E. Gunneriusson et al., SURFACE DISPLAY OF A FUNCTIONAL SINGLE-CHAIN FV ANTIBODY ON STAPHYLOCOCCI, Journal of bacteriology, 178(5), 1996, pp. 1341-1346
Two different host-vector expression systems designed for fell surface
display of chimeric receptors on Staphylococcus xylosus and Staphyloc
occus carnosus have been evaluated for surface display of a mouse immu
noglobulin G1(kappa) [IgG1(kappa)] anti-human IgE single-chain Fv (scF
v) antibody fragment. To achieve surface anchoring of the chimeric rec
eptors containing the scFv, the cell surface attachment regions from S
taphylococcus aureus protein A were used in both expression systems. T
he different chimeric receptors could be recovered from cell wall extr
acts of both S. xylosus and S. carnosus, and surface localization was
demonstrated by taking advantage of a serum albumin-binding reporter r
egion present within the two types of receptors. In addition, the two
different recombinant staphylococci carrying hybrid receptors containi
ng the scFv were demonstrated to react with the antigen, which was hum
an IgE, in whole-cell enzyme-linked immunosorbent assays. This is the
first report of an antibody fragment expressed in a functional form an
chored to the surface of gram-positive bacteria. The potential use of
recombinant gram-positive bacteria as whole-cell diagnostic devices or
alternatives to filamentous phages for surface display of scFv librar
ies is discussed.