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1.
J Sports Sci ; 42(5): 381-391, 2024 Mar.
Article in English | MEDLINE | ID: mdl-38626796

ABSTRACT

There has been limited empirical study allowing athletes to voice their opinions on transgender participation in elite sport. This study surveyed 175 national, elite and world class athletes eligible to compete in the female category regarding transgender inclusion and eligibility. The study compared current Olympic versus current Olympic Recognised sports, elite versus world class, and current versus retired Olympic sport athletes. Most athletes favoured biological sex categorisation (58%) and considered it unfair for trans women to compete in the female category, except for precision sports. This view was held most strongly by world class athletes regarding their own sport (77% unfair, 15% fair). For trans men inclusion in the male category, most athletes considered it fair, except for Olympic sport athletes regarding contact sports (49% unfair, 27% fair) and sports heavily reliant on physical capacity (53% unfair, 29% fair). Notwithstanding those views, athletes (81%) believed sporting bodies should improve inclusivity for transgender athletes. Opinion varied somewhat according to career stage, competitive level and sport type. Nevertheless, athletes in the present study favoured categorisation by biological sex and did not support trans women eligibility for the female category in sports reliant on performance-related biological factors that differ between sexes.


Subject(s)
Athletes , Transgender Persons , Humans , Male , Female , Transgender Persons/psychology , Transgender Persons/statistics & numerical data , Athletes/psychology , Adult , Sports/statistics & numerical data , Competitive Behavior , Attitude , Young Adult , Surveys and Questionnaires , Middle Aged , Retirement
2.
Poult Sci ; 90(4): 781-90, 2011 Apr.
Article in English | MEDLINE | ID: mdl-21406363

ABSTRACT

Our study was conducted to determine the effects of dietary phytase on a natural Eimeria challenge in naive and vaccinated broilers. Prior to the experiment the litter was seeded with Eimeria by orally infecting 10-d-old chicks with a cocktail containing 100,000 and 5,000 sporulated Eimeria acervulina and Eimeria tenella oocysts, respectively. Straight-run broiler chicks were placed across 48 floor pens on fresh or seeded litter. Eight treatment combinations were created to include 2 dietary Ca-nonphytate P (npP) levels [0.9% Ca, 0.45% npP; 0.7% Ca, 0.35% npP, 500 phytase units of Optiphos phytase (JBS United, Sheridan, IN)], unchallenged versus challenged, and unvaccinated versus vaccinated groups of chicks. Body weights and feed consumption (FC) were recorded on d 10, 18, and 21. A total of 10 birds/treatment were killed on d 10 and 18 to obtain tissue samples from the duodena and ceca for lesion scoring and cytokine response measurement. At 21 d of age, the left tibia was removed from 18 birds/treatment to assess bone strength. Body weight, FC, and bone strength were unaffected (P > 0.05) by diet or vaccination. By d 21, birds exposed to coccidia had lower FC (P < 0.01), higher feed conversion (P < 0.001), and decreased bone strength (P < 0.01) compared with those not challenged. Regardless of treatment, gross and microscopic scoring of the intestines showed few differences (P > 0.05). Expression of interferon-γ did not differ (P > 0.05) in the duodena or ceca at either time point. The IL-17 gene expression was increased (P < 0.05) in phytase-supplemented, vaccinated, or challenged birds by 18 d of age, with significant interactions (P < 0.05) occurring between birds challenged and fed the marginal diet or vaccinated. Phytase supplementation was unable to provide additional benefits to performance or P utilization in birds vaccinated, subjected to a coccidiosis infection, or both. Based on cytokine production in the intestinal tract on d 10 and 18 postchallenge, the response to the Eimeria challenge was characterized by a T-helper type (Th) 17-like immune response and to a lesser extent a Th1-like immune response, whereas no Th2 cytokine was detected.


Subject(s)
6-Phytase/administration & dosage , Chickens , Coccidiosis/veterinary , Eimeria/immunology , Intestinal Diseases, Parasitic/veterinary , Poultry Diseases/parasitology , Animals , Body Weight/drug effects , Coccidiosis/immunology , Coccidiosis/parasitology , Coccidiosis/prevention & control , Cytokines/biosynthesis , Cytokines/genetics , Eating/drug effects , Feces/parasitology , Intestinal Diseases, Parasitic/immunology , Intestinal Diseases, Parasitic/parasitology , Least-Squares Analysis , Parasite Egg Count/veterinary , Pilot Projects , Poultry Diseases/immunology , Poultry Diseases/prevention & control , RNA, Protozoan/chemistry , RNA, Protozoan/genetics , Random Allocation , Reverse Transcriptase Polymerase Chain Reaction/veterinary
3.
Poult Sci ; 89(2): 295-302, 2010 Feb.
Article in English | MEDLINE | ID: mdl-20075282

ABSTRACT

Two experiments were conducted to 1) assess any differences on breaking force in bones with or without flesh attachment and 2) determine the effects of dietary nonphytate phosphorus (npP) concentration, maternal flock age, and chick sex on live performance and tibia strength of broilers. For experiment 1, sixty chicks were placed in battery cages and selected weekly for removal of both tibiae (15 chicks/wk). Raw flesh was either completely cut from the bone or left intact and broken using a texture analyzer. For experiment 2, Ross 708 chicks (1,220) were hatched of 25- and 65-wk-old breeder flocks, separated by sex, vaccinated, and placed on used bedding across 64 floor pens (18 males or 17 females/pen, 8 repetitions/treatment). Through 28 d, all birds were fed corn-soybean meal diets (22% CP, 3,086 kcal/kg) adequate in all nutrients but npP, which was included at either 0.35 or 0.50%. Individual BW and pen feed consumption (FC) were recorded weekly and corrected for mortality. Each week, 24 birds/treatment were killed for tibia evaluation. Experiment 1 resulted in no differences in breaking force, whether flesh remained or was removed from the bone. In experiment 2, BW was increased with an increase in npP (P<0.001) at the end of the experiment. Both BW and FC were increased (P<0.001) from 0 to 28 d of age in chicks from the 65-wk-old breeder flock. Males had increased (P<0.001) final BW, FC, and tibia breaking forces. Breaking forces were also improved (P<0.001) when npP was increased or chicks were hatched from older breeder flocks. Interactions were present (P<0.05) for npP concentrationx25-wk breeder flock 7- to 21-d BW gain (BWG) and 0- to 28-d FC, npP x chick sex 7- to 14-d BWG and 21- to 28-d feed conversion ratio, and breeder flock age x chick sex 0 d BW and 7- to 14-d BWG. These results indicate that broiler growth and performance can be affected by maternal flock age, chick sex, and dietary npP.


Subject(s)
Aging/physiology , Bone Density/physiology , Chickens/physiology , Fractures, Bone/metabolism , Muscle, Skeletal/physiology , Phosphorus/chemistry , Animal Feed/analysis , Animal Nutritional Physiological Phenomena , Animals , Diet/veterinary , Female , Male , Phosphorus, Dietary , Sex Characteristics
4.
J Virol ; 75(13): 6052-61, 2001 Jul.
Article in English | MEDLINE | ID: mdl-11390607

ABSTRACT

Trypsin enhances rotavirus infectivity by an unknown mechanism. To examine the structural basis of trypsin-enhanced infectivity in rotaviruses, SA11 4F triple-layered particles (TLPs) grown in the absence (nontrypsinized rotavirus [NTR]) or presence (trypsinized rotavirus [TR]) of trypsin were characterized to determine the structure, the protein composition, and the infectivity of the particles before and after trypsin treatment. As expected, VP4 was not cleaved in NTR particles and was cleaved into VP5(*) and VP8(*) in TR particles. However, surprisingly, while the VP4 spikes were clearly visible and well ordered in the electron cryomicroscopy reconstructions of TR TLPs, they were totally absent in the reconstructions of NTR TLPs. Biochemical analysis with radiolabeled particles indicated that the stoichiometry of the VP4 in NTR particles was the same as that in TR particles and that the VP8(*) portion of NTR, but not TR, particles is susceptible to further proteolysis by trypsin. Taken together, these structural and biochemical data show that the VP4 spikes in the NTR TLPs are icosahedrally disordered and that they are conformationally different. Structural studies on the NTR TLPs after trypsin treatment showed that spike structure could be partially recovered. Following additional trypsin treatment, infectivity was enhanced for both NTR and TR particles, but the infectivity of NTR remained 2 logs lower than that of TR particles. Increased infectivity in these particles corresponded to additional cleavages in VP5(*), at amino acids 259, 583, and putatively 467, which are conserved in all P serotypes of human and animal group A rotaviruses and also corresponded with a structural change in VP7. These biochemical and structural results show that trypsin cleavage imparts order to VP4 spikes on de novo synthesized virus particles, and these ordered spikes make virus entry into cells more efficient.


Subject(s)
Capsid Proteins , Capsid/chemistry , Rotavirus/chemistry , Trypsin/pharmacology , Amino Acid Sequence , Animals , Capsid/metabolism , Chlorocebus aethiops , Microscopy, Electron
5.
FEMS Microbiol Lett ; 190(2): 203-8, 2000 Sep 15.
Article in English | MEDLINE | ID: mdl-11034280

ABSTRACT

Expression of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter is regulated by oxygen, light intensity and availability of substrate. Since dimethylsulfoxide reductase contains a pterin molybdenum cofactor, the role of molybdate in the regulation of dor operon expression was investigated. In this report we show that the molybdate-responsive transcriptional regulator, MopB, and molybdate are essential for maximal dimethylsulfoxide reductase activity and expression of a dorA::lacZ transcriptional fusion in Rhodobacter capsulatus. In contrast, mop genes are not required for the expression of the periplasmic nitrate reductase or xanthine dehydrogenase in R. capsulatus under conditions of molybdenum sufficiency. This is the first report demonstrating a clear functional difference between the ModE homologues MopB and MopA in this bacterium. The results suggest that MopA is primarily involved in the regulation of nitrogen fixation gene expression in response to molybdate while MopB has a role in nitrogen fixation and dimethylsulfoxide respiration.


Subject(s)
Carrier Proteins , Iron-Sulfur Proteins , Membrane Transport Proteins , Molybdenum/metabolism , Oxidoreductases/genetics , Oxidoreductases/metabolism , Rhodobacter capsulatus/enzymology , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Gene Expression Regulation, Bacterial , Lac Operon/physiology , Mutation , Nitrate Reductases/metabolism , Operon/genetics , Periplasm/enzymology , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Rhodobacter capsulatus/genetics , Transcription, Genetic , Xanthine Oxidase/metabolism
6.
J Biol Chem ; 274(15): 9911-4, 1999 Apr 09.
Article in English | MEDLINE | ID: mdl-10187763

ABSTRACT

The dorC gene of the dimethyl sulfoxide respiratory (dor) operon of Rhodobacter capsulatus encodes a pentaheme c-type cytochrome that is involved in electron transfer from ubiquinol to periplasmic dimethyl sulfoxide reductase. DorC was expressed as a C-terminal fusion to an 8-amino acid FLAG epitope and was purified from detergent-solubilized membranes by ion exchange chromatography and immunoaffinity chromatography. The DorC protein had a subunit Mr = 46,000, and pyridine hemochrome analysis indicated that it contained 5 mol heme c/mol DorC polypeptide, as predicted from the derived amino acid sequence of the dorC gene. The reduced form of DorC exhibited visible absorption maxima at 551.5 nm (alpha-band), 522 nm (beta-band), and 419 nm (Soret band). Redox potentiometry of the heme centers of DorC identified five components (n = 1) with midpoint potentials of -34, -128, -184, -185, and -276 mV. Despite the low redox potentials of the heme centers, DorC was reduced by duroquinol and was oxidized by dimethyl sulfoxide reductase.


Subject(s)
Cytochrome c Group/chemistry , Iron-Sulfur Proteins , Oxidoreductases/genetics , Rhodobacter capsulatus/genetics , Cytochrome c Group/metabolism , Dithionite , Electron Transport , Electrophoresis, Polyacrylamide Gel , Ferricyanides/metabolism , Molecular Weight , Oxidation-Reduction , Oxidoreductases/metabolism , Potentiometry , Rhodobacter capsulatus/enzymology
7.
Biochim Biophys Acta ; 1276(3): 176-80, 1996 Sep 30.
Article in English | MEDLINE | ID: mdl-8856102

ABSTRACT

The dimethylsulfoxide reductase structural gene (dorA) of Rhodobacter capsulatus was cloned from a lambda expression library. The nucleotide sequence of the dorA gene was determined and it was found to encode a protein of 825 amino acids. Comparison of the deduced amino-acid sequence of DorA with N-terminal sequence of purified dimethylsulfoxide reductase from Rhodobacter capsulatus showed that the pre-protein possesses a 41-amino-acid N-terminal signal polypeptide. All of the conserved segments which have been described in bacterial enzymes which bind molybdopterin guanine dinucleotide (Berks, B.C., Ferguson, S.J., Moir, J.W.B. and Richardson, D.J. (1995) Biochim, Biophys. Acta 1232, 97-173) were identified in Rhodobacter capsulatus dimethylsulfoxide reductase.


Subject(s)
Bacterial Proteins/genetics , Genes, Bacterial , Iron-Sulfur Proteins , Oxidoreductases/genetics , Protein Precursors/genetics , Rhodobacter capsulatus/genetics , Amino Acid Sequence , Base Sequence , Cloning, Molecular , Conserved Sequence , Molecular Sequence Data , Protein Sorting Signals/genetics , Rhodobacter capsulatus/enzymology , Sequence Analysis, DNA , Sequence Homology, Amino Acid
8.
Structure ; 4(8): 957-67, 1996 Aug 15.
Article in English | MEDLINE | ID: mdl-8805574

ABSTRACT

BACKGROUND: Aquareoviruses are important pathogens of aquatic animals and have severe consequences in aquaculture. These viruses belong to the family Reoviridae. A structural feature common to members of the Reoviridae is a multilayered capsid, formed by several concentric icosahedral shells with different protein compositions. How these proteins, which often are present in unequal stoichiometries, interact between icosahedral layers to stabilize the capsid is not well understood. RESULTS: We have determined the three-dimensional structure of aquareovirus to 23 A resolution using electron cryomicroscopy and computer image analysis. The protein capsid is composed of two structurally distinct icosahedral layers: an outer layer approximately 100 A thick, with incomplete T=13 left-handed symmetry, surrounds an inner layer 600 A in diameter that has T=1 symmetry and is perforated by channels near the fivefold axes. There are 120 subunits, arranged in dimers, in the inner layer, each of which interacts with two of the 600 subunits in the outer layer. A separate set of closely interacting proteins forms the fivefold axes of the virus structure, forming continuous density throughout both layers of the capsid. Comparison of full and empty (lacking RNA) virus structures reveals an RNA shell that lies directly beneath the inner layer. CONCLUSIONS: Our aquareovirus structure displays marked similarity to the mammalian reovirus intermediate subviral particles, suggesting a close evolutionary relationship. However, the noticeable distinction is that aquareovirus lacks the hemagglutinin spike observed in reovirus. The T=1 inner layer organization observed in the aquareovirus appears to be common to other members of the Reoviridae. Such organization may be of fundamental significance in the endogenous transcription of the genome in these viruses.


Subject(s)
Capsid/ultrastructure , Reoviridae/ultrastructure , Animals , Cryopreservation , Glycoproteins/ultrastructure , Image Processing, Computer-Assisted , Microscopy, Electron/methods , Models, Biological , Salmon/virology , Viral Proteins/ultrastructure
9.
Arch Virol Suppl ; 12: 21-7, 1996.
Article in English | MEDLINE | ID: mdl-9015098

ABSTRACT

Structural studies on rotavirus using electron cryomicroscopy and computer image analysis have permitted visualization of each shell in the triple-layered rotavirus structure. Biochemical results have aided our interpretation of the structural organization of these layers and protein interactions seen in the three-dimensional structure, and have provided a better understanding of the structure-function relationships of the rotavirus structural proteins.


Subject(s)
Capsid Proteins , Capsid/metabolism , Capsid/ultrastructure , Rotavirus/metabolism , Rotavirus/ultrastructure , Humans
10.
Cell ; 74(4): 693-701, 1993 Aug 27.
Article in English | MEDLINE | ID: mdl-8395350

ABSTRACT

Three-dimensional structures of a native simian and reassortant rotavirus have been determined by electron cryomicroscopy and computer image processing. The structural features of the native virus confirm that the hemagglutinin spike is a dimer of VP4, substantiated by in vivo radiolabeling studies. Exchange of native VP4 with a bovine strain equivalent results in a poorly infectious reassortant. No VP4 spikes are detected in the three-dimensional reconstruction of the reassortant. The difference map between the two structures reveals a novel large globular domain of VP4 buried within the virion that interacts extensively with the intermediate shell protein, VP6. Our results suggest that assembly of VP4 precedes that of VP7, the major outer shell protein, and that VP4 may play an important role in the receptor recognition and budding process through the rough endoplasmic reticulum during virus maturation.


Subject(s)
Capsid Proteins , Capsid/ultrastructure , Hemagglutinins, Viral/ultrastructure , Rotavirus/ultrastructure , Animals , Capsid/biosynthesis , Cell Line , Computer Graphics , Freezing , Hemagglutinins, Viral/biosynthesis , Macromolecular Substances , Methionine/metabolism , Microscopy, Electron/methods , Models, Structural , Rotavirus/metabolism
11.
Plant Cell ; 4(4): 397-411, 1992 Apr.
Article in English | MEDLINE | ID: mdl-1379865

ABSTRACT

Cell-to-cell spread of tobacco mosaic virus (TMV) is presumed to occur through plant intercellular connections, the plasmodesmata. Viral movement is an active process mediated by a specific virus-encoded P30 protein. P30 has at least two functions, to cooperatively bind single-stranded nucleic acids and to increase plasmodesmatal permeability. Here, we visualized P30 complexes with single-stranded DNA and RNA. These complexes are long, unfolded, and very thin (1.5 to 2.0 nm in diameter). Unlike TMV virions (300 x 18 nm), the complexes are compatible in size with the P30-induced increase in plasmodesmatal permeability (2.4 to 3.1 nm), making them likely candidates for the structures involved in the cell-to-cell movement of TMV. Mutational analysis using single and double deletion mutants of P30 revealed three regions potentially important for the protein function. Amino acid residues 65 to 86 possibly are required for correct folding of the active protein, and the regions between amino acid residues 112 to 185 and 185 to 268 potentially contain two independently active single-stranded nucleic acid binding domains designated binding domains A and B, respectively.


Subject(s)
DNA, Single-Stranded/metabolism , Tobacco Mosaic Virus/metabolism , Viral Proteins/metabolism , Amino Acid Sequence , DNA Topoisomerases, Type I/metabolism , DNA, Single-Stranded/ultrastructure , DNA-Directed RNA Polymerases/metabolism , Molecular Sequence Data , Nucleic Acid Hybridization , Plant Viral Movement Proteins , Protein Binding , Protein Conformation , RNA/metabolism , RNA/ultrastructure , Sequence Alignment , Tobacco Mosaic Virus/ultrastructure , Viral Proteins/ultrastructure
12.
J Manipulative Physiol Ther ; 10(5): 257-9, 1987 Oct.
Article in English | MEDLINE | ID: mdl-3694063

ABSTRACT

A case is reported of a 55-yr-old man complaining of interscapular pain, lethargy, anorexia with weight loss and shallowness of breath following a recent traumatic blow to the abdomen. Radiographs revealed a marked and extensive aneurysm of the thoracic aorta. The importance of performing X-ray studies of the thoracic region is emphasized for all cases where histories of recent or past significant chest trauma is suspected and with older patients having hypertension and atherosclerotic heart disease.


Subject(s)
Aortic Aneurysm/diagnostic imaging , Aorta, Thoracic , Aortic Aneurysm/etiology , Humans , Male , Middle Aged , Radiography
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