Staphylococcus aureus is a pathogen that utilizes a family of pore-forming toxins, leukocidins, to evade the host immune response and promote infection. Among these is leukocidin AB (LukAB), which engages host receptors to initiate pore formation on the host cell. The established cellular receptor for LukAB is CD11b. This study intoxicated CD11b-deficient cells with an alanine scanning library of CC8 LukAB to identify mutations that enable LukAB to exhibit full cytotoxicity in the absence of CD11b to understand the role of CD11b in the LukAB pore-forming process. 30 mutations primarily localized in the stem domains of LukA and LukB were found that enabled LukAB to exhibit full cytotoxicity in the absence of CD11b. Crosslinking, electron microscopy, and hydroxyl radical protein footprinting were used to determine that these mutations caused an increase in the solvent accessibility of the stem domain, priming LukAB for oligomerization. The dataset includes mass spectrometry data.