Clinical and Diagnostic Laboratory Immunology, 03 1996, 242-245, Vol 3, No. 2
EV Oaks, WD Picking and WL Picking
The antigen preparation most often used for determining the levels of
antibodies to virulence-associated proteins of Shigella spp. consists of a
mixture of proteins (including IpaB, IpaC, IpaD, and VirG*) extracted from
virulent shigellae with water (water extract). To overcome the lack of
specificity for individual antigens in the water- extract enzyme-linked
immunosorbent assay (ELISA), the ipaD gene from S. flexneri has been
cloned, expressed to a high level, and purified for use in a new ELISA for
the determination of the levels of antibody against IpaD in monkeys and
humans challenged with shigellae. The IpaD ELISA for serum immunoglobulins
G and A correlated well with the water- extract ELISA in that monkeys
infected with S. flexneri or S. sonnei responded with high serum antibody
titers in both assays. The IpaD assay required less antigen per well, had
much lower background levels, and did not require correction with antigens
from an avirulent organism. In conjunction with the water-extract ELISA, it
was possible to identify infected animals that did not respond to IpaD but
did produce antibodies that reacted in the water-extract ELISA. This
indicates that even though IpaB, IpaC, and IpaD are essential for the
invasiveness phenotype, the infected host does not always produce
antibodies against all components of the invasiveness apparatus.
Copyright © 1996 by the American Society for Microbiology. All rights reserved.
Antibody response of monkeys to invasion plasmid antigen D after infection with Shigella spp
Department of Enteric Infections, Walter Reed Army Institute of Research, Washington, D.C. 20307, USA.
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