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1.
Public Health ; 148: 56-62, 2017 Jul.
Article in English | MEDLINE | ID: mdl-28404534

ABSTRACT

OBJECTIVE: There is scarcity of information on the prevalence of female genital tuberculosis (FGTB) in the community. The present study was carried out to estimate the prevalence of FGTB, its risk factors and associated clinical features. STUDY DESIGN: Community-based cross-sectional survey. METHODS: This study was carried during October 2011 and May 2014 in the Andaman Islands. A total of 13,300 women aged 20-59 years were primarily screened using a structured questionnaire. About 721 (5.4%) were found initially eligible for screening for genital tuberculosis by clinical examination and specimen collection for laboratory tests but only 460 (63.8%) expressed their willingness. Endometrial specimens were collected from 405 (88%) subjects. The association of the potential risk factors with genital tuberculosis was tested by Chi-squared test. A similar analysis was performed to identify clinical features associated with genital tuberculosis. RESULTS: The estimated prevalence of FGTB was 45.1 cases per 100,000 women (95% confidence interval [CI]: 16.6-98.1). Infertility and oligomenorrhoea were identified as clinical features associated with FGTB. Past history of tuberculosis and history of close contact with tuberculosis cases were identified as risk factors. CONCLUSIONS: This study shows the prevalence of FGTB among the female population of the Andaman Islands. Though the estimated prevalence was close to the expected prevalence, but as only 63.8% of the eligible women could be adequately screened, a much higher prevalence of FGTB could not be ruled out. Infertility, oligomenorrhoea, past history of tuberculosis and contact with tuberculosis case were identified as factors associated with genital tuberculosis.


Subject(s)
Tuberculosis, Female Genital/epidemiology , Adult , Cross-Sectional Studies , Female , Humans , India/epidemiology , Infertility, Female/epidemiology , Middle Aged , Oligomenorrhea/epidemiology , Prevalence , Risk Factors , Young Adult
2.
Drug Res (Stuttg) ; 66(8): 427-31, 2016 Aug.
Article in English | MEDLINE | ID: mdl-27281447

ABSTRACT

The genus Iris is diverse both in the abundance of secondary metabolities as well as the biological activities. The rhizomes of Iris hookeriana exhibit significant anthelminthic activity against gastrointestinal nematodes of sheep. Although Iris hookeriana has been a subject of the study of so many phytochemical studies, yet we report some constituents for the first time from this plant using a different isolation approach. This manuscript presents the isolation, antimicrobial and antioxidant evaluation of bioactive principles from Iris hookeriana. LC-MS guided isolation technique was applied for the separation of target constituents. The isolates were characterised by spectral techniques and subjected to antioxidant evaluation by DPPH assay. Four compounds; resveratrol, resveratroloside, junipeginin C and isorhamnetin-3-O-neohesperidoside were isolated for the first time along with 3 known compounds viz piceid, irigenin and iridin from I. hookeriana using this approach. The antioxidant activity screening of the isolates revealed that all the 4 constituents isolated for the first time, have strong antioxidant potential with IC50 of 14.0 µg/ml (resveratroloside), 19.7 µg/ml (junipeginen C), 12.8 µg/ml (resveratrol) and 19.8 µg/ml (isorhamnetin-3-O-neohesperodoside). So it can be safely concluded that LC-MS guided isolation of chemical compounds from Iris hookeriana has furnished 4 antioxidant constituents. Thus Iris hookeriana can act as as a good source of wonder molecule resveratrol and its 2 glycosides, resveratrolside and piceid which upon hydrolysis can be converted into the parent drug resveratrol.


Subject(s)
Anti-Bacterial Agents/isolation & purification , Anti-Bacterial Agents/pharmacology , Antioxidants/isolation & purification , Antioxidants/pharmacology , Iris Plant/chemistry , Stilbenes/isolation & purification , Anti-Bacterial Agents/chemistry , Antioxidants/chemistry , Chromatography, Liquid , Flavonols/chemistry , Flavonols/isolation & purification , Flavonols/pharmacology , Glucosides/chemistry , Glucosides/isolation & purification , Glucosides/pharmacology , Isoflavones/chemistry , Isoflavones/isolation & purification , Isoflavones/pharmacology , Microbial Sensitivity Tests , Plant Extracts/chemistry , Resveratrol , Spectrometry, Mass, Electrospray Ionization , Stilbenes/chemistry , Stilbenes/pharmacology
3.
Parasitol Res ; 109(1): 1-8, 2011 Jul.
Article in English | MEDLINE | ID: mdl-21286754

ABSTRACT

The elimination of lymphatic filariasis in the Andaman and Nicobar Islands provides unique opportunities and challenges at the same time. Since these islands are remote, are sparsely populated, and have poor transport networks, mass drug administration programs are likely to be difficult to implement. Diurnally subperiodic Wuchereria bancrofti vectored by Downsiomyia nivea was considered for the scope of vector control options. Considering the bioecology of this mosquito, vector control including personal protection measures may not be feasible. However, since these islands are covered by separate administrative machinery which also plays an important role in regulating the food supply, the use of diethylcarbamazine (DEC)-fortified salt as a tool for the interruption of transmission is appealing. DEC-fortified salt has been successfully pilot tested in India and elsewhere, operationally used by China for eliminating lymphatic filariasis. Administration of DEC-fortified salt though simple, rapid, safe, and cost-effective, challenges are to be tackled for translating this precept into action by evolving operationally feasible strategy. Although the use of DEC-fortified salt is conceptually simple, it requires commitment of all sections of the society, an elaborate distribution mechanism that ensures the use of DEC-fortified salt only in the endemic communities, and a vigorous monitoring mechanism. Here, we examine the inbuilt administrative mechanisms to serve the tribal people, health infrastructure, and public distribution system and discuss the prospects of putting in place an operationally feasible strategy for its elimination.


Subject(s)
Diet Therapy/methods , Dietary Supplements , Diethylcarbamazine/administration & dosage , Filariasis/epidemiology , Filariasis/prevention & control , Filaricides/administration & dosage , Wuchereria bancrofti/isolation & purification , Animals , Culicidae/parasitology , Humans , India/epidemiology
6.
J Virol ; 66(6): 3355-62, 1992 Jun.
Article in English | MEDLINE | ID: mdl-1316452

ABSTRACT

The Epstein-Barr virus nuclear antigen EBNA-1 is essential for replication of the viral DNA during latency. EBNA-1 binds as a dimer to palindromic recognition sequences within the plasmid origin of replication, ori-P. In this study, proteinase K susceptibility has been used to further characterize the DNA-binding domain of EBNA-1. Limited protease digestion of EBNA-1 (amino acids 408 to 641) generated a smaller DNA-binding species that had a degree of inherent protease resistance. When EBNA-1 was preincubated with a specific DNA probe, the protease resistance of the smaller binding species increased 100-fold, suggesting that the conformation of EBNA-1 changes on binding. The protease-resistant species comprised an 18-kDa polypeptide that was further cleaved at high levels of protease to 11- and 5.4-kDa products. A model of the proposed protease-resistant domain structure is presented. Constructions carrying serial, internal deletions across the 18-kDa domain were created. Each of the deletions perturbed dimerization ability and abolished DNA binding. These studies suggest that the DNA-binding and dimerization motifs of EBNA-1 lie within a conformationally discrete domain whose overall integrity is necessary for EBNA-1-DNA interaction.


Subject(s)
Antigens, Viral/metabolism , DNA, Viral/metabolism , DNA-Binding Proteins/metabolism , Herpesvirus 4, Human/metabolism , Regulatory Sequences, Nucleic Acid/genetics , Antigens, Viral/drug effects , DNA Mutational Analysis , DNA-Binding Proteins/drug effects , Endopeptidase K , Epstein-Barr Virus Nuclear Antigens , Herpesvirus 4, Human/drug effects , Models, Biological , Nucleic Acid Conformation , Serine Endopeptidases/pharmacology
7.
J Virol ; 64(5): 2369-79, 1990 May.
Article in English | MEDLINE | ID: mdl-2157891

ABSTRACT

Interaction between the trans-acting DNA-binding protein EBNA-1 and cis-acting sequences in the ori-P region of Epstein-Barr virus DNA is required for maintenance of the viral plasmid state in latently infected B cells and is involved in the regulation of transcription during latency. In the Epstein-Barr virus genome, a total of 26 EBNA-1-binding sites occur within three clustered loci referred to as the family of repeats and dyad symmetry locus of ori-P and the separate BamHI-Q locus. Incubation of a bacterially expressed carboxy-terminal domain of EBNA-1 (28,000-molecular-weight EBNA-1 [28K EBNA-1]) with synthetic monomer and dimer consensus binding sites gave characteristic DNA-protein complexes in a mobility retardation assay. A similar approach with the naturally occurring Q locus confirmed that it contains two distinct but low-affinity binding sites. We then examined the precise sequence requirements for EBNA-1 binding, using a set of 30-base-pair oligonucleotides designed to contain symmetric point mutations within both halves of the palindromic target site. Analysis of all possible single substitutions between positions 1 and 10 in the consensus half-palindrome sequence revealed that positions 9 and 10 did not contribute to EBNA-1 binding and that considerable flexibility could be tolerated at positions 1 and 2. Positions 3 through 8 of the recognition site had the most stringent requirements, with transversions at these positions either reducing or eliminating binding. The relative spacing of the halves of the palindrome was also critical, since the addition or removal of 2 base pairs at the center of the sequence abolished binding. Similar results were obtained when a partially purified preparation of intact Raji EBNA-1 was substituted for the 28K EBNA-1, and the results were further supported by methylation interference studies which indicated contact points between EBNA-1 and the guanine residues at positions -8, -7, and +3 of the binding site. The three naturally occurring EBNA-1-binding loci have previously been shown to differ in their relative affinities for EBNA-1. The present study indicates that the sequence variations occurring within the family of repeats would not affect binding affinity, whereas certain base substitutions within the Q and dyad symmetry sites would be predicted to contribute to the observed lower affinities of these sites. An apparent Kd of 1.5 x 10(-11) M for binding of 28K EBNA-1 to a consensus recognition site was calculated from Scatchard analysis.


Subject(s)
Antigens, Viral/genetics , DNA, Viral/genetics , DNA-Binding Proteins/genetics , Herpesvirus 4, Human/genetics , Base Sequence , Cloning, Molecular , DNA-Binding Proteins/metabolism , Epstein-Barr Virus Nuclear Antigens , Escherichia coli/genetics , Herpesvirus 4, Human/immunology , Kinetics , Molecular Sequence Data , Mutation , Oligonucleotide Probes/chemical synthesis , Protein Binding , Recombinant Fusion Proteins/metabolism , Restriction Mapping
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