Hospitalisation and mortality risk of SARS-COV-2 variant omicron sub-lineage BA.2 compared to BA.1 in England.

The Omicron variant of SARS-CoV-2 became the globally dominant variant in early 2022. A sub-lineage of the Omicron variant (BA.2) was identified in England in January 2022. Here, we investigated hospitalisation and mortality risks of COVID-19 cases with the Omicron sub-lineage BA.2 (n = 258,875) compared to BA.1 (n = 984,337) in a large cohort study in England. We estimated the risk of hospital attendance, hospital admission or death using multivariable stratified proportional hazards regression models. After adjustment for confounders, BA.2 cases had lower or similar risks of death (HR = 0.80, 95% CI 0.71-0.90), hospital admission (HR = 0.88, 95% CI 0.83-0.94) and any hospital attendance (HR = 0.98, 95% CI 0.95-1.01). These findings that the risk of severe outcomes following infection with BA.2 SARS-CoV-2 was slightly lower or equivalent to the BA.1 sub-lineage can inform public health strategies in countries where BA.2 is spreading.

Chatoyant: a computer-aided- design tool for free-space optoelectronic systems.

Chatoyant is a tool for the simulation and the analysis of heterogeneous free-space optoelectronic architectures. It is capable of modeling digital and analog electronic and optical signal propagation with mechanical tolerancing at the system level. We present models for a variety of optoelectronic devices and results that demonstrate the system's ability to predict the effects of various component parameters, such as detector geometry, and system parameters, such as alignment tolerances, on system-performance measures, such as the bit-error rate.

D-glyceraldehyde-3-phosphate dehydrogenase. Complete amino-acid sequence of the enzyme from Bacillus stearothermophilus.

1. The complete amino acid sequence of D-glyceraldehyde-3-phosphate dehydrogenase from the moderate thermophile Bacillus stearothermophilus has been determined. 2. This has been achieved largely by the automated sequence analysis of large fragements derived by chemical cleavage with cyanogen bromide, BNPS-skatole [the product of reaction between N-bromosuccinimide and 2-(nitrophenyl-sulphenyl)-3-methylindole] and hydroxylamine and enzymic hydrolysis with trypsin at arginine residues. 3. The sequence is as follows: (See Text). It has been numbered to maximise homology with the four complete sequences of this enzyme from other sources. Hence the N-terminal residue is numberd 0 and two deletions and two insertions have been introduced. 4. The inability of the B. stearothermophilus apo-enzyme to transfer an acyl moiety from Cys-149 to Lys-183 oberved with muscle enzymes is explained by the replacement of lysine by arginine in the enzyme from the thermophilic organism. 5. The sequences of the S-loop regions, which form the core of the tetrameric enzyme, are similar to each other in B. stearothermophilus and Thermus aquaticus and differ from the highly conserved S-loops of three enzymes from mesophiles.

The keratin chains of avian scale tissue. Sequence heterogeneity and the number of scale keratin genes.

The three major proteins of chick scale keratin were isolated as their S-carboxymethylated derivatives and shown to be similar or identical in molecular weight by gel filtration but to be distinct by amino acid analysis and gel electrophoresis. The major amino-terminal sequence of scale keratin chains was determined and shown to be highly homologous to the corresponding region of feather keratin chains. The carboxyl-terminal peptides of the three scale keratin fractions differed in sequence but were all homologous to the carboxyl-terminal segment of feather keratin chains. The pronounced concentration of cysteine residues at the amino-terminal and carboxyl-terminal segments suggested a similar role for these regions in both scale and feather keratin chains, namely to provide a disulphide-linked matrix to maintain the organisation of fibrils which arise from the internal hydrophobic segments of both types of chain. Analysis of a large hydrophobic segment from each of the three isolated protein fractions revealed that each was composed largely of repeating tripeptide units of the type Gly-Gly-X (where X = Phe, Leu or Tyr). At a few positions in each hydrophobic peptide, microheterogeneity was apparent in the sequences indicating that each isolated protein fraction was composed of at least three different chains each encoded by a different gene. A minimum of nine keratin genes are therefore expressed in scale tissue.

High sensitivity amino acid sequence determination. Application to proteins eluted from polyacrylamide gels.

An automatic solid-phase procedure is described for determining the amino-terminal amino acid sequence of very small quantities of proteins. The sample is covalently attached to an inert support so that mechanical and physical losses during sequencing are eliminated. High sensitivity is achieved by using an initial coupling with high specific activity phenyl [35S]isothiocyanate followed by a longer reaction with the unlabeled reagent. The radioactive phenylthiohydantoins are identified by autoradiography after two-dimensional thin-layer chromatography. Unlabeled phenylthiohydantoin-amino acids are added to each fraction to assist in the identification and to act as carriers, hence reducing absorptive and extractive losses of the small quantities of sample. The method may be used on proteins eluted from polyacrylamide gels containing sodium dodecyl sulfate without removal of the detergent. Sequences of up to 20 residues have been obtained on quantities of protein ranging from 2.5 to 70 pmol. Results from proteins of hitherto unknown sequence are included.

Isolation and N-terminal amino acid sequence of membrane-bound human HLA-A and HLA-B antigens.

Membrane-bound HLA-A and HLA-B antigens have been extensively purified in good yield. The sequences of the N-terminal 16 amino acids have been determined using about 1 nmol of protein eluted from polyacrylamide gel after electrophoresis in sodium dodecyl sulphate.

Isolation, characterization and partial sequence of cyanogen bromide fragments and thiol peptides from pig kidney D-amino-acid oxidase.

A partial characterization of the primary structure of D-amino-acid oxidase (D-Amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3.) from hog kidney has been achieved by a CNBr cleavage of the 14C-carboxymethylated protein. Four fragments have been isolated and purified and their alignment made possible by overlapping with methionine-containing peptides derived from tryptic digestion of the 14C-carboxymethylated protein. A partial sequencing of the CNBr fragments has been carried out by the automated Edman procedure and by manual sequence analysis. Chymotryptic peptides containing the 5 alkylated thiols of the monomer enzyme (Curti, B., Ronchi, S., branzoli, U., Ferri, G. and Williams, Jr., C. H. (1973) Biochim. Biophys. Acta 327, 266-273) have been isolated and their sequence determined. The present results do not show any significant homologies with the known sequences of other flavoproteins.

Photoreceptor protein from the purple membrane of Halobacterium halobium. Molecular weight and retinal binding site.

The apparent molecular weight of the purple membrane protein of Halobacterium halobium was found to be 20 000 by sodium dodecyl sulfate gel electrophoresis and by gel filtration in sodium dodecyl sulfate. However, the molecular weight value determined by gel filtration in 6 M guanidine was 28 000. To resolve this discrepancy, methods insensitive to or independent of the conformation of the protein were used to estimate the molecular weight. Analytical ultracentrifugation of the sodium dodecyl sulfate-protein complex, peptide mapping, and amino acid analysis all gave values of 25 000 +/- 1000, a figure in agreement with a recent x-ray study. Borohydride reduction was used to attach the retinal cofactor covalently to a lysine residue. After digestion with thermolysin, peptide maps were prepared of the protein labeled at lysine residues with [14C] succinic anhydride both before and after reduction. Comparison of the maps showed one radioactive peptide with changed mobility. This peptide was isolated and shown to have the sequence Val-Ser-Asp-Pro-Asp-Lys-Lys with only one of the two lysine residues alkylated. Solid-phase sequencing showed the succinyl group to be at position 6 and hence the retinal group to be at position 7. It was possible that a small amount of retinal was also bound to Lys-6. There was no apparent homology with the corresponding peptide of vertebrate rhodopsin. No evidence of chain heterogeneity was found by radiochemical peptide mapping and sequence analysis of peptides containing lysine residues indicating that all protein chains of purple membrane are very similar or identical.

Triose phosphate isomerase from the coelacanth. An approach to the rapid determination of an amino acid sequence with small amounts of material.

The preparation and purification of cyanogen bromide fragments from [(14)C]carboxymethylated coelacanth triose phosphate isomerase is presented. The automated sequencing of these fragments, the lysine-blocked tryptic peptides derived from them, and also of the intact protein, is described. Combination with results from manual sequence analysis has given the 247-residue amino acid sequence of coelacanth triose phosphate isomerase in 4 months, by using 100mg of enzyme. (Two small adjacent peptides were placed by homology with the rabbit enzyme.) Comparison of this sequence with that of the rabbit muscle enzyme shows that 207 (84%) of the residues are identical. This slow rate of evolutionary change (corresponding to two amino acid substitutions per 100 residues per 100 million years) is similar to that found for glyceraldehyde 3-phosphate dehydrogenase. The reliability of sequence information obtained by automated methods is discussed.