One solution to this developing resistance problem is utilizing virulence inhibitors, which convert pathogenic organisms to benign ones by disarming them of their virulence. Many virulence inhibitors target external molecules or effectors, which can evade the development of antibacterial resistance caused by diminished permeability (where antibiotics become impermeable to the bacterial membrane as bacteria close protein channels) . In addition, it has been theorized that even when bacteria develop resistance to anti-virulents, it often results in nonfunctional virulent systems . Another benefit to virulence inhibitors is the relative lack of impact on the patient's microbiome: while traditional antibiotics often target both pathogenic and helpful bacteria, disarming the secretion system virtually exclusive to harmful gram-negative bacteria keeps intestinal flora intact and likely reduces gastrointestinal side effects . Salmonella, like many other gram-negative bacteria (Bordetella spp., Burkholderia spp., Chlamydia spp., Escherichia coli, Pseudomonas aeruginosa, Shigella spp., Vibrio cholerae, and Yersinia spp), utilizes the Type 3 Secretion System (T3SS) to secrete its bacterial effectors into the eukaryotic cell . The T3SS is a protein complex comprising over 20 different conserved proteins, creating a channel from the bacterial cell to the host cell , allowing it to "inject" bacteria effectors using a needle-like apparatus known as an injectosome . The T3SS contains 3 types of proteins: structural proteins, which form the body of the apparatus; translocators, which translocate the virulence factors into the host cells; and the effectors, which promote bacterial invasion and survival in the host cell . Its two continuous rings pass through the bacterial inner membrane, outer membrane, and peptidoglycan layer, anchoring the needle to the cell membrane. The structural apparatus contains the cytoplasmic complex, the export apparatus, the basal body, and the 2.5 nm needle (Figure ). To secrete the effectors, chaperone proteins form complexes with substrates, which are loaded onto free cytoplasmic complexes. SctK, SctQ, and SctL, specifically, are known as the "sorting platform" because of their involvement in recruiting chaperone-substrate complexes . The sorting platform then "unfolds" the effectors to "de-chaperone" them, and the ATPase in the cytoplasmic complex works with the export apparatus to guide and power the secretion of effector proteins through the needle . Effectors are passed through the translocon, which forms pores on the host cell membrane through the needle tip . This signals increased bacterial invasion and promotes bacterial survival, thus killing the host cell .