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, and IFN-
Administered Orally via Attenuated Salmonella typhimurium1
*
Department of Immunology and
Division of Infection and Immunity, University of Glasgow, Glasgow, United Kingdom;
Medeva Group Research and
§
Department of Biochemistry, Imperial College of Science, Technology, and Medicine, London, United Kingdom;
¶
Department of Virology, St. Bartholomew’s and Royal London School of Medicine, University of London, United Kingdom; and
||
Department of Tropical Public Health, Harvard School of Public Health, Boston, MA 02115
The genes encoding murine macrophage migration inhibitory factor
(MIF), IL-2, IFN-
or TNF-
were cloned individually into an
expression plasmid under the control of the inducible promoter
nirB and transfected into the
aroA-aroD- deletion mutant strain of
Salmonella typhimurium (BRD509). These S.
typhimurium derivatives (henceforward called constructs and
termed GIDMIF, GIDIL2, GIDIFN and GIDTNF) expressed their
respective cytokines in vitro under anaerobic conditions and stably
colonized BALB/c mice up to 14 days after oral administration. The
highly susceptible BALB/c mice that had received the constructs orally
and that had been subsequently infected via the footpad with
Leishmania major, developed significantly reduced disease
compared with control mice administered the untransfected
Salmonella strain (BRD509). Importantly, a combination of
GIDMIF, GIDIFN, and GIDTNF administered orally after L.
major infection was able to significantly limit lesion
development and reduced parasite loads by up to three orders of
magnitude. Spleen and lymph node cells of mice administered this
combination expressed markedly higher levels of inducible nitric oxide
synthase (iNOS) compared with those from mice receiving an equivalent
dose of the control strain of Salmonella (BRD509). These
data therefore demonstrate the feasibility of therapeutic treatment in
an infectious disease model using cytokines delivered by attenuated
Salmonella. The protective effect observed correlates with
the induction of inducible nitric oxide synthase in vivo.
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