Radiation dose reduction in scoliosis patients: low-dose full-spine radiography with digital flat panel detector and image stitching system.

PURPOSE: To evaluate the exposure dose reduction with a digital flat panel detector (FPD) and an image stitching system (ISS) in full-spine radiography for scoliosis patients. MATERIALS AND METHODS: During a 6-month period, all consecutive scoliosis patients with a clinical indication for full-spine radiography (n = 50) were examined with an FPD and ISS. Automatic exposure control adjusted to speed class 1600 was used together with age-adjusted tube voltage and filtration. Dose area products were recorded for all images (antero-posterior n = 50, lateral n = 18). Images were evaluated by two radiologists for the possibility (possible, impossible) of typical scoliosis measurements (Cobb angle, Stagnara angle, lateral deviation, Risser stage). All measurements assessed as impossible underwent a second evaluation categorizing the reason why a measurement was impossible (underlying pathology, projection, image quality). Patient characteristics influencing exposure were recorded (sex, age, weight, height). Mean dose area products were compared to the literature with consideration of patient group and image quality. RESULTS: The mean dose area product was 16.8 µGy m (2) for antero-posterior images and 26.6 µGy m (2) for lateral images. A comparison to published values showed an exposure dose reduction of 47 % to 93 %. Measurement of the Cobb and Stagnara angle, lateral deviation and Risser stage was possible in 96 % (n = 50), 83 % (n = 18), 100 % (n = 50) and 100 % (n = 50) of cases. The reasons for impossible measurements were independent of image quality (underlying pathologies, projection). CONCLUSION: When imaging scoliosis patients, an FPD combined with an ISS can substantially reduce the exposure dose.

Specific initiation of replication at the right-end telomere of the closed species of minute virus of mice replicative-form DNA.

We have developed an in vitro system that supports the replication of natural DNA templates of the autonomous parvovirus minute virus of mice (MVM). MVM virion DNA, a single-stranded molecule bracketed by short, terminal, self-complementary sequences, is converted into double-stranded replicative-form (RF) DNA when incubated in mouse A9 fibroblast extract. The 3' end of the newly synthesized complementary strand is ligated to the right-end hairpin of the virion strand, resulting in the formation of a covalently closed RF (cRF) molecule as the major conversion product. cRF DNA is not further replicated in A9 cell extract alone. On addition of purified MVM nonstructural protein NS1 expressed from recombinant baculoviruses or vaccinia viruses, cRF DNA is processed into a right-end (5' end of the virion strand) extended form (5'eRF). This is indicative of NS1-dependent nicking of the right-end hairpin at a distinct position, followed by unfolding of the hairpin and copying of the terminal sequence. In contrast, no resolution of the left-end hairpin can be detected in the presence of NS1. In the course of the right-end nicking reaction, NS1 gets covalently attached to the right-end telomere of the DNA product, as shown by immunoprecipitation with NS1-specific antibodies. The 5'eRF product is the target for additional rounds of NS1-induced nicking and displacement synthesis at the right end, arguing against the requirement of the hairpin structure for recognition of the DNA substrate by NS1. Further processing of the 5'eRF template in vitro leads to the formation of dimeric RF (dRF) DNA in a left-to-left-end configuration, presumably as a result of copying of the whole molecule by displacement synthesis initiated at the right-end telomere. Formation of dRF DNA is highly stimulated by NS1. The experimental results presented in this report support various assumptions of current models of parvovirus DNA replication and provide new insights into the replication functions of the NS1 protein.

The minute virus of mice (MVM) nonstructural protein NS1 induces nicking of MVM DNA at a unique site of the right-end telomere in both hairpin and duplex conformations in vitro.

The right-end telomere of replicative form (RF) DNA of the autonomous parvovirus minute virus of mice (MVM) consists of a sequence that is self-complementary except for a three nucleotide loop around the axis of symmetry and an interior bulge of three unpaired nucleotides on one strand (designated the right-end 'bubble'). This right-end inverted repeat can exist in the form of a folded-back strand (hairpin conformation) or in an extended form, base-paired to a copy strand (duplex conformation). We recently reported that the right-end telomere is processed in an A9 cell extract supplemented with the MVM nonstructural protein NS1. This processing is shown here to result from the NS1-dependent nicking of the complementary strand at a unique position 21 nt inboard of the folded-back genomic 5' end. DNA species terminating in duplex or hairpin configurations, or in a mutated structure that has lost the right-end bulge, are all cleaved in the presence of NS1, indicating that features distinguishing these structures are not prerequisites for nicking under the in vitro conditions tested. Cleavage of the hairpin structure is followed by strand-displacement synthesis, generating the right-end duplex conformation, while processing of the duplex structure leads to the release of free right-end telomeres. In the majority of molecules, displacement synthesis at the right terminus stops a few nucleotides before reaching the end of the template strand, possibly due to NS1 which is covalently bound to this end. A fraction of the right-end duplex product undergoes melting and re-folding into hairpin structures (formation of a 'rabbit-ear' structure).