Immunomodulation with Enterotoxins for the Generation of Secretory Immunity or Tolerance: Applications for Oral Infections
G. Hajishengallis1,5,
S. Arce2,4,
C.M. Gockel2,4,
T.D. Connell2,4, and
M.W. Russell2,3,4,*
1 Department of Microbiology, Immunology, and Parasitology, and Center of Excellence in Oral and Craniofacial Biology, Louisiana State University Health Sciences Center, New Orleans, LA, USA;
2 Departments of Microbiology and Immunology and
3 Oral Biology,
4 The Witebsky Center for Microbial Pathogenesis and Immunology, University at Buffalo, 3435 Main Street/Farber 138, Buffalo, NY 14214, USA;

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Figure. Molecular structure of heat-labile enterotoxins. A and B polypeptides are translated from a single mRNA, with an excess of B polypeptides. The leader sequences of both allow them to be transported into the periplasm, where B subunits assemble into pentamers. A disulfide bridge spans the junction of the A1 and A2 segments of the A polypeptide, where a proteolytic nick occurs. The A2 subunit non-covalently associates with the central pore in the B pentamer.
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