<?xml version="1.0" encoding="UTF-8"?>
<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns="http://purl.org/rss/1.0/" xmlns:taxo="http://purl.org/rss/1.0/modules/taxonomy/" xmlns:sy="http://purl.org/rss/1.0/modules/syndication/" xmlns:dc="http://purl.org/dc/elements/1.1/">
  <channel>
    <title>NISCAIR Online Periodicals Repository Collection: IJBB Vol.44(5) [October 2007]</title>
    <link>http://nopr.niscair.res.in/handle/123456789/74</link>
    <description />
    <items>
      <rdf:Seq>
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/142" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/141" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/140" />
        <rdf:li resource="http://nopr.niscair.res.in/handle/123456789/139" />
      </rdf:Seq>
    </items>
  </channel>
  <textInput>
    <title>The Collection's search engine</title>
    <description>Search the Channel</description>
    <name>search</name>
    <link>http://nopr.niscair.res.in/simple-search</link>
  </textInput>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/142">
    <title>Role of virulence plasmid of Aeromonas hydrophila in the pathogenesis of ulcerative disease syndrome in Clarias batrachus</title>
    <link>http://nopr.niscair.res.in/handle/123456789/142</link>
    <description>Title: Role of virulence plasmid of Aeromonas hydrophila in the pathogenesis of ulcerative disease syndrome in Clarias batrachus
&lt;br/&gt;
&lt;br/&gt;Authors: Majumdar, T; Datta, S; Ghosh, D; Dutta, S; Chakraborty, A; Goswami, R; Mazumder, S
&lt;br/&gt;
&lt;br/&gt;Abstract: Pathogenic Aeromonas hydrophila (strain VB21), a multiple-drug resistance strain contains a plasmid of about 21 kb. After curing of plasmid, the isolates became sensitive to antimicrobials, to which they were earlier resistant. The cured bacteria exhibited significant alterations in their surface structure, growth profile and virulence properties, and failed to cause ulcerative disease syndrome (UDS) when injected into the Indian catfish Clarias batrachus. Routine biochemical studies revealed that the plasmid curing did not alter the biochemical properties of the bacteria. After transformation of the plasmid into cured A. hydrophila the bacterium regained its virulence properties and induced all the characteristic symptoms of UDS when injected into fish. Thus, the plasmid plays a pivotal role in the phenotype, growth and virulence of &#xD;
A. hydrophila and pathogenesis of aeromonad UDS.
&lt;br/&gt;
&lt;br/&gt;Page(s): 401-406</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/141">
    <title>Correlation of circulatory immunoglobulin levels with Mu opiate receptor allele</title>
    <link>http://nopr.niscair.res.in/handle/123456789/141</link>
    <description>Title: Correlation of circulatory immunoglobulin levels with Mu opiate receptor allele
&lt;br/&gt;
&lt;br/&gt;Authors: Sharad, Shashwat; Gupta, A K; Singh, R A; Kapoor, Manav; Kapur, Suman
&lt;br/&gt;
&lt;br/&gt;Abstract: Opiates are known to induce immunosuppression in their users (addicts). Evidences supporting their role in suppressing a variety of immunological end points in addicts have been reported by several investigators. In the present study, we investigated the changes in serum immunoglobulin (Ig) levels and their correlation with Mu opiate receptor (MOR) genotypes. Eighty-seven users and forty-five non-users were recruited for the study. Genomic DNA, isolated from the peripheral blood, was used for genotyping for C17T and A118G polymorphism using PCR-RFLP method. The frequency of A and G alleles in non-users was 89% and 11% respectively, whereas in addicts, it was 67% and 33% respectively. Case control analysis between groups revealed that 118G allele was associated with opioid dependence [Chi square (X²) = 13.56, odds ratio (OR) = 3.90, confidence interval₉₅﹪ (CI₉₅﹪) = 1.80-8.67, p = 0.000231]. C17T polymorphism showed no association with opioid dependence [(X²) = 0.9, O R = 2.49, CI₉₅﹪ = 0.528-16.12, p = 0.343]. Mean Ig levels, both IgG (student’s t-test = 2.2738, p = 0.007) and IgA (student’s t-test = 2.848, p = 0.0051) differed between opiate users and non-users. IgG and IgA levels were also significantly different in individuals with different MOR genotypes. Immunosuppression was observed in AA genotype-bearing individuals, while no suppression was seen in AG and GG genotypes bearing individuals. In case of C17T polymorphism, both CC and CT genotypes bearing individuals showed immunosuppression, as judged by circulating Ig levels.
&lt;br/&gt;
&lt;br/&gt;Page(s): 394-400</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/140">
    <title>Liposomal delivery of Mycobacterium leprae antigen(s) with murabutide and Trat peptide inhibits Fas-mediated apoptosis of peripheral blood mononuclear cells derived from leprosy patients</title>
    <link>http://nopr.niscair.res.in/handle/123456789/140</link>
    <description>Title: Liposomal delivery of Mycobacterium leprae antigen(s) with murabutide and Trat peptide inhibits Fas-mediated apoptosis of peripheral blood mononuclear cells derived from leprosy patients
&lt;br/&gt;
&lt;br/&gt;Authors: Chattree, Vineeta; Khanna, Neena; Bisht, Vandana; Rao, D N
&lt;br/&gt;
&lt;br/&gt;Abstract: Protective immunity against intracellular pathogen Mycobacterium leprae is dependent on the activation of T cells. Repeated stimulation of T cells by M. leprae antigens MLCwA (M. leprae total cell wall antigen) and ManLAM (mannose capped lipoarabinomannan) may lead to apoptosis in leprosy patients. In the present study, inhibition of the Fas-induced apoptosis of peripheral blood mononuclear cells of leprosy patients was investigated using above M. leprae antigen(s), in combination with immunomodulators murabutide (MB) and a Trat peptide in particulate form (liposome). Incubation of the cells with particulate mode of antigen presentation led to both decreased percentage of propidium iodide (PI) positive cells and T cells expressing Fas-FasL, as well as decreased caspase-8/-3 activities in the lepromatous patients, thereby inhibiting apoptosis, while converse was true with stimulation with soluble antigen. Concurrently, there was an upregulation of anti-apoptotic protein Bcl-Xʟ in the lepromatous patients, thereby inhibiting apoptosis. Thus, the liposomal formulation of antigen promoted proliferation of anergized T cell by inhibiting apoptosis through decreased expression of death receptors and caspase activities and increased expression of anti-apoptotic protein Bcl-Xʟ in these patients.
&lt;br/&gt;
&lt;br/&gt;Page(s): 386-393</description>
  </item>
  <item rdf:about="http://nopr.niscair.res.in/handle/123456789/139">
    <title>Partial purification and characterization of acetylcholinesterase isozymes from adult bovine filarial parasite Setaria cervi</title>
    <link>http://nopr.niscair.res.in/handle/123456789/139</link>
    <description>Title: Partial purification and characterization of acetylcholinesterase isozymes from adult bovine filarial parasite Setaria cervi
&lt;br/&gt;
&lt;br/&gt;Authors: Singh, Shravan K; Kaushal, Deep C; Murthy, P Kalpana; Kaushal, Nuzhat A
&lt;br/&gt;
&lt;br/&gt;Abstract: Filariasis is a major health problem, affecting millions of people in tropical and sub-tropical regions of the world. The isolation and characterization of parasite-specific enzyme targets is essential for developing effective control measures against filariasis. Acetylcholinesterase (AchE, E.C. 3.1.1.7), an important enzyme of neuromuscular transmission is found in a number of helminths including filarial parasites and may be playing a role in host-parasite interactions. Earlier, we demonstrated the presence of two isozymes of AchE, different from the host enzyme in the human (Brugia malayi) and bovine (Setaria cervi) filarial parasites. In the present study, two isozymes of AchE (pAchE1 and pAchE2) were isolated from S. cervi adults and characterized biochemically and immunochemically. The AchE was partially purified on Con-A Sepharose column and then subjected to preparative polyacrylamide gel electrophoresis (PAGE) for separation of the isozymes. The AchE activity was localized by the staining of gel and the isozymes were isolated from the PAGE strips by electroelution. Both isozymes preferentially utilized acetylcholine iodide as substrate and were strongly inhibited by the true AchE inhibitor (BW284c51), suggesting that they were true AchE. The polyclonal antibodies produced against the isozymes showed significant cross-reactivity with B. malayi AchE, but not against the host enzyme. These findings suggested that both the isozymes were biochemically (in terms of their substrate specificity and inhibitor sensitivity) and immunochemically similar, but different from the host enzyme.
&lt;br/&gt;
&lt;br/&gt;Page(s): 379-385</description>
  </item>
</rdf:RDF>

