AFM study of complement system assembly initiated by antigen-antibody complex

Sector of Immunoanalysis and Informatics, Institute of Immunology, Vilnius University, Moletu pl. 29, 08409 Vilnius 21, Lithuania
Central European Journal of Chemistry (Impact Factor: 1.33). 02/2006; 4(1):194-206. DOI: 10.1007/s11532-005-0015-8

ABSTRACT The shape and size of complement system C1 components assembled on a SiO2 surface after classical activation by antigen-antibody complex was determined by tapping mode atomic force microscopy (AFM).
The SiO2 substrate was silanized and bovine leukemia virus proteins gp51 were covalently bound to the SiO2 substrate. Self-assembly of complement system proteins was investigated by AFM. Uniform coating of silanized surface by gp51 proteins was observed by AFM. After incubation of gp51 coated substrate in anti-gp51 antibody containing solution, Ag-Ab complexes were detected on the substrate surface by AFM. Then after treatment of Ag-Ab
complex modified substrate by guinea-pig blood serum containing highly active complement system proteins for 3 minutes and
30 minutes features 2–3 times and 5–8 times higher in diameter and in height if compared with those observed after formation
of Ag-Ab complex, were observed respectively on the surface of SiO2. This study revealed that AFM might be applied for the imaging of complement system assembly and provides valuable information
that can be used to complement other well-established techniques.

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Available from: Almira Ramanaviciene, Jun 21, 2015
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