DsbA antibodies are immunoglobulins developed to recognize DsbA, a periplasmic disulfide oxidoreductase essential for catalyzing disulfide bond formation in bacterial proteins. DsbA is conserved across Gram-negative pathogens and is a virulence factor due to its role in folding toxins, adhesins, and biofilm-related proteins . Antibodies against DsbA are primarily used in Western blot (WB), ELISA, and immunohistochemistry (IHC) to study its expression, localization, and interaction with substrates .
DsbA antibodies vary in clonality, host species, and applications:
Notes:
DsbA antibodies have been instrumental in studying virulence mechanisms:
In Vibrio parahaemolyticus, DsbA antibodies confirmed that DsbA mutants exhibit reduced cytotoxicity and hemolytic activity due to impaired disulfide bonding in toxins like TDH .
Acinetobacter baumannii DsbA (AbDsbA) antibodies revealed its role in biofilm formation and interaction with elongation factor Tu (EF-Tu), highlighting its potential as an anti-virulence target .
Insulin reduction assays using DsbA antibodies demonstrated that V. parahaemolyticus DsbA has a redox potential of −89 mV, enabling efficient substrate oxidation .
Structural studies with E. coli DsbA antibodies identified its hydrophobic groove as critical for binding partner oxidase DsbB .
Monoclonal antibodies (e.g., 8A10) achieve >95% purity in WB, detecting DsbA at 24 kDa without cross-reactivity .
Anti-DsbA antibodies are used in affinity columns to purify DsbA-fusion proteins from bacterial lysates .
Function: Essential for disulfide bond formation in periplasmic proteins (e.g., PhoA, OmpA) .
Redox Properties:
KEGG: pau:PA14_72450