Chlorhexidine resistance in a Gram-negative bacterium isolated from an aquatic source.

Aeromonas hydrophila is a Gram-negative bacterium of considerable importance in both clinical, especially nosocomial infections, and zoonotic respects, both aquatic and terrestrial infections. In addition to the ability to thrive in a wide range of conditions, A. hydrophila is resistant to numerous antibiotics and antimicrobials.

Triclosan-resistant bacteria isolated from feedlot and residential soils.

Triclosan is an antimicrobial agent that is currently incorporated into hundreds of consumer and medical products. It can be either a bacteriostatic or bactericidal agent, depending on its formulation. It has activity against Gram-positive and Gram-negative bacteria, as well as some viruses and protists.

Bacteria isolated from sewage influent resistant to ciprofloxacin, chloramphenicol and tetracycline.

This study assessed the presence of antibiotic-resistant bacteria in sewage influent. Resistance was measured by determining the lowest concentration of antibiotic, in micrograms per milliliter (microg mL(- 1)). To determine the minimum inhibitory concentration (MIC), which is used in diagnostic laboratories, we used the Etest, a plastic strip containing an antibiotic concentration gradient.

The multifunctional capsid proteins of plant RNA viruses.

This article summarizes studies of viral coat (capsid) proteins (CPs) of RNA plant viruses. In addition, we discuss and seek to interpret the knowledge accumulated to data. CPs are named for their primary function; to encapsidate viral genomic nucleic acids.

Avian polyomavirus major capsid protein VP1 interacts with the minor capsid proteins and is transported into the cell nucleus but does not assemble into capsid-like particles when expressed in the baculovirus system.

The baculovirus system was used to construct and isolate AcMNPV-VP1, AcMNPV-VP2 and AcMNPV-VP3 recombinant viruses which express the respective avian polyomavirus (APV) structural proteins in Sf9 insect cells. These recombinant AcMNPVs containing APV structural protein genes were utilized to investigate protein-protein interactions between the structural proteins. Immunofluorescence studies utilizing Sf9 cells infected with the AcMNPV-VP1 revealed that the VP1 protein was expressed and localized in the cytoplasm and not transported into the nucleus.

Use of the baculovirus system to assemble polyomavirus capsid-like particles with different polyomavirus structural proteins: analysis of the recombinant assembled capsid-like particles.

The genes encoding the structural proteins (VP1, VP2 and VP3) of murine polyomavirus were cloned into the p2Bac dual multiple cloning site vector, individually or jointly, and the corresponding proteins were expressed in Spodoptera frugiperda (Sf9) insect cells by cotransfecting Sf9 cells with the constructed vector and the linear DNA of Autographa californica multiple nuclear polyhedrosis virus (AcMNPV). Recombinant capsid-like particles could be purified 5 days post-infection from Sf9 cells infected with AcMNPV-VP1, with or without the involvement of minor protein (VP2 or VP3). Although VP2 and VP3 alone could not generate recombinant particles, they became incorporated into these particles when expressed with VP1 in Sf9 cells.

Truncation of the nuclear localization signal of polyomavirus VP1 results in a loss of DNA packaging when expressed in the baculovirus system.

Using the pBlueBacIII baculovirus transfer vector, N11-VP1, a truncated form of the polyomavirus major capsid protein VP1, was cloned for expression in the baculovirus-insect cell expression system. The N11-VP1 protein is virtually identical to full-length, wild-type VP1, except that the first 11 amino acids have been deleted from the amino terminus of the protein. The N-terminal region of VP1 has previously been shown to contain the nuclear localization signal (NLS) of the protein and contains residues essential for both nuclear transport as well as DNA-binding functions.

Polyomavirus major capsid protein VP1 is capable of packaging cellular DNA when expressed in the baculovirus system.

Using the p2Bac dual multiple cloning site transfer vector, the polyomavirus major capsid protein gene VP1 was cloned for expression in the baculovirus-insect cell expression system. The 5-day-infected cellular lysate from this recombinant preparation was purified by cesium chloride density gradient centrifugation. Capsid-like particles were observed in the resulting preparation.

The effect of space flight on monoclonal antibody synthesis in a hybridoma mouse cell line.

The hybridoma cell line, 3G10G5, producing a monoclonal antibody to the major capsid protein VP1 from the avian polyomavirus budgerigar fledgling disease virus, was produced from a Balb/C mouse. This cell line was used to test the effects of microgravity on cellular processes, specifically protein synthesis. A time course study utilizing incorporation of [35S]methionine into newly synthesized monoclonal antibody was performed on STS-77.