Polymyxin B sensitive strains of Vibrio cholerae non-O1 from recent epidemic in India.
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Cholera↗
Biomedical subjects
S Garg
Publications and source records attributed to S Garg.
Emergence of novel strain of Vibrio cholerae with epidemic potential in southern and eastern India.
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Cholera↗
Distribution of the zot (zonula occludens toxin) gene among strains of Vibrio cholerae 01 and non-01.
The distribution of the zot gene that encodes the zonula occludens toxin, a newly described toxin of Vibrio cholerae, among clinical, environmental and food isolates of V. cholerae 01 and non-01 was investigated. Both the zot gene and the ctx gene that encode cholera toxin were found in 247 of 257 clinical strains and 62 of 415 environmental or food isolates of V. cholerae 01. The zot gene, but not the ctx gene was found in 37 strains (one clinical strain and 36 environmental or food isolates). In addition, two of 31 clinical strains and six of 98 environmental or food isolates of V. cholerae' non-01 possessed both the zot gene and the ctx gene. These results demonstrated the predominantly concurrent occurrence of the zot gene and ctx genes among strains of V. cholerae 01 which suggests a possible synergistic role of ZOT in the causation of acute dehydrating diarrhea produced by V. cholerae 01.
Cholera Toxin↗
Studies on the contraceptive efficacy of Praneem polyherbal cream.
Praneem polyherbal cream, a spermicidal formulation, has been developed at the National Institute of Immunology, which makes use of Praneem, a purified extract from the dried seeds of an ancient Indian plant Azadirachta indica (Neem), extract from the pericarp of fruits of Sapindus species and quinine hydrochloride. These ingredients have a synergistic spermicidal activity and an optimised formula was derived. The components were made into a water-soluble cream base prepared by using pharmaceutically acceptable base and stabilised by addition of IP grade antioxidant and preservatives. The cream is devoid of irritation and sensitization potential, as seen with standard Draize test on normal and abraded skin of rabbits and by 21-day cumulative skin sensitivity in human volunteers. The formulation was found to be safe under subacute toxicity studies in monkeys. The formulation has shown high contraceptive efficacy in rabbits and in monkeys after intravaginal application. The shelf-life of the cream at room temperature is estimated to be 18 months by accelerated stability studies.
Animals↗
Clinical profile of acute diarrhoea cases infected with the new epidemic strain of Vibrio cholerae O139: designation of the disease as cholera.
A total of 113 patients suffering from acute watery diarrhoea caused by the novel epidemic strain of Vibrio cholerae non-O1, currently assigned to a new serogroup O139, were investigated in order to determine the clinical presentation of the new epidemic strain causing outbreaks of cholera-like infection in the Indian subcontinent. Estimations of electrolyte concentration in serum and stool were also performed in a representative number of the above cases. The clinical features and blood and stool biochemical parameters of V. cholerae serogroup O139 diarrhoeal patients were indistinguishable from those in typical cholera, except for 44.3% cases infected by O139 had abdominal cramps. In view of the above, we propose to designate the disease caused by V. cholerae O139 as cholera.
Acute Disease↗
Nationwide prevalence of the new epidemic strain of Vibrio cholerae O139 Bengal in India.
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Cholera↗
Topical phenytoin in the treatment of split-thickness skin autograft donor sites: a comparative study with polyurethane membrane drape and conventional dressing.
The effectiveness of topical phenytoin as a wound healing agent was compared with that of OpSite (Smith & Nephew) and a conventional topical antibiotic dressing (Soframycin, Roussel) in a controlled study of 60 patients with partial-thickness skin autograft donor sites on the lower extremities. Mean time to complete healing (complete epithelialization) was 6.2 +/- 1.6 days in the phenytoin-treated group (30 patients), compared to 8.6 +/- 2.2 days with OpSite (15 patients), and 12.6 +/- 3.4 days in the 15 Soframycin-treated patients. The differences between the treatment groups were significant at P < 0.001. Mean pain scores were also lower in the phenytoin-treated group, 0.40 +/- 0.55 vs. 0.66 +/- 0.60 with OpSite (P < 0.05) and 1.4 +/- 0.50 with the conventional dressing (P < 0.001). Both phenytoin and OpSite were superior to the Soframycin dressing with respect to bacterial contamination and wound infection as measured by Gram stains of wound smears, swab and aspirate (OpSite) cultures, and clinical assessments (P < 0.001) carried out on the fifth day of treatment. No local or systemic adverse effects of the three agents used were noted. Phenytoin appears to be an effective, low-cost and safe method for the treatment of partial-thickness skin graft donor sites, comparing very favourably with, and in some aspects superior to, occlusive dressings. Further clinical use and evaluation of topical phenytoin are merited.
Administration, Topical↗
N-succinimidyl 4-methyl-3-(tri-n-butylstannyl)benzoate: synthesis and potential utility for the radioiodination of monoclonal antibodies.
N-succinimidyl 4-methyl-3-(tri-n-butylstannyl)benzoate (MATE) was synthesized in two steps from 4-methyl-3-iodobenzoic acid. Radioiododestannylation of MATE proceeded more slowly than N-succinimidyl 3-(tri-n-butylstannyl)benzoate (ATE), but for reaction periods of 10 min or more, identical yields were obtained. Paired-label biodistribution studies were performed in mice with an intact monoclonal antibody and an F(ab')2 fragment labeled using MATE, ATE and Iodogen. Thyroid uptake with MATE was low, comparable to that seen with ATE, and considerably lower than that observed when the Iodogen method was used. With the F(ab')2 fragment, kidney uptake using MATE was 8-fold higher than that observed when either the ATE or Iodogen methods were used.
Animals↗
Radioiodination of a monoclonal antibody using N-succinimidyl 5-iodo-3-pyridinecarboxylate.
The potential utility of N-succinimidyl 5-iodo-3-pyridinecarboxylate (SIPC) for the radioiodination of monoclonal antibodies was investigated. Paired-label studies were performed using the anti-tenascin antibody 81C6 in athymic mice bearing subcutaneous D-54 MG human glioma xenografts. Radiolabeling was also done using N-succinimidyl 3-iodobenzoate (SIB). Radioiodination of SIPC and SIB both proceeded in 60-80% yield, but protein coupling efficiencies with SIB were higher (76 +/- 16 vs 60 +/- 7%). Immunoreactivity and affinity of both preparations were similar. Using SIPC, thyroid uptake was quite low, decreasing from 0.3% at day 1 to 0.05% at day 8. Tumor uptake reached 46 +/- 11% injected dose/g at day 1 but declined gradually thereafter. This apparent decline reflected the rapid growth of these xenografts since tumor accumulation expressed as percentage of injected dose remained nearly constant up to day 9. These results suggest that SIPC, like SIB, offers significant advantages for labeling antibodies when compared with conventional protein iodination methods.
Animals↗
Quantitative two-site enzyme-linked immunosorbent assays for inhibin A, activin A and activin B.
We have developed three specific enzyme-linked immunosorbent assay (ELISA) formats which quantitate inhibin A in conditioned media and serum. The assays are sensitive in a range 0.078-5.0 ng/ml and have been characterized in terms of cross-reactivity to inhibin related proteins. The CK:CK assay format recognizes inhibin A, inhibin B and inhibin-related molecules, while the 9A9:CK assay format recognizes inhibin A and inhibin A precursors, but not free alpha-subunit. The 11B5:CK assay appears to recognize only mature 32 kDa inhibin A. Additionally, we have developed separate, specific ELISA formats which quantitate activin A and activin B. The assays have a range of 0.2-50 ng/ml and 0.4-50 ng/ml for activin A and recombinant activin B, respectively. These assays are presently being used to examine the concentration of inhibin A, activin A and activin B in clinical serum samples.
Activins↗
Bend and splay elastic constants of diheptylazoxybenzene.
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Journal Article↗
Identification and characterization of binding proteins for inhibin and activin in human serum and follicular fluids.
Inhibins and activins are produced by a variety of tissues and may have important endocrine and paracrine roles in development, reproduction, and hematopoiesis. However, little is known regarding the physical properties or concentrations of inhibin and activin in biological fluids. Binding proteins for inhibin or activin in serum or at production or target sites may have important implications for restricting the bioactivity of these hormones and may alter the immunoreactivity of these molecules in biological fluids. The objective of this study was to identify inhibin- and activin-binding proteins in human serum (HS) and follicular fluid (hFF) and determine the ability of these proteins to alter biological or immunological activity. In HS, [125I]activin and inhibin bound to a protein identified as alpha 2-macroglobulin (alpha 2M) using three criteria: 1) [125I]inhibin and activin bind purified alpha 2M, but not several other serum proteins tested; 2) complexes formed by [125I]inhibin and activin in HS and in the presence of purified alpha 2M elute with similar retention times on HPLC; and 3) preadsorption of HS with alpha 2M antiserum inhibits inhibin and activin binding to this protein while antiserum directed against follistatin or other serum proteins had no effect. A small amount of a lower mol wt [125I]activin-follistatin complex was also found in HS. This complex eluted with a retention time similar to that of activin bound to purified porcine follistatin. Binding of inhibin to follistatin could not be detected in HS. In contrast, follistatin was the major binding protein of both activin and inhibin in hFF. Concentrations up to 100 micrograms/ml purified alpha 2M had no effect on the bioactivity or immunoreactivity of either inhibin or activin. In contrast, follistatin inhibited both activin-stimulated pituitary FSH release and K562 hemoglobin production as well as antiserum binding in a specific activin-A immunoassay. Follistatin did not interfere with inhibin immunodetection. These data indicate that two inhibin- and activin-binding proteins are present in different relative amounts in HS and hFF, alpha 2M, the primary binding protein in HS, did not alter inhibin or activin bio- or immunoactivity under the conditions of these experiments, while follistatin, the major binding protein in hFF, may mask activin's bio- and immunoactivities.
Activins↗
Pharmacokinetic profile of recombinant human (rh) inhibin A and activin A in the immature rat. I. Serum profile of rh-inhibin A and rh-activin A in the immature female rat.
The serum pharmacokinetics of recombinant human inhibin A (rh-inhibin A) and rh-activin A were examined in immature female Sprague Dawley-derived rats after iv and sc injection of the drugs. After iv administration of rh-inhibin A (120 micrograms/kg), the serum concentrations were described by a biexponential equation. The weight-normalized clearance was 21.3 ml/min.kg, and the initial (t1/2 alpha) and terminal (t1/2 beta) half-lives were 2.9 min and 37.9 min, respectively. Subcutaneous administration of 120 micrograms/kg rh-inhibin A resulted in a peak serum concentration of 10.6 ng/ml at 30.8 min after injection. Approximately 24% of the sc administered material was absorbed. Serum concentrations of rh-activin A also declined biexponentially after iv injection of the drug (120 micrograms/kg). The clearance of rh-activin A was 5.1 ml/min.kg, the t1/2 alpha was 6.1 min, and the t1/2 beta was 46.3 min. The peak serum concentration of rh-activin A (104.7 ng/ml) was achieved 24.7 min after sc delivery of the drug. The bioavailability of the sc dose was 38%. Iodinated rh-inhibin A and rh-activin A were used to examine the serum forms and metabolites of the drugs. [125I]rh-inhibin A and [125I]rh-activin A associated with two serum-binding proteins. Within 2 min of iv injection, the labeled hormones bound follistatin and alpha-2-macroglobulin. Even though rh-inhibin A and rh-activin A are structurally similar and appear to bind to the same serum proteins, their disposition in the immature rat differ.
Activins↗
A birth control vaccine is on the horizon for family planning.
Vaccines for control of fertility are likely to have an important impact on family planning methods. They are designed to act by mobilization of an internal physiological process and do not require external medication on a continuous basis. A number of birth control vaccines are at different stages of development, the most advanced being a vaccine inducing antibodies against human chorionic gonadotrophin (hCG). This vaccine consists of a heterospecies dimer (HSD, beta hCG associated with alpha-subunit of ovine luteinizing hormone, beta hCG:alpha oLH) linked to tetanus toxoid (TT) or diphtheria toxoid (DT) as carriers. The vaccine has recently passed an important milestone; it has completed the first leg of phase II efficacy trials. Women of proven fertility leading active sexual life were protected from becoming pregnant at antibody titres > or = 50 ng of hCG bioneutralization capacity per ml. This vaccine has previously been demonstrated to be reversible in its effect. It is free from any notable side-effects on endocrine, cardiovascular and other body functions. Ovulation was not disturbed and menstrual regularity was maintained. A logistic disadvantage of the present vaccine is the requirement for multiple injections. This is expected to be overcome by encapsulation of the requisite doses of the vaccine in biodegradable microspheres, which could be given at a single contact point for sustained antibody titres lasting over a year. A live recombinant vaccine has also been made that elicits high anti-hCG titres in monkeys for nearly 2 years following primary immunization and a booster at 8-9 months.
Adult↗
Magnitude of acute respiratory infections in under five.
A community-based study was carried out in a rural area of Delhi to measure the prevalence and incidence of acute respiratory infections among children below the age of 5 years. The prevalence of 12.1%, was similar in boys and girls and was seen to decline with age. The incidence of acute respiratory infections was 2.5 episodes per child per year; it was not different in boys and girls. There was a statistically significant decline in the incidence with age. Upper respiratory tract infections comprised 87.5% of total acute respiratory infection morbidity while lower respiratory tract infections were 12.5%. Both upper and lower respiratory tract infections declined with increasing age; while the former was similar among boys and girls, the incidence of latter was significantly greater in boys (0.4 episodes per year) as compared to girls (0.2 episodes per year). A total of 87.5% episodes were mild, 10.4% moderate and only 2.1% were severe. The results suggest that acute respiratory infections are a major community health problem and an acute respiratory infection control programme needs to be implemented urgently.
Acute Disease↗
Oral hygiene and gingival status in orthodontic patients.
The study was conducted to find out the plaque deposition and changes in the gingiva in patients under going orthodontic treatment with Fixed appliances, active removable appliances and with myofunctional appliances; taking 25 subjects in each group. A matching control of 25 dental students was taken for comparison. Findings reveal that though the plaque index and gingival index values in all treatment groups were higher than control group, but the values in all the 4 groups were found within the range of good oral hygiene i.e. less than 1.50 exhibiting that the orthodontic appliances whether fixed, active removable or Myofunctional would not affect oral hygiene or gingival health adversely if a proper oral hygiene instructions, were followed.
Adolescent↗
Localization of fluorine-18-labeled Mel-14 monoclonal antibody F(ab')2 fragment in a subcutaneous xenograft model.
Positron emission tomography is an imaging method that might improve the effectiveness of radioimmunoscintigraphy and might provide more accurate estimates of monoclonal antibody dosimetry prior to therapy. Because of its widespread availability, 2-h half-life 18F could be a useful nuclide for labeling monoclonal antibody fragments, provided that adequate tumor uptake and satisfactory tumor:normal tissue ratios could be achieved rapidly. In this study, the tissue distribution of 18F-labeled Mel-14 F(ab')2, a monoclonal antibody reactive with gliomas, was evaluated in a s.c. athymic mouse human glioma xenograft model. 18F labeling was performed using N-succinimidyl-8-(4-[18F]fluorobenzylamino) suberate. For paired-label comparisons both in vitro and in vivo, Mel-14 F(ab')2 was also labeled using N-succinimidyl 3- [125I]- iodobenzoate. When 100-120 micrograms of disuccinimidyl suberate was used in the 18F-labeled acylation agent synthesis, the binding of 18F-labeled Mel-14 F(ab')2 to glioma homogenates was comparable to that of the radioiodinated fragment. Scatchard analyses indicated nearly identical affinity constants for fragments with both labels (18F, 6.4 x 10(8) M-1; 125I, 6.7 x 10(8) M-1). Tumor levels of 18F increased between 1 and 2 h and then were relatively constant between 2 and 6 h. When lower levels of disuccinimidyl suberate were used, there was an excellent correlation between 18F and 125I tumor uptake (r = 0.984, slope 1.03-1.04). At 4 h, tumor:normal tissue ratios for 18F-labeled Mel-14 F(ab')2 in liver, spleen, muscle, and brain were 2.3, 4.2, 14, and 40, respectively. Localization indices, determined by comparison with 18F-labeled nonspecific F(ab')2, were 3.7 at 4 h and 6.9 at 6 h for tumor and about 1 for normal tissues, indicating the specificity of 18F-labeled Mel-14 F(ab')2 tumor uptake.
Animals↗
Immunomodulatory effects of neem (Azadirachta indica) oil.
Immunomodulatory effects of neem oil were studied in mice. The animals were treated intraperitoneally (i.p.) with neem oil; control animals received the emulsifying agent with or without peanut oil. Peritoneal lavage, collected on subsequent days, showed a maximum number of leukocytic cells on day 3 following treatment with neem oil; peritoneal macrophages exhibited enhanced phagocytic activity and expression of MHC class-II antigens. Neem oil treatment also induced the production of gamma interferon. Spleen cells of neem oil-treated animals showed a significantly higher lymphocyte proliferative response to in vitro challenge with Con A or tetanus toxoid (TT) than that of the controls. Pre-treatment with neem oil, however, did not augment the anti-TT antibody response. The results of this study indicate that neem oil acts as a non-specific immunostimulant and that it selectively activates the cell-mediated immune (CMI) mechanisms to elicit an enhanced response to subsequent mitogenic or antigenic challenge.
Adjuvants, Immunologic↗