Recombinant Bifidobacterium longum subsp. infantis Prolipoprotein diacylglyceryl transferase (lgt) is a bacterial enzyme responsible for lipidating prolipoproteins, a critical step in the maturation of bacterial membrane proteins. This post-translational modification involves transferring a diacylglyceryl group to the sulfhydryl group of a conserved cysteine residue in prolipoproteins, anchoring them to the cell membrane . The enzyme is encoded by the lgt gene (Blon_1369 in strain ATCC 15697) and plays a role in cell envelope biogenesis, virulence, and host-microbe interactions .
B. longum subsp. infantis ATCC 15697 is a keystone gut symbiont in breastfed infants, specializing in human milk oligosaccharide (HMO) metabolism . While the lgt enzyme itself is not directly linked to HMO utilization, its role in membrane protein maturation supports:
Oligosaccharide Transport: Membrane-bound solute-binding proteins (SBPs) critical for HMO uptake require proper lipidation for functionality .
Host Interaction: Lipoproteins contribute to bacterial adhesion and immune modulation, which are essential for colonization .
Research Tool: Recombinant lgt is used to study lipoprotein processing in Bifidobacterium and other Gram-positive bacteria .
Structure-Function Studies: Investigating how lipid modification affects membrane protein localization and stability .
Mechanistic Studies: Limited data exist on substrate specificity or regulatory interactions in B. infantis.
Therapeutic Potential: No direct evidence links lgt to probiotic efficacy, though strain-specific genomic clusters (e.g., HMO utilization) suggest synergies .
Structural Biology: High-resolution crystal structures of lgt remain unpublished.
KEGG: bln:Blon_1369