NONSPECIFIC FACTORS OF ORGANISM RESISTANCE IN PATIENTS WITH ERYSIPELAS

Summary. Aim. The article is aimed to assess the nonspecific factors of the body’s resistance in patients with erysipelas and in the development of sepsis in these patients. Materials and methods. 114 case histories of patients who underwent inpatient treatment in the center of purulent-septic surgery in the Non-profit municipal enterprise “City Hospital № 3” in Zaporizhzhia for the period 2019-2020 were analyzed. According to the forms of the disease, the patients were distributed as follows: erythematous — 24 (21.0 %), bullous — 28 (24.6 %), phlegmonous — 48 (42.1 %), necrotic — 14 (12.3 %). Recurrent cases of the disease were noted in 21 patients. From them: with erythematous form — 4 (16.7 %), bullous — 5 (17.9 %), phlegmonous — 9 (18.7 %), necrotic — 3 (21.4 %). Among 10 patients, the disease was complicated by sepsis. 6 patients died, mortality was 60 %. Results and their discussion. Depending on the detected disorders, the patients were divided into three groups: with uniformly activated immune status; with a suppressive type of immune response; with a mixed type of immune status, where with a normal or suppressive cellular link of immunity, activation of some indicators of the humoral link against the background of a normal or reduced level of complement is determined, which indicates the sensitization of T-cell populations with an antigen and the development of autoimmune processes. Conclusions. An increase in complement levels is an indicator of active antigen-antibody binding reactions in patients with erysipelas. Weak NBT-reaction in patients with sepsis indicates depletion of the enzymological activity of neutrophilic leukocytes and, to some extent, can serve as a predictor of a lethal outcome. An increase in the rates of phagocytosis is a prognostically favorable sign indicating the effective removal of the antigenic material of immune complexes from the patient’s body.

Bacterial expression and purification of functional recombinant SARS-CoV-2 spike receptor binding domain

The COVID-19 pandemic caused by SARS-CoV-2 has applied significant pressure on overtaxed healthcare around the world, underscoring the urgent need for rapid diagnosis and treatment. We have developed a bacterial strategy for the expression and purification of the SARS-CoV-2 spike protein receptor binding domain using the CyDisCo system to create and maintain the correct disulfide bonds for protein integrity and functionality. We show that it is possible to quickly and inexpensively produce functional, active antigen in bacteria capable of recognizing and binding to the ACE2 (angiotensin-converting enzyme) receptor as well as antibodies in COVID-19 patient sera.

Dynamics of the Autoimmune Response as Specific Differentiation Programs of T-cells in Multiple Sclerosis

Systems of characterization of antigeniciy implicate active antigen differentiation in terms of the system biology of response to progressive cell injury. Subset incorporation employs active diversification of dysequilibrating sub-populations of given profile exposure of epitope recognition in specific establishment of an immune response. The diversification of such immune responses permit the potential establishment, paradoxicity of systems of adaptation as central to active cell differentiation. Incorporation of injury within the dynamics of evolving epitope exposure guarantee the propagation of the initial establishment of the auto-antigen response within working fabric of a differentiation set of operative interventions in terms of ongoing establishment as specific progression hallmarks of autoimmune disease potentiation

Monoclonal IgG antibodies generated from joint-derived B cells of RA patients have a strong bias toward citrullinated autoantigen recognition

Antibodies targeting citrullinated proteins (ACPAs [anticitrullinated protein antibodies]) are commonly found in patients with rheumatoid arthritis (RA), strongly associate with distinct HLA-DR alleles, and predict a more aggressive disease course as compared with seronegative patients. Still, many features of these antibodies, including their site of production and the extent of MHC class II–driven T cell help, remain unclarified. To address these questions, we have used a single B cell–based cloning technology to isolate and express immunoglobulin (Ig) genes from joint-derived B cells of active RA patients. We found ∼25% of synovial IgG-expressing B cells to be specific for citrullinated autoantigens in the investigated ACPA+ RA patients, whereas such antibodies were not found in ACPA− patients. The citrulline-reactive monoclonal antibodies did not react with the unmodified arginine peptides, yet several reacted with more than one citrullinated antigen. A role for active antigen selection of the citrulline-reactive synovial B cells was supported by the strong bias toward amino acid replacement mutations in ACPA+ antibodies and by their loss of reactivity to citrullinated autoantigens when somatic mutations were reverted to the corresponding germline sequences.

Comparative cellular immune response study of anthraxin prepared by a modified method with antigens extracted from Bacillus anthracis

The study was aimed to comparison of anthraxin prepared by a modifiedmethod from cell-wall extract of avirulent B .anthracis strain 34F2(Sterne)with antigens extracted from the same strain as 1/40 antigen, autoclaved 1/40and the crude toxin. These antigens were compared on their induction of cellmediatedimmunity (CMI) in guinea pigs. Animals were immunized andboosted subcutaneously with the Sterne live veterinary anthrax vaccine. Twoweeks after the booster dose, animals were skin-tested with the four antigens.Anthraxin was the most active antigen which recorded 16.66 mm a mean oferythema and 2.3 mm a difference of skin thickness after 24 hours. Both 1/40and autoclaved 1/40 antigens gave approximately the same results whichwere 12.5 mm as a mean of erythema and 2.25 mm skin thickness for thefirst one; and 12.8mm ,1.66mm for the other respectively. The toxin showedthe lowest results of erythema 7.8 mm with edema. These antigens were alsocompared according to the histological changes on their sites of inoculation.Marked (typical) picture of delayed type of hypersensitivity (DTH) reactionwas occurred for anthraxin

Insulin Resistance Is Unrelated to Circulating Retinol Binding Protein and Protein C Inhibitor

Context: Recent data suggest that circulating retinol-binding protein (RBP) might be involved in the pathogenesis of insulin resistance. Moreover, protein C inhibitor (PCI), which specifically binds retinoic acid, was found to be increased in myocardial infarction survivors who are also insulin resistant. Objective: The objective of this study was to investigate the association of insulin resistance with RBP factors and PCI active antigen. Design and Setting: This was a clinical study. Patients: Nondiabetic humans with high (IS; n = 20, 14 females, six males, aged 47.2 ± 1.9 yr, body mass index 26 ± 1 kg/m2) and low (IR; n = 20, 14 females, six males, aged 45.5 ± 1.7 yr, body mass index 28 ± 1 kg/m2) insulin-stimulated glucose-disposal (M) participated in this study. Main Outcome Measures: M was measured by 2-h hyperinsulinemic (40 mU·min−1·m−2)-isoglycemic clamp tests. Measurements of RBP were performed using a nephelometric method and validated using quantitative Western blotting. Results: M (80–120 min) was higher in IS (10.9 ± 0.6 mg·min−1·kg−1) than IR (4.0 ± 0.2; P < 10−12). Fasting plasma RBP concentrations were comparable between IS and IR measured by both nephelometry (IS: 4.4 ± 0.3; IR: 4.6 ± 0.3 mg/dl, P = 0.6) and quantitative Western blot (IS 7.9 ± 0.5, IR 8.3 ± 0.6 mg/dl; P = 0.6). Fasting plasma PCI active antigen was similar in both groups. Plasma RBP and PCI were not significantly related to M. RBP was positively correlated with uric acid (r = 0.488, P = 0.003), triglycerides (r = 0.592, P < 0.001), prealbumin (r = 0.63, P < 0.0001), and vitamin A (r = 0.75, P < 10−6). Conclusions: Our data demonstrate that healthy, insulin-resistant humans do not show altered plasma retinol binding factors, such as RBP and PCI. Both do not significantly correlate with insulin sensitivity. Thus, our findings do not support the hypothesis of insulin sensitivity modulation by proteins involved in retinol transport.