Recombinant Human lspA protein

**Background of LspA Recombinant Protein**

LspA (lipoprotein signal peptidase A) is a bacterial enzyme critical for processing lipoproteins, a class of membrane-associated proteins essential for bacterial viability, virulence, and host-pathogen interactions. It specifically cleaves the signal peptide of precursor lipoproteins, enabling their maturation and proper localization in the bacterial cell envelope. LspA is highly conserved in Gram-negative bacteria, including pathogens like *Escherichia coli*, *Pseudomonas aeruginosa*, and *Salmonella enterica*, making it a potential target for novel antimicrobial therapies.

The recombinant LspA protein is produced through genetic engineering, typically by cloning the *lspA* gene into expression vectors (e.g., in *E. coli*), followed by purification using affinity chromatography. Recombinant LspA retains enzymatic activity, allowing researchers to study its structure-function relationships, substrate specificity, and inhibition mechanisms. Structural studies (e.g., X-ray crystallography or cryo-EM) have revealed its unique aspartic protease-like fold and membrane-embedded catalytic site, providing insights into its role in lipoprotein processing.

Research on LspA recombinant protein is pivotal for developing broad-spectrum antibiotics, particularly as multidrug-resistant bacterial infections rise globally. Inhibitors targeting LspA could disrupt bacterial lipoprotein biogenesis, impairing membrane integrity and virulence. Additionally, LspA studies contribute to understanding bacterial physiology and evolutionary adaptations. Its recombinant form also aids in high-throughput screening for drug candidates and elucidating resistance mechanisms, bridging gaps between basic microbiology and translational antimicrobial development.