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Immunology & Immunological Disorders Poster Session






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Activation and Deposition of Human Breast-milk Complement C3 Opsonins on a Serum Sensitive Bacteria

Ogundele, M.O. (Dept. of Immunology, Gerog-August University Goettingen, Germany)

Contact Person: Michael O. Ogundele (mogundel@yahoo.com)


Abstract

There has been much controversy about the physiological significance of secretory complement components in human breast-milk, as well as in other biological fluids. The presence of very low concentrations of native proteins in comparison to serum, wide variety of prominent 'anti-complement' factors and other non-specific anti-inflammatory agents in the body secretions, lack of standardized methods, have been some of the reasons for the drawbacks in further research into this field. In the present study, the ability of a serum sensitive Escherichia coli to activate the complement components of the human breast-milk was assessed in-vitro. The consequent deposition of C3 fragments, C3b, iC3b and C3dg, on the bacteria was analysed. Colostrum and transitional milk samples from voluntary lactating donors were obtained. A slight modification of a standard ELISA technique for the assessment of activated C3 fragments was utilized. The deposition C3 fragments, C3b, iC3b and C3dg, from HBM, identified by the antibody I3/15, were demonstrated on the killed serum susceptible bacteria, Escherichia coli NCTC 8007, serotype 0111 K58(B4) H2. Differences were observed between the deposition of the opsonins in the presence of different buffers, and between whole- and de-fatted-milk samples.

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Poster Number PAogundele0177
Keywords: Complement system, bacteriolysis, human breast-milk, opsonin, milk fat globule


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Ogundele, M.O.; (1998). Activation and Deposition of Human Breast-milk Complement C3 Opsonins on a Serum Sensitive Bacteria. Presented at INABIS '98 - 5th Internet World Congress on Biomedical Sciences at McMaster University, Canada, Dec 7-16th. Available at URL http://www.mcmaster.ca/inabis98/immunology/ogundele0177/index.html
© 1998 Author(s) Hold Copyright