Prolipoprotein diacylglyceryl transferase (Lgt) is a membrane-bound enzyme critical for bacterial lipoprotein biosynthesis. It catalyzes the transfer of an sn-1,2-diacylglyceryl group from phosphatidylglycerol to the cysteine residue of prolipoproteins, forming a thioether bond essential for lipoprotein maturation . In Bordetella avium, Lgt is hypothesized to play a role in virulence by modifying lipoproteins involved in host-pathogen interactions, though direct studies on the recombinant form remain limited.
Lgt initiates a three-step lipoprotein maturation pathway:
Diacylglyceryl transfer: Lgt attaches diacylglycerol to prolipoproteins.
Signal peptide cleavage: By signal peptidase II (Lsp).
N-acylation: By apolipoprotein N-acyltransferase (Lnt) in select bacteria .
In B. avium, this process likely underpins outer membrane protein localization, as seen in its 21K and 37K surface-exposed lipoproteins .
While recombinant B. avium Lgt has not been explicitly documented, B. pertussis Lgt is produced in E. coli for vaccine development . Potential applications for B. avium Lgt include:
Vaccine antigen: Surface-exposed lipoproteins modified by Lgt are immunogenic targets .
Antimicrobial target: Essentiality of Lgt for bacterial growth makes it a drug candidate .
Diagnostic tool: ELISA assays using recombinant Lgt could detect B. avium antibodies .
Current limitations include:
No structural or kinetic data for B. avium Lgt.
Lack of direct evidence for its role in virulence.
Underexplored potential in diagnostic or therapeutic contexts.
Future studies should prioritize heterologous expression, enzymology, and immunological profiling of recombinant B. avium Lgt to address these gaps.
Recombinant Bordetella avium Prolipoprotein diacylglyceryl transferase (Lgt) catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein. This is the initial step in mature lipoprotein formation.
KEGG: bav:BAV2897
STRING: 360910.BAV2897