By Francisco A. Uzal, J. Glenn Songer, John F. Prescott, Michel R. Popoff
Clostridial ailments of Animals is the 1st publication to target clostridial ailments in family and wild animals, delivering a accomplished reference on those universal diseases.
- Provides a unmarried source for all facets of clostridial diseases
- Presents present, accomplished details with a spotlight on scientific relevance
- Covers each one sickness extensive, together with etiology, epidemiology, clinics, gross pathology, histopathology, diagnostics, diagnostic standards, prophylaxis, keep watch over, and treatment
- Written through the world-leading specialists within the box of clostridial ailments in animals
- Offers images and precis tables to help the techniques mentioned within the textual content and reduction in recognition
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Extra resources for Clostridial diseases of animals
Baratii, C. butyricum) can also cause botulism in humans C. 1 Summary of the main characteristics of the major clostridial pathogens of animals Intestinal tract quail, chickens, grouse, partridge, pheasants, turkey Soil, intestine, latent in muscle of healthy animals (endogenous) Meat, fish Soil Raw fish, marine mammals Carrion, chicken manure Meat, pork products. 6–17 µm; spores oval, C to STa; colonies 1–5 mm, circular or irregular, scalloped or rhizoid margin; β‐hemolytic; motile; C. novyi type A and C.
There are two major classes of clostridial toxins that act at the cytoplasmic level in the host cell. These toxins contain a binding component that adheres to a receptor(s) on the host cell membrane, which results in the formation of an endocytic vacuole that contains the toxin. Lysosomal fusion leads to the acidification of the vacuole, a conformation change in the toxin, and secretion of the active enzymatic component of the toxin into the cytoplasm, where it leads to cellular damage. The first class of toxins is represented by tetanus neurotoxin (TeNT) and the seven related, but distinct, botulinum neurotoxins (BoNT/A to BoNT/G) (Chapter 7).
LCGTs contain C‐terminal repeats involved in the recognition of the cell surface receptor and a central hydrophobic domain mediating the translocation of the N‐terminal catalytic domain into the cytosol through the endosome membrane. The catalytic domain is cleaved from the rest of the molecule by an autocleavage process involving the cysteine protease domain which contains the active site DHC. The catalytic domain structure shows a compact core of β‐sheet surrounded by numerous α‐helices with central catalytic motif (DxD) and an extension of four N‐terminal helices.