Interactions Between Acanthamoeba culbertsoni and Pathogenic Bacteria and their Inhibition by Lectin-Antibodies

Suk-Yul Jung
2020 Journal of Pure and Applied Microbiology  
In this study, using pathogenic and non-pathogenic bacteria, it was analyzed whether a polyclonal serum and a monoclonal antibody to A. culbertsoni mannose-binding protein (MBP) could inhibit its interaction. The association of the amoeba with E. coli O157:H7 was very strong at a level of over 100%, but the non-pathogenic E. coli strain was about five times lower at 22%. Pathogenic K. pnueumoniae also showed high association with amoeba by about 92% as compared with pathogenic E. coli O157:H7
more » ... c E. coli O157:H7 and S. agalactiae. The polyclonal serum to MBP inhibited E. coli O157:H7 association to amoeba 2.5 times more than untreated E. coli O157:H7. Monoclonal antibody to MBP also inhibited bacterial association with amoeba but was not stronger than the polyclonal serum. Pathogenic E. coli O157:H7 showed about 88% invasion into amoeba and decreased about 22% as compared with associated E. coli O157:H7. Polyclonal serum to MBP inhibited about 55%, 50%, and 44% in E. coli O157:H7, K. pneumoniae and S. agalactiae, respectively. The invasion of K. pneumoniae and S. agalactiae was not high as polyclonal serum but was about 8% to 10% weaker than polyclonal serum. The pathogenic strains of K. pneumoniae and S. agalactiae showed less decrease in survival as shown at invasion than E. coli O157:H7 without antibody. This study provided the information that the pathogenic bacteria could be more interactive with A. culbertsoni trophozoites as a reservoir host than non-pathogenic E. coli, and the amoeba should interact with bacteria by the MBP lectin.
doi:10.22207/jpam.14.3.07 fatcat:op7smqgqlbg57ke3kwhbkruheq