gcvP is the P-protein of the GCS, which binds glycine via its pyridoxal phosphate (PLP) cofactor . Key features include:
Function: Converts glycine into 5,10-methylenetetrahydrofolate, supporting nucleotide and amino acid biosynthesis .
Structure: Contains a PLP-binding domain critical for decarboxylation activity .
Recombinant Form: Partial sequences are often engineered for functional studies, omitting non-essential regions while retaining catalytic domains .
gcvP is essential for chronic persistence in hosts:
Mouse Infection Models:
Recombinant GCS proteins like gcvP are explored as subunit vaccine candidates:
Immunogenicity: Recombinant B. abortus proteins (e.g., r-glk) induce Th1 immune responses and protect against challenge .
Cross-Protection: GCS enzymes are conserved across Brucella species, making them broad-spectrum antigen targets .
Apoptosis Modulation: GCS homologs in Mycoplasma inhibit host apoptosis by stabilizing endoplasmic reticulum kinases . While unconfirmed for Brucella gcvP, similar mechanisms may enhance intracellular survival.
Metabolic Adaptations: gcvP supports gluconeogenesis in nutrient-limited intracellular niches, as shown by proteomic studies of B. abortus-infected macrophages .
Expression Systems: E. coli BL21 is commonly used for recombinant Brucella protein expression .
Enzymatic Assays: GFP-refolding and CsA-inhibition tests validate PPIase-like activity in related proteins (e.g., CypB) .
KEGG: bmb:BruAb2_0506