Use of FTA sampling cards for molecular detection of avian influenza virus in wild birds.

Current avian influenza (AI) virus surveillance programs involving wild birds rely on sample collection methods that require refrigeration or low temperature freezing to maintain sample integrity for virus isolation and/or reverse-transcriptase (RT) PCR. Maintaining the cold chain is critical for the success of these diagnostic assays but is not always possible under field conditions. The aim of this study was to test the utility of Finders Technology Associates (FTA) cards for reliable detection of AI virus from cloacal and oropharyngeal swabs of wild birds.

Avian influenza surveillance in hunter-harvested waterfowl from the Gulf Coast of Texas (November 2005-January 2006).

The objectives of our study were to determine prevalence of avian influenza viruses (AIV) on wintering grounds on the Texas Gulf Coast, USA, and to compare real-time reverse-transcriptase polymerase chain reaction (rRT-PCR) and virus isolation for detection of AIV in cloacal swabs from wild waterfowl. Cloacal swabs were collected from hunter-harvested waterfowl from November 2005 to January 2006 at four wildlife management areas. Seven AIV were isolated from four species of ducks: Green-winged Teal (Anas crecca) in November; Blue-winged Teal (Anas discors) in November; Mottled Duck (Anas fulvigula) in December, and Northern Shoveler (Anas clypeata) in January.

Folding of a universal ribozyme: the ribonuclease P RNA.

Ribonuclease P is among the first ribozymes discovered, and is the only ubiquitously occurring ribozyme besides the ribosome. The bacterial RNase P RNA is catalytically active without its protein subunit and has been studied for over two decades as a model system for RNA catalysis, structure and folding. This review focuses on the thermodynamic, kinetic and structural frameworks derived from the folding studies of bacterial RNase P RNA.

Dimeric and monomeric Bacillus subtilis RNase P holoenzyme in the absence and presence of pre-tRNA substrates.

Ribonuclease P (RNase P) is a ribonucleoprotein enzyme that catalyzes the 5' maturation of tRNA precursors. The bacterial RNase P holoenzyme is composed of a large, catalytic RNA and a small protein. Our previous work showed that Bacillus subtilis RNase P forms a specific "dimer" that contains two RNase P RNA and two RNase P protein subunits in the absence of substrate.