Recombinant Human Igl protein

Igl (intracellular growth locus) recombinant protein is derived from the pathogenic bacterium *Yersinia pestis*, the causative agent of plague. The *igl* operon, located on a virulence-associated plasmid, encodes components critical for the bacterium’s ability to survive and replicate within host macrophages, a key step in its pathogenesis. Igl proteins, particularly IglA and IglB, form a heterodimeric complex that interacts with the type III secretion system (T3SS) to facilitate the delivery of virulence effectors into host cells, disrupting immune responses and promoting intracellular survival.

The development of recombinant Igl proteins stems from efforts to dissect *Y. pestis* pathogenesis and identify targets for diagnostics, therapeutics, or vaccines. Using genetic engineering, the *igl* genes are cloned and expressed in heterologous systems like *E. coli* or yeast, enabling large-scale production of purified proteins. These recombinant proteins retain functional epitopes and structural features, making them valuable tools for studying host-pathogen interactions, antibody production, and immune evasion mechanisms.

Research on Igl recombinant proteins has provided insights into their role in bacterial adhesion, macrophage invasion, and modulation of host cell signaling. Additionally, they serve as antigens in serological assays to detect plague exposure and are explored as potential components of subunit vaccines. Challenges include maintaining protein stability and conformational integrity during production, as improper folding may reduce immunogenicity or functional utility. Advances in structural biology and protein engineering have improved yield and functionality, supporting their application in both basic research and translational medicine. Overall, Igl recombinant proteins represent a critical resource for understanding *Y. pestis* virulence and developing countermeasures against plague.