Clumping Of Erythrocytes Research Articles

Pfizer, Moderna and Janssen vaccine InflammoThrombotic and Prion Type Effect on Erythrocytes When Added to Human Blood

Background: Three EUA approved drug vaccine biologics have been approved for use by the United States Food and Drug Administration (FDA) for SARS-CoV-2. Their effect upon erythrocytes has not previously been reported. Methods: Seven individuals (4 men; 3 women) including two people with prior SARS-CoV-2 infections, one previously vaccinated with the Pfizer vaccine (two doses), and one previously vaccinated with the Moderna vaccine (three doses including one booster) provided blood drawn by venipuncture for analysis. In the first part of the study, one male subjected provided blood by venipuncture analysis. This blood was microscopically analyzed before and after the administration of the Pfizer BioNTech vaccine and normal saline. In the second part of the study, 3 men and 3 women provided blood samples obtained by venipuncture. Each of the individual’s blood was directly examined microscopically before and after administration of the Pfizer, Moderna, and Janssen vaccines to the blood. In the third part of the study the vaccines were independently analyzed for extraneous material. Results: Seven individuals including 4 men and 3 women showed normal erythrocyte coloration when their blood was drawn by venipuncture. Each individual’s blood when analyzed microscopically demonstrated normal morphology and appearance. In each instance, the administration of the Pfizer, Moderna, or Janssen vaccines directly into the blood on peripheral blood smear demonstrated an almost immediate loss of red color. This loss of red color persisted throughout the examination and was only seen where the vaccines mixed with erythrocytes. As the vaccines spread across the blood smear, the erythrocytes demonstrated (a) a loss of red color that was not transient, (b) clumping of erythrocytes not observed during the same time period following the administration of normal saline to the blood, and (c) alterations in the morphology of erythrocytes. While several of the vials had extraneous material; none of them had evidence of significant graphene oxide, living organisms, or nanotechnology. Conclusion: Administration of Pfizer, Moderna, and Janssen vaccines resulted in the immediate loss of red coloration present in erythrocytes. This loss of red coloration indicates that there is a disruption of the hemoglobin binding of oxygen. Since atmospheric oxygen is immediately available to re-saturate the hemoglobin molecules restoring the red color responsible for the function and name of erythrocytes; the results of this investigation suggest that there is an alteration in the hemoglobin molecule preventing the hemoglobin from binding with oxygen. This alteration of the hemoglobin molecule could be explained if the vaccines merge with the erythrocytes and release their genetic material (RNA or DNA) directly into the erythrocytes; having a prion altering effect upon the hemoglobin molecule. Some of the vaccine samples included extraneous materials. The vaccines did not include observable graphene oxide, eggs or living organisms.

Pharmacological properties of biogenically synthesized silver nanoparticles using endophyte Bacillus cereus extract of Berberis lyceum against oxidative stress and pathogenic multidrug-resistant bacteria

The emergence of multidrug resistance in pathogenic bacteria limits the utilization of available antibiotics. The development of alternate options to treat infectious diseases is the need of the day.The present study was aimed to synthesize, characterize and evaluate the bioactive properties of silver nanoparticles. Endophytic bacterium Bacillus cereus (MT193718) isolated from Berberis lycium was used to synthesize biocompatible silver nanoparticles. Antibacterial properties of AgNPs were evaluated against clinically isolated multidrug-resistant strains of Staphylococcus aureus, Pseudomonas aeruginosa, Acinetobacter baumannii and Klebsiella pneumoniae. AgNPs indicated significant antibacterial activity against S. aureus and K. pneumoniae fwith a zone of inhibition of 17 and 18 mm at a concentration of 1000 µg/ mL with minimum inhibitory concentration of 15.6 and 62.5 µg/mL respectively. Significant antioxidant activity with an IC50 value of 9.5 µg/mL was recorded. Biosynthesized AgNPs were found compatible with red blood cells at a concentration of 31.5 µg/ml with no clumping of erythrocytes. The study suggested that AgNPs synthesized by the endophytic bacterium Bacillus cereus are biologically active and can be used as antioxidant and antibacterial agents against drug-resistant bacteria.

Arginine is a Common Ligand for Haemagglutination and Protein Binding by Organisms Inhabiting Mucosal Surfaces

Treponema denticola, T. vincentii and T. socranskii can be added to the diverse group of oral organisms which haemagglutinate via surface receptors that bind proteins and peptides. Model peptides and selective chemical modification of arginyl or lysyl residues of protein ligands showed that for both Porphyromonas gingivalis and oral Treponema , binding involves predominantly arginyl and some lysyl residues. We have previously identified a relationship between protein binding, proteolytic activity and haemagglutination in P. gingivalis and were able to extend this finding to oral Treponema . Oral spirochaetes have both trypsin-and chymotrypsin-like proteases and peptidases and their haemagglutinins are blocked by both trypsin and chymotrypsin inhibitors. The narrow specificity of haemagglutination by these protein-and peptide-binding organisms allows a variety of dissimilar proteins in the oral environment to block haemagglutination. Possession of arginyl-directed haemagglutinins by both the non-motile P. gingivalis and the motile Treponema indicates that adherence to oral surfaces must involve additional mechanisms beyond those demonstrated by in vitro clumping of erythrocytes. The bulky structure and intense charge of the guanidinium group of arginine appear to make this ammo acid residue an 'ideal' ligand in the mucosal environment. Binding of proteins via the guanidinium group of arginine is a widely-occurring adaptation among different species of oral microbes. Agents such as chlorhexidine that also possess guanidinium groups would interfere with the central role of arginine as a ligand involved in a variety of binding reactions exhibited by bacteria inhabiting mucosal surfaces. Keywords: Porphyromonas gingivalis , Treponema denticola, T. vincentii, T. socranskii , haemagglutination, protein binding, arginine, lysine, guanidinium, oral mucosa, adherence.

赤血球計算希釈液の検討

1. When Hayem's solution containing 0-1.0% HgCl2 was used in microscopical examination the blood, clumps of erythrocytes appeared more of less in all kinds of animals. They were very large in number in the blood of goats, not so large in that of sheep and swine, and very small that of horses, cattle, and dogs.2. It was thought that such clump had been caused in the diluted blood of horses and cattle mainly by some factors existing in the blood plasma and in that of sheep, goats, swine, and dogs by some factors in the erythrocytes.3. There were the following relations between the concentration of HgC12 in Hayem's solution and the species of animals in which hemolysis occurred when such solution had been used as diluent: under 0.25% in cattle, under 0.05% horses and dogs, and under 0.01% in goats, sheep, and swine.4. Taking the clumping of erythrocytes and hemolysis into consideration, the optimum concentrations of HgC12 in Hayem's solution are as fallows; 0.25-1.0% for horses and dogs, 0.5% for cattle, and 0.05% for sheep, goats, and swine.5. No clumping occurred in physiologic saline solution at all, but hemolysis appeared in the blood diluted with this solution in all domestic animals examined in a short time. Therefore, physiologic saline solution cannot be a suitable diluent for erythrocytes of domestic animals.6. When blood was diluted with Gowers' solution, no clumping nor hemolysis occurred for 24 hours. So, this solution can be recommended as a satisfactory diluent.7. Toisson's solution caused no clumping but sometimes hemolysis especially in swine.

Development of Cold Agglutinins in Atypical Pneumonia

IN addition to the classical iso-agglutinins that delineate the four primary blood groups of man, there exist in many normal sera other substances which may cause clumping of erythrocytes and are called 'cold' agglutinins because in most instances their action appears at low temperatures only. Specific cold agglutinins, concerned with the sub-groups of type A blood, have been distinguished1. The cold agglutinins are, however, otherwise considered to be non-specific inasmuch as they will produce clumping of all human red blood cells irrespective of group. Moreover, since they likewise affect the cells of the individual in whose serum they appear, they are sometimes named auto-agglutinins. The reaction is delicate and usually disappears when the serum is diluted beyond 1: 10. Cold agglutinins of this type have attracted attention from time to time when existing in quantity enough to be manifest even at room temperature and so interfere with the crossmatching of bloods for transfusion. Such occasions are still rare enough to warrant reports of single cases of their occurrence. McCombs and McElroy found in the literature thirty-eight instances2. Among these were represented diseases as varied as cirrhosis of the liver, trypanosomiasis and pneumonia. With the exception of paroxysmal haemoglobinuria, which occupies a unique position, there would seem to be no regularity in the behaviour of cold agglutinins in disease, although it may be pointed out that systematic clinical and serological investigation of the subject has been neglected.

FAULTY BLOOD GROUPING DUE TO AUTO-AGGLUTININS: AN UNUSUAL CASE

For many years, serologists have been interested in the comparatively rare phenomenon of auto-agglutination. This has been quite clearly defined by Boxwell and Bigger 1 in the following simple sentence: Autohemagglutination is a clumping of erythrocytes into irregular masses, visible to the naked eye, occurring in the presence of the individual's own serum, without bacterial action, at air temperature and reversible at body Landsteiner, 2 Clough and Richter, 3 Li Chen-Pien 4 and other investigators have shown that the auto-agglutinins are present in the blood serum and are dependent on a lower than body temperature. They are absorbed from the serum at low temperature and fixed to the red blood cells. The auto-agglutinins can then be freed from the red cells by washing and suspending in warm saline solution, in which solution they can be demonstrated. The case reported here is the first instance in our experience in which