Updated project metadata. The plasma membrane (PM) protects cells from extracellular threats and supports cellular homeostasis. Some pathogens produce pore-forming toxins (PFTs) that disrupt PM integrity by forming transmembrane pores. High PFT concentrations cause massive damage leading to cell death and facilitating infection. Sub-lytic PFT doses activate repair mechanisms to restore PM integrity, support cell survival and limit disease. Shedding of extracellular vesicles (EVs) was proposed as a mechanism to eliminate PFTs pores and restore PM integrity. We show here that indeed PFTs are at least partially eliminated through EV release and hypothesized that proteins important for PM repair might be included in EVs shed by cells during repair. To identify new PM repair proteins, we collected EVs released by cells challenged with sub-lytic doses of two different PFTs, Listeriolysin O and Pneumolysin, and determined their proteomic repertoire by LC-MS/MS analysis. Intoxicated cells release similar EVs irrespectively of the PFT used. Also, they release more and larger EVs than non-intoxicated cells. A cluster of 76 proteins including calcium-binding proteins, molecular chaperones, cytoskeletal, scaffold and membrane trafficking proteins, was detected enriched in EVs collected from intoxicated cells. While some of these proteins have well-characterized roles in repair, the involvement of others requires further studies. We reveal here new proteins potentially involved in PM repair and give new insights into common mechanisms and machinery engaged by cells in response to PM damage.