Pasteurella lipoprotein E interacts with host ABCF2 to facilitate adhesion and cell apoptosis.

Pasteurella multocida can cause serious diseases in many animal species and humans, yet the mechanisms of its pathogenesis remain to be elucidated. In this study, we found that the lipoprotein E (PlpE) of P. multocida contributed to bacterial adhesion to host cells. Through turboID-based proximity labeling screening, we identified ATP-binding cassette sub-family F member 2 (ABCF2) as a host-interaction protein for PlpE, and Asp-123 in PlpE was identified as the crucial amino acid residue for the interaction. Knocking out ABCF2 significantly reduced the adhesion of P. multocida to host cells. Additionally, we demonstrated that P. multocida infection upregulated the expression of host ABCF2 by activating the NF-κB signaling. Furthermore, we showed that ABCF2 was involved in the P. multocida-induced p53-dependent apoptotic signaling pathway. To the best of our knowledge, this is the first identification of ABCF2 as a host factor contributing to the adhesion of P. multocida and only the second report of ABCF2's involvement in bacterial pathogenesis.