Abstract
Abstract The research aims to develop and characterize monoclonal antibodies(MAbs) with high specificity and affinity for surface antigens of all major serotypes of Listeria monocytogenes(L. monocytogenes). Hybridomas were produced using extraction of L. monocytogenes surface protein as the immunogen. Detected by enzyme-linked-immunosorbent assay (ELISA), MAb1B10 was capable of binding to cell-surface antigens of live L. monocytogenes. MAb1B10, 2C10 and 1G3 reacted with both formalin-inactivated and heat-killed L. monocytogenes without any cross reactions with other Listeria spp.; MAb1C10 and 3G8 highly reacted with L. monocytogenes, L. innocua and L. welshimeri, but seldom reacted with non-Listeria spp.. Immunoprecipitation-mass spectrometry (IP-MS) and western blot were applied to convince that the reactive epitope was on the MurA protein of 72kDa. Recombinant MurA protein produced in Escherichia coli was confirmed to be the antigen which was recognized by MAb1B10, 2C10 and 1G3. To sum up, MAbs reacting with live L. monocytogenes, formalin-inactivated and heat-killed L. monocytogenes were produced. The results indicated that MurA could be exploited as a marker for specifically identifying pathogenic L. monocytogenes in suspect food samples.
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