Neisseria meningitidis is the bacterial causative agent of invasive meningococcal disease (IMD). The rate of IMD in Australia is increasing, with 2017 showing the highest infection rates since 2007. Macrophage infectivity potentiator (Mip) proteins exhibit peptidyl-prolyl cis/trans isomerase activity and are found in a wide range of pathogens. N. meningitidis encodes for two putative Mip-like proteins, which is uncommon in comparison to other pathogens which encode for a single Mip protein. Previous work has shown presence of one Mip protein to be important for survival of N. meningitidis in whole human blood. It is hypothesised both Mip-like proteins encoded by N. meningitidis are important novel anti-virulence targets. Three insertional deletion mutants have been created in the N. meningitidis strain NMB; two single mutants, each lacking one of the two putative Mip proteins (NMB∆mip1 and NMB∆mip2), and one double mutant (NMB∆mip1∆mip2), lacking both putative Mip proteins. All three mutant strains have been assessed for growth at sub-optimal temperatures and survival within a range of host cells. Deletion of the putative Mip proteins has resulted in decreased survival of N. meningitidis at high temperatures. Adhesion of mutant strains to host epithelial cells is also impaired, with attachment rates of NMB∆mip1, NMB∆mip2 and NMB∆mip1∆mip2 decreased by 50%, 30% and 53% respectively, when compared to the control strain NMB. Reduced survival of mutant strains is observed in macrophages, with survival of NMB∆mip1, NMB∆mip2 and NMB∆mip1∆mip2 decreased by 69%, 79% and 91% respectively. Both recombinant Mip1 and Mip2 proteins are correctly folded and enzymatically active. This indicates both Mip-like proteins are important in N. meningitidis to resist macrophage killing, epithelial cell attachment and survival, as well as growth at sub-optimal temperatures. Mip-like proteins represent important anti-virulence targets in N. meningitidis.