Activation of the alternative pathway of complement in human serum byPropionibacterium acnes (Corynebacterium parvum) cell fractions

Inflammation ◽  
1981 ◽  
Vol 5 (2) ◽  
pp. 165-176 ◽  
Author(s):  
Guy F. Webster ◽  
Ulf R. Nilsson ◽  
William P. McArthur
Keyword(s):  
Human Serum ◽  
Alternative Pathway ◽  
Corynebacterium Parvum ◽  
Alternative Pathway Of Complement ◽  
Cell Fractions

Activation of the alternative pathway of complement by human serum IgA

1987 ◽  
Vol 17 (3) ◽  
pp. 321-326 ◽  
Author(s):  
Pieter S. Hiemstra ◽  
Arko Gorter ◽  
Marly E. Stuurman ◽  
Leendert A. Van Es ◽  
Mohamed R. Daha
Keyword(s):  
Human Serum ◽  
Alternative Pathway ◽  
Serum Iga ◽  
Alternative Pathway Of Complement

scholarly journals Studies on neutralization of human serum bactericidal activity by sodium amylosulfate

1977 ◽  
Vol 6 (2) ◽  
pp. 128-131
Author(s):  
W H Traub
Keyword(s):  
Human Serum ◽  
Bactericidal Activity ◽  
Complement Activation ◽  
Alternative Pathway ◽  
Magnesium Ions ◽  
Tetraacetic Acid ◽  
Blood Samples ◽  
Serum Bactericidal Activity ◽  
Alternative Pathway Of Complement

The synthetic anticoagulant sodium amylosulfate (SAS) at concentrations of 125 to 2,000 microgram/ml failed to completely neutralize the bactericidal activity of 80 and 50% (by volume) fresh human serum. Furthermore, SAS failed to inhibit the alternative pathway of complement activation in 80% (by volume) fresh human serum that had been chelated with 0.01 M magnesium ions plus 0.01 M ethyleneglycol-bis(beta-aminoethylether)-N,N-tetraacetic acid. However, SAS at 250 to 1,000 microgram/ml effectively neutralized the bactericidal activity of 20% (by volume) fresh human serum. Therefore, SAS (at 250 to 1,000 microgram/ml) should be used only in blood samples that have been diluted at least fivefold (less than or equal to 20% [by volume]) in suitable broth media.

scholarly journals Complement Protein C3 Binding to Mycobacterium tuberculosis Is Initiated by the Classical Pathway in Human Bronchoalveolar Lavage Fluid

2004 ◽  
Vol 72 (5) ◽  
pp. 2564-2573 ◽  
Author(s):  
J. Scott Ferguson ◽  
Jeremy J. Weis ◽  
Jennifer L. Martin ◽  
Larry S. Schlesinger
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Bronchoalveolar Lavage ◽  
Human Serum ◽  
Alveolar Macrophages ◽  
Bronchoalveolar Lavage Fluid ◽  
Alternative Pathway ◽  
Lavage Fluid ◽  
Classical Pathway ◽  
Complement Protein ◽  
Alternative Pathway Of Complement

ABSTRACT In high concentrations of fresh nonimmune human serum, Mycobacterium tuberculosis activates the alternative pathway of complement and binds C3 protein, resulting in enhanced phagocytosis by complement receptors on human alveolar macrophages. Yet in the lung, the alternative pathway of complement is relatively inactive compared to the classical pathway. To begin to determine whether C3 opsonophagocytosis of M. tuberculosis by alveolar macrophages can occur in the lung of the immunologically naive host, we characterized the binding of C3 to M. tuberculosis in different concentrations of fresh nonimmune human serum and concentrated human bronchoalveolar lavage fluid. Here we show that in human serum, C3 binding to M. tuberculosis is rapid, initiated by either the alternative pathway or the classical pathway, depending on the concentration of serum, and occurs by covalent linkages between the bacterial surface and the C3 cleavage products, C3b or C3bi. Human bronchoalveolar lavage fluid contains C3 protein and functional classical pathway activity that mediates the binding of C3 to the surface of M. tuberculosis. These studies provide evidence that when M. tuberculosis is first inhaled into the lungs of the human host, the bacterium is opsonized by C3 cleavage via classical pathway activation within the alveolus, providing a C3-dependent entry pathway into resident alveolar macrophages.

scholarly journals The binding of complement component C3 to antibody-antigen aggregates after activation of the alternative pathway in human serum

1981 ◽  
Vol 195 (2) ◽  
pp. 471-480 ◽  
Author(s):  
K J Gadd ◽  
K B M Reid
Keyword(s):  
Human Serum ◽  
Heavy Chain ◽  
Alternative Pathway ◽  
Complement Component ◽  
Amide Bond ◽  
Alpha Chain ◽  
Complement Component C3 ◽  
Alternative Pathway Of Complement ◽  
Immune Aggregates ◽  
Covalently Bound

Preformed immune aggregates, containing antigen and either IgG (immunoglobulin G) or F(ab')2 rabbit antibody, were incubated with normal human serum under conditions allowing activation of only the alternative pathway of complement. Both the IgG and F(ab')2 immune aggregates bound C3b, the activated form of the complement component C3, in a similar manner, 2-3% of the C3 available in the serum being bound to the aggregates as C3b, and the rest remaining in the fluid phase as inactive C3b or uncleaved C3. It was found that the C3b was probably covalently bound to the IgG in the aggregates, since C3b-IgG complexes could be demonstrated on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, after repeated washing with buffers containing high salt or boiling under denaturing conditions. Incubation of the C3b-antibody-antigen aggregates in buffers known to destroy ester linkages had little effect on the C3b-IgG complexes, which suggested that C3b and IgG might be linked by an amide bond. Two main types of C3b-IgG complexes were found that had apparent mol.wts. of 360000 and 580000, corresponding to either one to two C3b molecules respectively bound to one molecule of antibody. On reduction of the C3b-IgG complexes it was found that the beta-chain, but not the alpha'-chain, of C3b was released along with all the light chain of IgG but only about half or less of the heavy chain of IgG. These results indicate that, during activation of the alternative pathway of complement by immune aggregates containing IgG antibody, the alpha'-chain of C3b may become covalently bound at one or two sites in the Fd portion of the heavy chain of IgG.

Recruitment of properdin by bi-specific nanobodies activates the alternative pathway of complement

2020 ◽  
Vol 124 ◽  
pp. 200-210 ◽  
Author(s):  
Dennis V. Pedersen ◽  
Thies Rösner ◽  
Annette G. Hansen ◽  
Kasper R. Andersen ◽  
Steffen Thiel ◽  
...  
Keyword(s):  
Alternative Pathway ◽  
Alternative Pathway Of Complement
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