Biomedical subjects

Amita Gupta

Publications and source records attributed to Amita Gupta.

23 records · Page 2Linked to original sources

PubMed2003

Emergence of multidrug-resistant Salmonella enterica serotype Newport infections resistant to expanded-spectrum cephalosporins in the United States.

We describe a field investigation in New England that identified the emergence and epidemiology of new strains of multidrug-resistant Salmonella, Newport-MDRAmpC, and summarize the Center for Disease Control and Prevention's surveillance data for these infections. In Massachusetts, the prevalence of Newport-MDRAmpC among Salmonella serotype Newport isolates obtained from humans increased from 0% (0/14) in 1998 to 53% (32/60) in 2001 (P<.001). In a retrospective case-control study, infection with Newport-MDRAmpC was domestically acquired and was associated with exposure to a dairy farm. Isolates from both humans and cattle had indistinguishable or closely related antibiograms and pulsed-field gel electrophoresis patterns. Nationally, the prevalence of ceftriaxone-resistant Salmonella increased from 0.5% in 1998 to 2.4% in 2001; 85% of the isolates in 2001 were Newport-MDRAmpC, and at least 27 states have isolated these strains from humans, cattle, or ground beef. These data document the widespread emergence of Newport-MDRAmpC strains in the United States and show that the 5-fold increase in the prevalence of Salmonella resistant to expanded-spectrum cephalosporins, between 1998 and 2001, is primarily due to the emergence of Newport-MDRAmpC strains.

Adolescent↗

PubMed2003

Ferromagnetism above room temperature in bulk and transparent thin films of Mn-doped ZnO.

The search for ferromagnetism above room temperature in dilute magnetic semiconductors has been intense in recent years. We report the first observations of ferromagnetism above room temperature for dilute (<4 at.%) Mn-doped ZnO. The Mn is found to carry an average magnetic moment of 0.16 mu(B) per ion. Our ab initio calculations find a valance state of Mn(2+) and that the magnetic moments are ordered ferromagnetically, consistent with the experimental findings. We have obtained room-temperature ferromagnetic ordering in bulk pellets, in transparent films 2-3 microm thick, and in the powder form of the same material. The unique feature of our sample preparation was the low-temperature processing. When standard high-temperature (T > 700 degrees C) methods were used, samples were found to exhibit clustering and were not ferromagnetic at room temperature. This capability to fabricate ferromagnetic Mn-doped ZnO semiconductors promises new spintronic devices as well as magneto-optic components.

Journal Article↗

PubMed2003

Facial and body blood contamination in major gynecologic surgeries.

AIM: To determine the incidence of facial and body blood contamination in various major gynecologic surgeries. METHODS: A prospective study was conducted over a 6-month period on 122 major gynecologic surgeries (abdominal and vaginal) to determine the incidence of blood splashes on masks, goggles (or spectacles), body and feet of surgeons and assistants. RESULTS: The overall incidence of blood splashes was 49.18%, 59.5%, 28.68% and 22.95% on surgeons masks, goggles, body and feet, respectively. This incidence was significantly higher (P < 0.05) than for first assistants, who showed an incidence of blood splashes of 35.24% (mask), 38.13% (goggles), 20.49% (body) and 9.83% (feet). The lowest incidence of splashes was seen on second assistants, with 22.1% (mask), 24.73% (goggles), 10.52% (body) and 7.36% (feet). There was no significant difference in the facial splash rate between major abdominal and vaginal surgeries, but body and feet contamination was significantly higher in major vaginal surgeries (P < 0.05). CONCLUSION: There is a very high risk of facial and body blood contamination in major gynecologic surgeries, putting the surgeon and assistants at risk of acquiring viral disease. Routine use of universal precautions in all gynecologic surgeries is strongly recommended.

Blood↗

PubMed2003

Whole-blood agglutination assay for on-site detection of human immunodeficiency virus infection.

Simple and rapid diagnostic tests are needed to curtail human immunodeficiency virus (HIV) infection, especially in the developing and underdeveloped nations of the world. The visible-agglutination assay for the detection of HIV with the naked eye (NEVA HIV, which represents naked eye visible-agglutination assay for HIV) is a hemagglutination-based test for the detection of antibodies to HIV in whole blood. The NEVA HIV reagent is a cocktail of highly stable recombinant bifunctional antibody fusion proteins with HIV antigens which can be produced in large quantities with a high degree of purity. The test procedure involves mixing of one drop of the NEVA HIV reagent with one drop of blood sample on a glass slide. The presence of anti-HIV antibodies in the blood sample leads to clumping of erythrocytes (agglutination) that can be seen with the naked eye. Evaluation with commercially available panels of sera and clinical samples has shown that the performance of NEVA HIV is comparable to those of U.S. and European Food and Drug Administration-approved rapid as well as enzyme-linked immunosorbent assay kits. The test detects antibodies to both HIV type 1 (HIV-1) and HIV-2 in a single spot and gives results in less than 5 min. The test was developed by keeping in mind the practical constraints of testing in less developed countries and thus is completely instrument-free, requiring no infrastructure or even electricity. Because the test is extremely rapid, requires no sample preparation, and is simple enough to be performed by a semiskilled technician in any remote area, NEVA HIV is a test for the hard-to-reach populations of the world.

Antibodies, Monoclonal↗

PubMed2002

Expression, purification, and characterization of an anti-RBCFab-p24 fusion protein for hemagglutination-based rapid detection of antibodies to HIV in whole blood.

A fusion protein A41Fabp246 consisting of Fab of an anti-RBC MAb A41 and amino acids 8-153 of HIV-1 p24 (p246) fused at the C-terminus of A41Fd was purified following assembly of A41Fdp246 with A41 LC in vitro, using a denaturation- renaturation protocol and a 4-step column chromatography procedure. The highly purified, monomeric A41Fabp246 was then evaluated for hemagglutination-based detection of anti-p24 antibodies using sera from HIV-infected individuals. This derivative of p24 is devoid of maximum homology region and the C-terminal domain of p24, which is responsible for oligomerization of p24, but retains full complement of immunodominant epitopes. This new fusion protein in combination with fusion proteins consisting of monovalent fragment of another anti-human RBC antibody fused to immunodominant regions of envelope glycoproteins of HIV-1 and HIV-2 should be useful in preparing a cocktail of reagents for highly sensitive detection of anti-HIV antibodies in whole blood.

Animals↗