Coding-Complete Genome Sequences of Emerging Rabbit Hemorrhagic Disease Virus Type 2 Isolates Detected in 2020 in the United States.

Five rabbit hemorrhagic disease virus type 2 (RHDV2) coding-complete genome sequences were obtained from the livers of domestic and wild rabbits during the 2020 outbreak in the United States. These represent the first available RHDV2 sequences from the United States.

Genome Sequences of Vesicular Stomatitis Indiana Viruses from the 2019 Outbreak in the Southwest United States.

We report the genomes of three vesicular stomatitis Indiana virus (VSIV) isolates collected from naturally infected bovines in Wyoming and Colorado during the 2019 outbreak in the United States. These genomes support molecular diagnostic efforts and provide data on the spread and ecology of VSIV in the United States.

FNR-mediated oxygen-responsive regulation of the nrdDG operon of Escherichia coli.

Transcription of the nrdDG operon, which encodes the class III nucleotide reductase, which is only active under anaerobic conditions, was strongly induced after a shift to anaerobiosis. The induction was completely dependent on the transcriptional activator FNR and was independent of the ArcA-ArcB two-component response regulator system. The nrdD transcript start site was mapped to a position immediately downstream of two FNR binding sites. Transcription of the other two nucleotide reductase operons, nrdAB and nrdEF, did not respond to oxygen conditions in a wild-type background, but nrdAB expression was increased in the fnr mutant under anaerobic conditions.

A hospital's non-delegable duty of care.

Visiting, honorary and staff medical practitioners, to name but a few, provide medical treatment and services to a variety of "patients", including private, public, in-patients and out-patients. The legal implications arising from the often complex fact situations created by the interactions of these participants and the relationship between hospitals and these participants can lead to hospitals both incurring and avoiding liability for injuries sustained by patients from negligent medical treatment. This article discusses the legal principles governing hospitals' liabilities in this context on the more onerous non-delegable duty of care ground.

The acute phase response and exercise: court and field sports.

OBJECTIVE: To determine the presence or absence of an acute phase response after training for court and field sports. PARTICIPANTS: All members of the Australian women's soccer team (n = 18) and all members of the Australian Institute of Sport netball team (n = 14). METHODS: Twelve acute phase reactants (white blood cell count, neutrophil count, platelet count, serum iron, ferritin, and transferrin, percentage transferrin saturation, alpha(1) antitrypsin, caeruloplasmin, alpha(2) acid glycoprotein, C reactive protein, and erythrocyte sedimentation rate) were measured during a rest period and after moderate and heavy training weeks in members of elite netball and women's soccer teams. RESULTS: Responses consistent with an acute phase response were found in five of 24 tests in the soccer players, and in three of 24 tests in the netball players. Responses in the opposite direction were found in seven of 24 tests in the soccer players and two of 24 tests in the netballers. The most sensitive reactant measured, C reactive protein, did not respond in a manner typical of an acute phase response. CONCLUSION: An acute phase response does not seem to occur as a consequence of the levels of training typical of elite female netball and soccer teams. This has implications for the interpretation of biochemical variables in these groups.

Evaluation of the Lactate Pro blood lactate analyser.

An evaluation of the hand-held portable Lactate Pro Analyser (KDK) was undertaken to assess its accuracy, reliability and versatility. Capillary blood samples were drawn from elite athletes in both laboratory and field settings and analysed in parallel. Accuracy was determined in relation to three other lactate analysers: (1) the ABL 700 Series Acid-Base analyser (n = 172 cases), (2) the Accusport Lactate Meter (n = 118 cases), and (3) the YSI 2300 Stat lactate analyser (n = 22 cases). The level of agreement was determined over the range of 1-18 mM. The repeatability of results between two different Lactate Pro analysers was also determined over the same range. Versatility was assessed in the field, where the Lactate Pro was used with elite athletes under a range of outdoor and indoor testing conditions. The correlations between the Lactate Pro and the ABL 700 Series Acid-Base analyser, YSI 2300 and Accusport were r = 0.98, r = 0.99, r = 0.97. The correlation between the two Lactate Pro analysers on the same sample (n = 96 cases) was r = 0.99. The level of agreement between the Lactate Pro and other analysers was generally less than +/- 2.0 mM over the physiological range of 1.0-18.0 mM (range of mean difference: -0.06 mM to 0.52 mM). The Lactate Pro was easy to operate and successfully completed the sample analysis in 100% of the tests performed. In summary, the Lactate Pro is accurate, reliable and exhibits a high degree of agreement with other lactate analysers.

Beta-hydroxy beta-methylbutyrate (HMB) supplementation does not influence the urinary testosterone: epitestosterone ratio in healthy males.

Six healthy, recreationally active, males undertook two weeks supplementation with beta-Hydroxy beta-Methylbutyrate (HMB). Supplementation was in capsule form with 3 g consumed each day in three even doses of 1 g at main meals. Mid stream urine samples were collected prior to, as well as, after one and two weeks of supplementation and subsequently analysed for testosterone and epitestosterone. The testosterone: epitestosterone ratio was not affected by 2 weeks of HMB supplementation (mean +/- SD baseline 1.02 +/- 0.68; week one 0.98 +/- 0.61; week two 0.92 +/- 0.62). Our results support the claim that supplementation with HMB at the doses recommended will not influence the urinary testosterone: epitestosterone ratio and thus not breach doping policies of the International Olympic Committee for exogenous testosterone or precursor administration.

Simulated moderate altitude elevates serum erythropoietin but does not increase reticulocyte production in well-trained runners.

The purpose of this study was to investigate whether the modest increases in serum erythropoietin (sEpo) experienced after brief sojourns at simulated altitude are sufficient to stimulate reticulocyte production. Six well-trained middle-distance runners (HIGH, mean maximum oxygen uptake, VO2max = 70.2 ml x kg(-1) x min(-1) spent 8-11 h per night for 5 nights in a nitrogen house that simulated an altitude of 2650 m. Five squad members (CONTROL, mean VO2max= 68.9 ml x kg(-1) x min(-1) undertook the same training, which was conducted under near-sea-level conditions (600 m altitude), and slept in dormitory-style accommodation also at 600 m altitude. For both groups, this 5-night protocol was undertaken on three occasions, with a 3-night interim between successive exposures. Venous blood samples were measured for sEpo after 1 and 5 nights of hypoxia on each occasion. The percentage of reticulocytes was measured, along with a range of reticulocyte parameters that are sensitive to changes in erythropoiesis. Mean serum erythropoietin levels increased significantly (P < 0.01) above baseline values [mean (SD) 7.9 (2.4) mU x ml(-1)] in the HIGH group after the 1st night [11.8 (1.9) mU x ml(-1), 57%], and were also higher on the 5th night [10.7 (2.2) mU x ml(-1), 42%] compared with the CONTROL group, whose erythropoietin levels did not change. After athletes spent 3 nights at near sea level, the change in sEpo during subsequent hypoxic exposures was markedly attenuated (13% and -4% change during the second exposure; 26% and 14% change during the third exposure; 1st and 5th nights of each block, respectively). The increase in sEpo was insufficient to stimulate reticulocyte production at any time point. We conclude that when daily training loads are controlled, the modest increases in sEpo known to occur following brief exposure to a simulated altitude of 2650 m are insufficient to stimulate reticulocyte production.

Elite endurance athletes and the ACE I allele--the role of genes in athletic performance.

Genetic markers that might contribute to the making of an elite athlete have not been identified. Potential candidate genes might be found in the renin-angiotensin pathway, which plays a key role in the regulation of both cardiac and vascular physiology. In this study, DNA polymorphisms derived from the angiotensin converting enzyme (ACE), the angiotensin type 1 receptor (AT1) and the angiotensin type 2 receptor (AT2) were studied in 64 Australian national rowers. Compared with a normal population, the rowers had an excess of the ACE I allele (P<0.02) and the ACE II genotype (P=0.03). The ACE I allele is a genetic marker that might be associated with athletic excellence. It is proposed that the underlying mechanism relates to a healthier cardiovascular system.

A viral peptide with limited homology to a self peptide can induce clinical signs of experimental autoimmune encephalomyelitis.

Molecular mimicry has been suggested as a mode of autoreactive T cell stimulation in autoimmune diseases. Myelin basic protein (MBP) peptide 1-11 induces experimental autoimmune encephalomyelitis (EAE) in susceptible strains of mice. Here we show that a herpesvirus Saimiri (HVS) peptide, AAQRRPSRPFA, with a limited homology to MBP1-11 peptide, ASQKRPSQRHG (underlined letters showing homology), can stimulate a panel of MBP-11-specific T cell hybridomas and more importantly cause EAE in mice. We demonstrate that this is due to cross-recognition of these two peptides by TCRs. Results presented in this communication are the first demonstration that a viral peptide with homology at just 5 amino acids with a self peptide can induce clinical signs of EAE in mice. These findings have important implications in understanding the breakdown of T cell tolerance to self Ags in autoimmune diseases by means of cross-reactivity with unrelated peptides.

Identification of residues in the class II-associated Ii peptide (CLIP) region of invariant chain that affect efficiency of MHC class II-mediated antigen presentation in an allele-dependent manner.

Invariant chain (Ii) associates with class II MHC molecules and is crucial for Ag presentation by class II molecules. A general explanation for how invariant chain (Ii) associates with polymorphic MHC class II molecules has been suggested by the crystallographic structure of CLIP (class II-associated Ii peptide) complexed with an HLA class II molecule, HLA-DR3. We show here that methionine residues at positions 93 and 99 in Ii are important in MHC class II-mediated Ag presentation, but function in an allele-dependent manner. Introduction of a Met-->Ala mutation at position 99 in Ii (M99AIi) impaired presentation of peptides derived from exogenous proteins by I-Ad and I-Au class II molecules. Mutating Met-->Ala in Ii at position 93 (M93AIi) abrogated presentation by I-Au molecules, but not by I-Ad. Impaired Ag presentation was associated with conformationally altered expression of I-A molecules on the surface of cells expressing mutated Ii. Cell surface CLIP staining and immunoprecipitation studies showed that both I-Ad and I-Au molecules were associated with an increased abundance of Ii peptides, CLIP, in cells expressing mutated Ii. These results show that methionine 93 and methionine 99 play an important physiologic role in Ii association with class II molecules by regulating release of CLIP from class II in the endocytic compartments to allow binding of cognate peptides.

Impaired antigen presentation by murine I-Ad class II MHC molecules expressed in normal and HLA-DM-defective human B cell lines.

The inability of certain antigen processing mutant cell lines to present intact proteins to T cells and to form SDS-stable MHC class II dimers has been shown to result from defective expression of HLA-encoded DMA and DMB genes. We have utilized some of these mutants to determine species compatibility of antigen presentation components. Mouse MHC class II I-Ad cDNA was transfected into the human B cell lymphoblastoid cell lines 8.1.6, 7.9.6 (a mutant cell line derived from 8.1.6) and an independent deletion mutant T2 (called 8.1.6d, 7.9.6d and T2.d respectively). These cells were than examined for various functions in antigen presentation. Interestingly, none of the cells transfected with I-Ad presented peptides derived from intact proteins to specific T cell hybridomas. However, presentation of synthetic peptides by these cells was normal. The ability to form SDS-stable dimers was dramatically reduced in the transfectants. In addition, I-Ad molecules at the cell surface appeared loaded predominantly with the invariant chain peptides, CLIP. These properties of the I-Ad transfectants are identical to those described for HLA class II molecules expressed in HLA-DM mutants. Perhaps the most interesting finding was the inability of I-Ad in 8.1.6 to present protein antigens. Since 8.1.6 cells present antigens to HLA-DR, DP, DQ-restricted T cells and also have intact HLA-DM and invariant chain (II) functions, these results argue that some component of human antigen processing machinery is incompatible with I-Ad molecules.