@article{mbs:/content/journal/jmm/10.1099/00222615-46-2-122, author = "Lun, M. T. and Raponi, G. and Amatucci, A. M. and Natali, P. G. and Fraioli, R. and Mancini, C.", title = "Characterisation and protective capacity of monoclonal antibodies elicited in mice against protein epitopes of antibiotic-exposed Escherichia coli", journal= "Journal of Medical Microbiology", year = "1997", volume = "46", number = "2", pages = "122-128", doi = "https://doi.org/10.1099/00222615-46-2-122", url = "https://www.microbiologyresearch.org/content/journal/jmm/10.1099/00222615-46-2-122", publisher = "Microbiology Society", issn = "1473-5644", type = "Journal Article", abstract = "The binding capacity and the protective activity of three monoclonal antibodies (MAbs) – ARM 1-4, ARM 1-7 and ARM 2-2 – obtained from spleen cells of mice immunised with Escherichia coli O6:K– pre-treated with sub-MIC of aztreonam were studied. The MAbs belonged to IgG1 isotype and showed different reactivity toward protein epitopes of E. coli in an immunoblotting assay. ARM 1-4 recognised epitopes on molecules of 30 kDa and 40 kDa. ARM 1-7 identified an epitope of a molecule of 41 kDa, and ARM 2-2 recognised epitopes of molecules of 15 kDa and 41 kDa. In ELISA the MAbs cross-reacted with E. coli O7:K–, E. coli O111:B4 and E. coli O128:K– with different binding affinity. Furthermore, the MAbs showed complement-dependent bactericidal activity. The MAbs displayed different protective capacities when given to mice 90 min before lethal challenges with 2 × LD50, 4 × LD50 and 8 × LD50 of E. coli strains. In all but one instance (ARM 1-4 versus E. coli O7:K–) it was not possible to correlate protective capacity with binding affinity of a MAb to a given bacterial cell. Therefore, the epitopes recognised by the MAb may be more closely associated with bacterial virulence than in binding to the bacterial cell.", }