1,721,462 research outputs found
Generation of neutralizing antibodies to <i>Bm</i>-TPI.
No full text<p><b>A</b>. TPI enzyme activity in presence of 10% serum from jirds infected for 21 weeks with <i>B. malayi</i> following immunisation with BSA or <i>Bm</i>-TPI. * p<0.05 by <i>t</i>-test. <b>B</b>. TPI enzyme activity in presence of 10% polyclonal anti-<i>Bm</i>-TPI serum from BALB/c mice or naive mouse serum (nms). <b>C</b>. TPI enzyme activity in presence of 10% serum from human filariasis patients. Serum was used from the 5 strongest anti-<i>Bm</i>-TPI reactors (black circles) or 5 non-reactors (white circles) from each group (<a href="http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003930#ppat-1003930-g003" target="_blank">Fig. 3</a>). <b>D</b>. Generation of antibody specificities that neutralise <i>Bm</i>-TPI activity is a relatively rare event. Ability of a panel of murine mAb specific for <i>Bm</i>-TPI (data not shown) to inhibit enzyme activity was determined. Clones with neutralising capacity are shown in red. <b>E</b>. Specificity of neutralizing mAb 1.11.1 for <i>Bm</i>-TPI (black bars) and not rabbit TPI (white bars). <b>F</b>. Specificity of neutralizing mAb 1.11.1 for <i>Bm</i>-TPI (black bars) and not <i>Ls</i>-TPI (grey bars). A, B, E and F are representative of multiple batches of recombinant enzyme. <b>G</b>. Neutralisation of native <i>Bm</i>-TPI activity in BES (4 independent batches) by mAb 1.11.1. MOPC31C IgG1 myeloma protein was used as a control. Dotted lines in (A–D) represent enzyme activity in the absence of serum or antibody (normalised to 100%).*** p<0.001 by <i>t</i>-test.</p
Adult worms preferentially secrete enzymatically active <i>Bm</i>-TPI.
No full text<p><b>A</b>. Western blot for <i>Bm</i>-TPI of 1 mg parasite extract (somatic extacts of L3 (L3A), Mf (MfA) and adult (BmA) or three independent batches of adult BES. Recombinant <i>Bm</i>-TPI included as a positive control. <b>B</b>. TPI activity in multiple independent batches of native BES or heat-denatured (hd)–BES. ** p<0.01 by <i>t</i>-test. <b>C</b>. Immunofluorescence of adult <i>B. malayi</i> female with polyclonal mouse anti-<i>Bm</i>-TPI (left panels) and control normal mouse serum (right panels) applied to longitudinal (Upper panels) and transverse (lower panels) sections. Scale bar represents 100 mm.</p
Inhibition curve of displayed <i>Bm</i>AChE.
No full text<p>(A), inhibition curve of displayed <i>Bm</i>AChE for eserine; (B), inhibition curve of displayed <i>Bm</i>AChE for CB pesticide (n = 3); and (C), inhibition curve of displayed <i>Bm</i>AChE for OP pesticides (n = 3). B, the average absorbance at the indicated concentrations; B<sub>0</sub>, the average absorbance at zero concentration. The data were fitted with a four-parameter-logistic equation to calculate the IC<sub>50</sub> using OriginPro 7.5 software. The data points are mean values and the errors observed from triplicate determinations.</p
Mutagenesis of the <i>Bm-re</i> gene.
No full text<p>Embryos were photographed five days after <i>Bm-re</i> TALEN microinjection. (A) not injected control, (B) <i>Bm-re</i> mutant, (C, D) embryos injected with buffer, (E-H) G<sub>0</sub> embryos injected with TALEN mRNA.</p
Vaccination with <i>Bm</i>-TPI does not curtail infection.
No full text<p><b>A</b>. Immunisation induces high titers of week 8 post-challenge anti-<i>Bm</i>-TPI IgG1 antibodies in vaccinated jirds, compared to animals immunised with BSA control. <b>B</b>. Week 8 post-challenge adult <i>B. malayi</i> worm burdens in <i>Bm-T</i>PI and BSA vaccinated jirds. <b>C</b>. Anti-<i>Bm</i>-TPI IgG1 titers remain high by week 21 post-challenge in vaccinated jirds, compared to BSA control animals. <b>D</b>. Week 21 post-challenge adult <i>B. malayi</i> worm burdens in <i>Bm-T</i>PI and BSA vaccinated jirds. <b>E</b>. Peritoneal <i>B. malayi</i> microfilarial counts in jirds at week 21 post-infection previously vaccinated with BSA or <i>Bm</i>-TPI. <b>F</b>. Immunisation induces high titers of day 70 post-challenge anti-<i>Ls</i>-TPI IgG1 antibodies in vaccinated BALB/c mice, compared to animals immunised with BSA control. <b>G</b>. Day 70 post-challenge adult <i>L. sigmodontis</i> worm burdens in <i>Ls-T</i>PI and BSA vaccinated BALB/c mice. <b>H</b>. Day 70 post-challenge blood <i>L. sigmodontis</i> microfilarial counts in <i>Ls-T</i>PI and BSA vaccinated BALB/c mice. Dotted lines in A, C and F represent background antibody titers naïve jird or mouse sera. n.s. non-significant, ** p>0.01, *** p>0.001, **** p>0.0001, by <i>t</i>-test.</p
Treatment of adult female <i>B. malayi</i> with <i>Bm-cpl-1</i>, <i>Bm-cpl-5</i>, and <i>Bm-cpz</i> dsRNAs leads to phenotypic changes in developing embryos.
No full text<p>Intrauterine progeny from individual female worms were examined 2 d after treatment with medium control (A), <i>Ov-cpz-Int2</i> control dsRNA (B), <i>Bm-cpl-5</i> dsRNA (C) and <i>Bm-cpl Pro</i> dsRNA (D).</p
Going Beyond Counting First Authors in Author Co-citation Analysis
Get PDFThe present study examines one of the fundamental aspects of author co-citation analysis (ACA) - the way co-citation
counts are defined. Co-citation counting provides the data on which all subsequent statistical analyses and mappings
are based, and we compare ACA results based on two different types of co-citation counting - the traditional type that
only counts the first one among a cited work's authors on the one hand and a non-traditional type that takes into
account the first 5 authors of a cited work on the other hand. Results indicate that the picture produced through this non-traditional author co-citation counting contains more coherent author groups and is therefore considerably clearer. However, this picture represents fewer specialties in the research field being studied than that produced through the traditional first-author co-citation counting when the same number of top-ranked authors is selected and analyzed. Reasons for these effects are discussed
Purification of <i>Bm</i>K-YA from Fraction 17.
No full text<p>(A) Chromatographic profile of F17 separated by Click Maltose column using HILIC mode. The mobile phase was composed of water (A), ACN (B) and 100 mM TEAP buffer (pH 2.3) (C). The gradient was from 10% A to 45% A over 40 min, then from 45% A to 50% A over 20 min under a constant 5% C. (B) RPLC analysis and comparison of the purified natural <i>Bm</i>K-YA and the synthetic one. The mobile phase B (ACN with 0.1%TFA) was from 5% to 35% in 25 min on a Xterra MS C18 column at a flow rate of 0.2 mL/min. Absorbance was measured at 220 nm. (C) Q-TOF mass spectra of the natural <i>Bm</i>K-YA with a [M+H]<sup>+</sup> monoisotopic mass of 871.3088. (D) Single charged and deconvoluted (MaxEnt3 processed spectra) CID spectra and amino acid sequence of <i>Bm</i>K-YA.</p
Stage specific expression of <i>w</i>Bm-MurA gene and the enzyme.
No full text<p><b>A:</b> Expression of <i>w</i>Bm-MurA gene. The full-length DNA (1278 bp, <i>w</i>Bm-MurA gene) was amplified from the cDNA of three life- stages of <i>B. malayi</i> using gene specific primers. Lane 1, molecular size markers (GeneRuler 1 kb DNA Ladder, Thermo Scientific); lane 2, infective larvae; lane 3, adults (both sexes); lane 4, microfilariae. Lane 5, 6 and 7 are controls containing PCR products from infective larvae, adults and microfilariae respectively in absence of reverse transcriptase. <b>B:</b> Endogenous protein (<i>w</i>Bm-MurA) expression. Western blot was performed with anti-<i>w</i>Bm-MurA antibody to confirm the presence of <i>w</i>Bm-MurA. Lane 1, molecular mass markers (Puregene 4 Color Prestain protein ladder, Genetix); lane 2, microfilariae; lane 3, infective larvae; lane 4, adult worms (both sexes); and lane 5, purified <i>w</i>Bm-MurA protein (positive control).</p
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