Solute carrier family 11 member a1 (Slc11a1) also known as natural resistance-associated macrophage protein 1 (NRAMP1) is a proton/divalent cation antiporter, known for its role in regulating the antimicrobial activity of macrophages¹. The structure of Slc11a1 includes a common and conserved hydrophobic core of 10 transmembrane domains (TM) and either one or two non-conserved, highly hydrophobic TM domains⁴.

Slc11a1 delivers divalent cations such as Fe²⁺, Zn²⁺, and Mn²⁺ from the cytosol to the late endosome/lysosome acidic compartments where the Fenton reaction can use ferrous iron to generate toxic hydroxyl radicals². Thus, providing one mechanism by which Slc11a1 could influence antimicrobial activity in macrophages.

Transition of metal ions is essential and participates in numerous cellular functions such as regulation of transcription. In addition, hundreds of enzymes require metal ions as co-factors³.  

Studies show that polymorphism in SLC11A1 is correlated to the occurrence of autoimmune and infectious disease susceptibility, as well as innate and adaptive immune responses to mycobacterial products/antigens. Therefore, research on this ion transporter is of high importance¹.