Antimicrobial Effect of Human Serum IgA
- 1 March 1982
- journal article
- Published by Wiley in Microbiology and Immunology
- Vol. 26 (3) , 227-239
- https://doi.org/10.1111/j.1348-0421.1982.tb00174.x
Abstract
Serum IgA, IgG and colostrum secretory IgA prepared from specimens pooled from a large number of human beings were shown to have measurable levels of antibodies against Escherichia coli, Pseudomonas aeruginosa, Klebsiella Pneumoniae, poliovirus, Coxsackie B virus, echovirus and influenza virus. Serum IgA exerted a bacteriostatic effect in vitro on E. coli and P. aeruginosa, which increased in the presence of the iron-binding proteins lactoferrin and transferrin. This bacteriostasis was reduced when the iron-binding proteins were saturated with iron. Similar results were obtained with IgG and secretory IgA. The bacteriostatic effect of serum IgA was also shown in vivo, in the peritoneal cavity of mice. The effect was suppressed by iron. Iron-chelating substances, siderophores, excreted by E. coli diminished the co-operative bacteriostatic effect of serum IgA and transferrin. Siderophore production by E. coli was inhibited in the presence of serum IgA, but not when serum IgA was deprived of specific antibody by absorption with E. coli. These results indicate that serum IgA has a potent bacteriostatic effect in co-operation with transferrin or lactoferrin because of the inhibitory effect of the specific antibody on siderophore production by E. coli.Keywords
This publication has 11 references indexed in Scilit:
- Distribution of transferrin, ferritin, and lactoferrin in human tissues.Journal of Clinical Pathology, 1978
- Host resistance factors in human milkThe Journal of Pediatrics, 1973
- Bacterial Assimilation of ironCRC Critical Reviews in Microbiology, 1973
- Inhibition of Growth of Candida albicans by Iron-Unsaturated Lactoferrin: Relation to Host-Defense Mechanisms in Chronic Mucocutaneous CandidiasisThe Journal of Infectious Diseases, 1971
- Bacterial Iron Metabolism and Immunity to Pasteurella septica and Escherichia coliNature, 1969
- 2,3-dihydroxy-N-benzoylserine: Chemical synthesis and comparison with the natural productBiochimica et Biophysica Acta (BBA) - General Subjects, 1969
- Immunohistochemical localization and bacteriostatic properties of an iron-binding protein from bronchial mucus.Thorax, 1966
- A Large‐Scale Method for the Purification of Human Transferrin*Vox Sanguinis, 1961
- Über die Extraktion von Bakterien mit Phenol/WasserZeitschrift für Naturforschung B, 1952
- Preparation and Properties of Serum and Plasma Proteins. IV. A System for the Separation into Fractions of the Protein and Lipoprotein Components of Biological Tissues and Fluids1a,b,c,dJournal of the American Chemical Society, 1946