Attachment of Escherichia coli to Listeria monocytogenes for Pediocin-Mediated Killing

Abstract

Listeria phage endolysin cell wall-binding domain (CBD) from the Listeria phage A500 was fused with flagellar subunit FliC in Escherichia coli, aiming at binding of E. coli cells to Listeria cells, followed by enhanced killing of Listeria by pediocin production. FliC::CBD chimeric flagella were expressed and detected by Western blot. However, only few chimeric flagella could be isolated from the recombinant cells compared with sufficient amount of wild-type flagella obtained from the host cells. Interestingly, wild-type flagella extract showed capacity of binding Listeria cells. Pediocin-secreting E. coli cells with Listeria-binding flagella killed approximately 40 % of the Listeria cells, whereas cell-free spent growth medium with the same pediocin concentration only inhibited Listeria growth. These results suggested that binding the Listeria to bacteriocin-secreting cells improves killing.

Staphylococcal Biofilms: Challenges and Novel Therapeutic Perspectives

“…Consequently, it is not surprising that many of these antimicrobials have activity against bacterial species closely related to the producer, although broad-spectrum bacteriocins do exist [182,184]. Bacteriocins are broadly subdivided into three classes, depending on whether they are modified at the post-translational level (class I) or not (class II), in addition to class III bacteriocins that are a group of large (M r > 25 kDa) thermo-labile proteins [185][186][187]. Bacteriocins have gained increasing interest for their antimicrobial potency (being active in the nanomolar concentration range) and for their amenability to manipulation and bioengineering for increased target specificity, potency and improved physicochemical properties [188][189][190][191][192][193][194][195][196].…”