19 research outputs found

    Liana Abundance, Diversity, and Distribution on Barro Colorado Island, Panama

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    Lianas are a key component of tropical forests; however, most surveys are too small to accurately quantify liana community composition, diversity, abundance, and spatial distribution – critical components for measuring the contribution of lianas to forest processes. In 2007, we tagged, mapped, measured the diameter, and identified all lianas ≥1 cm rooted in a 50-ha plot on Barro Colorado Island, Panama (BCI). We calculated liana density, basal area, and species richness for both independently rooted lianas and all rooted liana stems (genets plus clones). We compared spatial aggregation patterns of liana and tree species, and among liana species that varied in the amount of clonal reproduction. We also tested whether liana and tree densities have increased on BCI compared to surveys conducted 30-years earlier. This study represents the most comprehensive spatially contiguous sampling of lianas ever conducted and, over the 50 ha area, we found 67,447 rooted liana stems comprising 162 species. Rooted lianas composed nearly 25% of the woody stems (trees and lianas), 35% of woody species richness, and 3% of woody basal area. Lianas were spatially aggregated within the 50-ha plot and the liana species with the highest proportion of clonal stems more spatially aggregated than the least clonal species, possibly indicating clonal stem recruitment following canopy disturbance. Over the past 30 years, liana density increased by 75% for stems ≥1 cm diameter and nearly 140% for stems ≥5 cm diameter, while tree density on BCI decreased 11.5%; a finding consistent with other neotropical forests. Our data confirm that lianas contribute substantially to tropical forest stem density and diversity, they have highly clumped distributions that appear to be driven by clonal stem recruitment into treefall gaps, and they are increasing relative to trees, thus indicating that lianas will play a greater role in the future dynamics of BCI and other neotropical forests

    A neurophysiological interpretation of the respiratory act

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    Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/47945/1/10254_2005_Article_BF02320667.pd

    Expression of functional protease and subviral particles by vaccinia virus containing equine infectious anaemia virus \u3ci\u3egag\u3c/i\u3e and 5\u27 \u3ci\u3epol\u3c/i\u3e genes

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    Cells infected with vaccinia viruses expressing the equine infectious anaemia virus (EIAV) gag gene (VGag) or gag plus the 5\u27 pol encoding protease (VGag/PR) were evaluated with monoclonal antibody to a p26 capsid protein linear epitope (QEISKFLTD). Both recombinant viruses expressed Gag precursor protein (55K) whereas only VGag/PR expressed a detectable Gag-Pol fusion protein (82K) with a functional protease, shown by subviral particles containing processed p26. Horses inoculated with VGag/PR produced antibodies reactive with EIAV Gag proteins

    Major Histocompatibility Complex-Restricted CD8\u3csup\u3e+\u3c/sup\u3e Cytotoxic T Lymphocytes from Horses with Equine Infectious Anemia Virus Recognize Env and Gag/PR Proteins

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    Cytotoxic T lymphocytes (CTL) can control some viral infections and may be important in the control of lentiviruses, including human immunodeficiency virus type 1. Since there is limited evidence for an in vivo role of CTL in control of lentiviruses, dissection of immune mechanisms in animal lentiviral infections may provide needed information. Horses infected with equine infectious anemia virus (EIAV), a lentivirus, have acute plasma viremia which is terminated in immunocompetent horses. Viremic episodes may recur, but most horses ultimately control infection and become asymptomatic carriers. To begin dissection of the immune mechanisms involved in EIAV control, peripheral blood mononuclear cells (PBMC) from infected horses were evaluated for CTL to EIAV-infected cells. By using noninfected and EIAV-infected autologous equine kidney (EK) cells in Cr-release assays, EIAV-specific cytotoxic activity was detected in unstimulated PBMC from three infected horses. The EIAV-specific cytotoxic activity was major histocompatibility complex (MHC) restricted, as determined by assaying EIAV-infected heterologous EK targets, and was mediated by CD8+ T lymphocytes, as determined by depleting these cells by a panning procedure with an anti-CD8 monoclonal antibody. MHC-restricted CD8+ CTL in unstimulated PBMC from infected horses caused significant specific lysis of autologous EK cells infected with recombinant vaccinia viruses expressing EIAV genes, either env or gag plus 5\u27 pol. The EIAV-specific MHC-restricted CD8+ CTL were detected in two EIAV-infected horses within a few days after plasma viremia occurred and were present after viremia was terminated. The detection of these immune effector cells in EIAV-infected horses permits further studies to determine their in vivo role

    Transmembrane protein oligomers of caprine arthritis-encephalitis lentivirus are immunodominant in goats with progressive arthritis

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    To dissect mechanisms of caprine arthritis-encephalitis lentivirus-induced arthritis, an undefined immunodominant viral glycoprotein, gp90 (G. C. Johnson, A. F. Barbet, P. Klevjer-Anderson, and T. C. McGuire, Infect. Immun. 41:657-665, 1983), was characterized. Monoclonal antibody to gp90 and specific antiserum to env gene products demonstrated that gp90 was a transmembrane protein (TM) dimer. Goats with progressive arthritis had high antibody titers to oligomeric and monomeric (38-kDa) TM

    Identification of Anaplasma marginale long-term carrier cattle by detection of serum antibody to isolated MSP-3

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    Rapid and accurate detection of Anaplasma marginale-infected cattle would enhance anaplasmosis control procedures and evaluation of vaccines. Current tests based on detection of antibodies in serum are not widely used for several reasons, including the occurrence of either false-positive or false-negative results. We evaluated binding of antibodies in serum to a subunit antigen isolated from A. marginale initial bodies--major surface protein 3 (MSP-3). MSP-3 was detected in lysates of eight geographically different isolates of A. marginale and purified by affinity chromatography with monoclonal antibody AmG75C2. Antibodies from cattle infected with any of five geographically different isolates of A. marginale reacted in immunoblots with MSP-3. Sera from uninfected cattle and cattle infected with another rickettsial organism and two hemoprotozoal organisms failed to react with MSP-3. Six carrier cattle infected with the Florida isolate of A. marginale had antibody titers to MSP-3 ranging from 10(3) to 10(6) during a 5-year evaluation period. Since specific antibodies to isolated MSP-3 persist in high titers in long-term carrier cattle sera and MSP-3 is common among A. marginale isolates, it is recommended as a subunit antigen for an anaplasmosis test

    Structure and genetic variability of envelope glycoproteins of two antigenic variants of caprine arthritis-encephalitis lentivirus

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    To define the structure of the caprine arthritis-encephalitis virus (CAEV) env gene and characterize genetic changes which occur during antigenic variation, we sequenced the env genes of CAEV-63 and CAEV-Co, two antigenic variants of CAEV defined by serum neutralization. The deduced primary translation product of the CAEV env gene consists of a 60- to 80-amino-acid signal peptide followed by an amino-terminal surface protein (SU) and a carboxy-terminal transmembrane protein (TM) separated by an Arg-Lys-Lys-Arg cleavage site. The signal peptide cleavage site was verified by amino-terminal amino acid sequencing of native CAEV-63 SU. In addition, immunoprecipitation of [35S]methionine-labeled CAEV-63 proteins by sera from goats immunized with recombinant vaccinia virus expressing the CAEV-63 env gene confirmed that antibodies induced by env-encoded recombinant proteins react specifically with native virion SU and TM. The env genes of CAEV-63 and CAEV-Co encode 28 conserved cysteines and 25 conserved potential N-linked glycosylation sites. Nucleotide sequence variability results in 62 amino acid changes and one deletion within the SU and 34 amino acid changes within the TM
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