicine Ant Manica rubida: Identification of Insecticidal Toxins Type Journal Article
  Year 2020 Publication Journal of proteome research Abbreviated Journal J. Proteome Res.  
  Volume 19 Issue 4 Pages 1800-1811  
  Keywords glycosylated toxin; peptidome; polycationic α-helix; predation; pyroglutamate; reversible neurotoxicity  
  Abstract Using an integrated transcriptomic and proteomic approach, we characterized the venom peptidome of the European red ant, Manica rubida. We identified 13 “myrmicitoxins” that share sequence similarities with previously identified ant venom peptides, one of them being identified as an EGF-like toxin likely resulting from a threonine residue modified by O-fucosylation. Furthermore, we conducted insecticidal assays of reversed-phase HPLC venom fractions on the blowfly Lucilia caesar, permitting us to identify six myrmicitoxins (i.e., U3-, U10-, U13-, U20-MYRTX-Mri1a, U10-MYRTX-Mri1b, and U10-MYRTX-Mri1c) with an insecticidal activity. Chemically synthesized U10-MYRTX-Mri1a, -Mri1b, -Mri1c, and U20-MYRTX-Mri1a irreversibly paralyzed blowflies at the highest doses tested (30-125 nmol·g-1). U13-MYRTX-Mri1a, the most potent neurotoxic peptide at 1 h, had reversible effects after 24 h (150 nmol·g-1). Finally, U3-MYRTX-Mri1a has no insecticidal activity, even at up to 55 nmol·g-1. Thus, M. rubida employs a paralytic venom rich in linear insecticidal peptides, which likely act by disrupting cell membranes.  
  Address VenomeTech, 473 Route des Dolines – Villa 3, Valbonne, 06560, France  
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  Publisher NLM (Medline) Place of Publication Editor  
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  ISSN 15353907 (Issn) ISBN Medium  
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  Notes Export Date: 20 April 2020 Approved no  
  Call Number EcoFoG @ webmaster @ Serial 927  
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Author (down) Touchard, A.; Aili, S.R.; Fox, E.G.P.; Escoubas, P.; Orivel, J.; Nicholson, G.M.; Dejean, A. pdf  url
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  Title The biochemical toxin arsenal from ant venoms Type Journal Article
  Year 2016 Publication Toxins Abbreviated Journal Toxins  
  Volume 8 Issue 1 Pages 30  
  Keywords Alkaloids; Ant venom; Enzymes; Formic acid; Peptides; Toxins; Venom biochemistry  
  Abstract Ants (Formicidae) represent a taxonomically diverse group of hymenopterans with over 13,000 extant species, the majority of which inject or spray secretions from a venom gland. The evolutionary success of ants is mostly due to their unique eusociality that has permitted them to develop complex collaborative strategies, partly involving their venom secretions, to defend their nest against predators, microbial pathogens, ant competitors, and to hunt prey. Activities of ant venom include paralytic, cytolytic, haemolytic, allergenic, pro-inflammatory, insecticidal, antimicrobial, and pain-producing pharmacologic activities, while non-toxic functions include roles in chemical communication involving trail and sex pheromones, deterrents, and aggregators. While these diverse activities in ant venoms have until now been largely understudied due to the small venom yield from ants, modern analytical and venomic techniques are beginning to reveal the diversity of toxin structure and function. As such, ant venoms are distinct from other venomous animals, not only rich in linear, dimeric and disulfide-bonded peptides and bioactive proteins, but also other volatile and non-volatile compounds such as alkaloids and hydrocarbons. The present review details the unique structures and pharmacologies of known ant venom proteinaceous and alkaloidal toxins and their potential as a source of novel bioinsecticides and therapeutic agents. © 2016 by the authors; licensee MDPI, Basel, Switzerland.  
  Address Laboratoire Écologie Fonctionnelle et Environnement, 118 Route de Narbonne, Toulouse, France  
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  Notes Export Date: 8 February 2016 Approved no  
  Call Number EcoFoG @ webmaster @ Serial 656  
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Author (down) Torroba-Balmori, P.; Budde, K.B.; Heer, K.; González-Martínez, S.C.; Olsson, S.; Scotti-Saintagne, C.; Casalis, M.; Sonké, B.; Dick, C.W.; Heuertz, M. url  doi
openurl 
  Title Altitudinal gradients, biogeographic history and microhabitat adaptation affect fine-scale spatial genetic structure in African and Neotropical populations of an ancient tropical tree species Type Journal Article
  Year 2017 Publication PLoS ONE Abbreviated Journal PLoS ONE  
  Volume 12 Issue 8 Pages e0182515  
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  Abstract The analysis of fine-scale spatial genetic structure (FSGS) within populations can provide insights into eco-evolutionary processes. Restricted dispersal and locally occurring genetic drift are the primary causes for FSGS at equilibrium, as described in the isolation by distance (IBD) model. Beyond IBD expectations, spatial, environmental or historical factors can affect FSGS. We examined FSGS in seven African and Neotropical populations of the late-successional rain forest tree Symphonia globulifera L. f. (Clusiaceae) to discriminate the influence of drift-dispersal vs. landscape/ecological features and historical processes on FSGS. We used spatial principal component analysis and Bayesian clustering to assess spatial genetic heterogeneity at SSRs and examined its association with plastid DNA and habitat features. African populations (from Cameroon and São Tomé) displayed a stronger FSGS than Neotropical populations at both marker types (mean Sp = 0.025 vs. Sp = 0.008 at SSRs) and had a stronger spatial genetic heterogeneity. All three African populations occurred in pronounced altitudinal gradients, possibly restricting animal-mediated seed dispersal. Cyto-nuclear disequilibria in Cameroonian populations also suggested a legacy of biogeographic history to explain these genetic patterns. Conversely, Neotropical populations exhibited a weaker FSGS, which may reflect more efficient wide-ranging seed dispersal by Neotropical bats and other dispersers. The population from French Guiana displayed an association of plastid haplotypes with two morphotypes characterized by differential habitat preferences. Our results highlight the importance of the microenvironment for eco-evolutionary processes within persistent tropical tree populations. © 2017 Torroba-Balmori et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.  
  Address Smithsonian Tropical Research Institute, Panama  
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  Notes Export Date: 2 September 2017 Approved no  
  Call Number EcoFoG @ webmaster @ Serial 762  
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