scholarly journals High COVID‐19 virus replication rates, the creation of antigen–antibody immune complexes and indirect haemagglutination resulting in thrombosis

2020 ◽  
Vol 67 (4) ◽  
pp. 1418-1421 ◽  
Author(s):  
Kevin Roe
Keyword(s):  
Virus Replication ◽  
Immune Complexes ◽  
Indirect Haemagglutination ◽  
The Creation ◽  
Antigen Antibody

Immune complexes: characteristics, clinical correlations, and interpretive approaches in the clinical laboratory.

1982 ◽  
Vol 28 (6) ◽  
pp. 1259-1271 ◽  
Author(s):  
S E Ritzmann ◽  
J C Daniels
Keyword(s):  
Immune Complex ◽  
Lupus Erythematosus ◽  
Immune Complexes ◽  
Complex Disease ◽  
Clinical Medicine ◽  
Clinical Laboratory ◽  
Therapeutic Monitoring ◽  
Serum Samples ◽  
Complement Components ◽  
Antigen Antibody

Abstract Immune-complex-mediated injury is thought to play a role in diseases such as rheumatoid arthritis, systemic lupus erythematosus, serum sickness, various infectious diseases, and malignancies. With increased appreciation of the biological and pathological significance of circulating immune complexes has come efforts to develop appropriate techniques for identifying and measuring them. Common approaches exploit such phenomena as the attachment of complement components to antigen-antibody complexes, the presence of specialized receptors for immune complexes at the surface of cells, and the ability of rheumatoid factor to bind with immune complexes. This variety of assay systems for immune complexes has yielded abstruse results in numerous human pathological conditions. Unfortunately, these results seldom correlate with one another in a given disease. Thus, use of a panel of immune complex assays has been recommended. Indirect consequences of immune complex disease may still be appraised and evaluated with some confidence in clinical medicine: measurements of C3 and C4, cryoglobulins, serum viscosity, and turbidity of serum samples. Measurement of immune complexes may be useful in diagnosis, prognosis, and therapeutic monitoring, but it is the characterization of immune complexes that holds the greatest potential for better understanding of disease mechanisms.

scholarly journals Immune reactions in polysaccharide media. The composition of the antigen–antibody complexes in the precipitin reaction

1969 ◽  
Vol 114 (1) ◽  
pp. 141-144 ◽  
Author(s):  
Krister Hellsing
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Immunoglobulin G ◽  
Immune Complexes ◽  
Aggregate Size ◽  
Precipitin Reaction ◽  
Soluble Immune Complexes ◽  
Immune Aggregates ◽  
Antigen Antibody ◽  
Free Antigen

The precipitin reaction is enhanced in the presence of polysaccharides (Hellsing, 1966). This reaction has now been studied in detail with labelled antigen (125I-labelled human serum albumin) and antibody (131I-labelled rabbit anti-albumin immunoglobulin G). The relative proportions of antigen and antibody in the precipitates are unchanged by the addition of dextran in spite of the increased precipitation. The ratio of antibody to antigen in the soluble immune complexes decreases with increasing polysaccharide concentration. This can be interpreted as a decrease in the aggregate size of the complexes. At the same time the amount of free antigen in the solution increases. The results are consistent with a decrease in solubility, primarily of the large immune aggregates, together with a shift in the equilibrium between small and large complexes. The effect is in accord with a steric-exclusion phenomenon.

scholarly journals Immune reactions in polysaccharide media. The effect of hyaluronate, chondroitin sulphate and chondroitin sulphate–protein complex on the precipitin reaction

1969 ◽  
Vol 112 (4) ◽  
pp. 475-481 ◽  
Author(s):  
Krister Hellsing
Keyword(s):  
Molecular Weight ◽  
Human Serum Albumin ◽  
Connective Tissue ◽  
Immune Complexes ◽  
Protein Complex ◽  
Chondroitin Sulphate ◽  
Pathological Conditions ◽  
Precipitin Reaction ◽  
Soluble Immune Complexes ◽  
Antigen Antibody

The influence of the connective-tissue polysaccharides hyaluronate, chondroitin 4-sulphate and a chondroitin 4-sulphate–protein complex (PP-L) from cartilage on the precipitin reaction was investigated. In a system consisting of 125I-labelled human serum albumin and the immunoglobulin G fraction from rabbit anti-albumin sera, the precipitation is greatly increased in the region of antigen excess. This effect depends on the concentration, molecular weight and configuration of the polysaccharide. The increase parallels a decrease in the amount of soluble immune complexes in the supernatant. It is suggested that the effect is due to steric exclusion of the complexes from the domains of the polysaccharides. The possibility that such a mechanism might enhance precipitation of antigen–antibody complexes in certain pathological conditions is discussed.

Detection of HBeAg/anti-HBe immune complexes in the reactivation of hepatitis B virus replication among anti-HBe chronic carriers

2008 ◽  
Vol 10 (2) ◽  
pp. 79-84 ◽  
Author(s):  
Inmaculada Castillo ◽  
Javier Bartolomé ◽  
Juan Antonio Quiroga ◽  
Juan Carlos Porres ◽  
Vicente Carreño
Keyword(s):  
Hepatitis B Virus ◽  
Hepatitis B ◽  
Virus Replication ◽  
Immune Complexes ◽  
B Virus

scholarly journals STUDIES ON ANTIGEN-ANTIBODY COMPLEXES

1971 ◽  
Vol 133 (4) ◽  
pp. 713-739 ◽  
Author(s):  
Mart Mannik ◽  
William P. Arend ◽  
Anthony P. Hall ◽  
Bruce C. Gilliland
Keyword(s):  
Immune Complexes ◽  
Disulfide Bonds ◽  
Complement Fixation ◽  
Solid Phase ◽  
Complement Components ◽  
Specific Antibodies ◽  
Optimal Function ◽  
Soluble Immune Complexes ◽  
Rapid Removal ◽  
Antigen Antibody

Solid phase immunoadsorbents were prepared by coupling antigens to agarose. With this technique specific antibodies were easily isolated in large amounts. The γG-globulin class of antibodies isolated in this manner were not denatured as judged by their normal biological half-life in rabbits. Soluble immune complexes at fivefold antigen excess were prepared from isolated specific antibodies and HSA, human λ-chains, human λG-globulins, and a Waldenström's macroglobulin as antigens. In all these preparations a characteristic immune complex was encountered that represented the smallest stable antigen-antibody union. In the HSA-anti-HSA system they were found to be AgAb2 complexes, and Ag2Ab complexes in the γG-anti-γG system. These stable complexes fixed complement ineffectively. Also, a spectrum of larger complexes was present in each system, and these complexes fixed complement effectively. With intact antibodies the disappearance curves of immune complexes from the circulation were composed of three exponential components. The immune complexes larger than AgAb2 were quickly removed from the circulation with half-lives of 0.09–0.37 hr. Their clearance was not dependent on complement components, in that depletion of complement by cobra venom factor and aggregated γG-globulin did not alter the pattern of their removal from the circulation. However, when the interchain disulfide bonds of antibodies were reduced and alkylated, the removal of the λ-anti-λ, HSA-anti-HSA, and γG-anti-γG complexes was altered. In these experiments the disappearance curves were composed of two exponential components and the rapid removal of the greater than AgAb2 complexes did not occur. The immune complexes prepared from reduced and alkylated antibodies fixed complement ineffectively. The presented data indicate that the rapid removal of circulating immune complexes, containing γG-globulin molecules as antibodies, depends primarily on the number of antibodies involved. Furthermore, complement fixation is not involved in the rapid removal of such complexes. Nevertheless, the rapid removal of immune complexes and their ability to fix complement have similarities for optimal function in that both processes require intact interchain disulfide bonds of antibodies and complexes that exceed the AgAb2 combination.

scholarly journals COMPLEMENT FIXATION IN DISEASED TISSUES

1961 ◽  
Vol 114 (5) ◽  
pp. 605-616 ◽  
Author(s):  
Peter M. Burkholder
Keyword(s):  
Guinea Pig ◽  
Immune Complexes ◽  
Complement Fixation ◽  
Rat Kidney ◽  
Membranous Glomerulonephritis ◽  
Causative Role ◽  
Glomerular Capillary ◽  
Antigen Antibody ◽  
Capillary Walls

An immunohistologic complement fixation test has been used in an effort to detect immune complexes in sections of kidney from rats injected with rabbit anti-rat kidney serum and in sections of biopsied kidneys from four humans with membranous glomerulonephritis. Sections of the rat and human kidneys were treated with fluorescein-conjugated anti-rabbit globulin or antihuman globulin respectively. Adjacent sections in each case were incubated first with fresh guinea pig serum and then in a second step were treated with fluorescein-conjugated antibodies against fixed guinea pig complement to detect sites of fixation of the complement. It was demonstrated that the sites of rabbit globulin in glomerular capillary walls of the rat kidneys and the sites of localized human globulin in thickened glomerular capillary walls and swollen glomerular endothelial cells of the human kidneys were the same sites in which guinea pig complement was fixed in vitro. It was concluded from these studies that rabbit nephrotoxic antibodies localize in rat glomeruli in complement-fixing antigen-antibody complexes. Furthermore, it was concluded that the deposits of human globulin in the glomeruli of the human kidneys behaved like antibody globulin in complement-fixing antigen-antibody complexes. The significance of demonstrating complement-fixing immune complexes in certain diseased tissues is discussed in regard to determination of the causative role of allergic reactions in disease.

Relation of Circulating Levels of Human Immunodeficiency Virus (HIV) Antigen, Antibody to p24, and HIV-Containing Immune Complexes in HIV-Infected Patients

1988 ◽  
Vol 158 (5) ◽  
pp. 1088-1091 ◽  
Author(s):  
T. M. McHugh ◽  
D. P. Stites ◽  
M. P. Busch ◽  
J. F. Krowka ◽  
R. B. Stricker ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Immune Complexes ◽  
Immunodeficiency Virus ◽  
Hiv Antigen ◽  
Antigen Antibody ◽  
Circulating Levels
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