scholarly journals SERUM THERAPY IN BACILLARY DYSENTERY.

The Lancet ◽  
1919 ◽  
Vol 194 (5018) ◽  
pp. 794
1920 ◽  
Vol 31 (1) ◽  
pp. 19-33 ◽  
Author(s):  
Peter K. Olitsky ◽  
I. J. Kligler

With the methods which have been described we have separated an exotoxin and an endotoxin from cultures of the Shiga dysenteric bacillus. The study of the nature and effect of the poison of this microorganism is thus simplified. The two toxins are physically and biologically distinct. The exotoxin is relatively heat-labile, arises in the early period of growth, and yields an antiexotoxic immune serum. The endotoxin, on the other hand, is heat-stable, is formed in the later period of growth, and is not neutralized by the antiexotoxic serum. The exotoxin exhibits a specific affinity for the central nervous organs in the rabbit, giving rise to a characteristic lesion—mainly, hemorrhages, necroses, and possibly a perivascular infiltration in the gray matter of the upper spinal cord and medulla. The endotoxin exerts a typical action on the intestinal tract, producing edema, hemorrhages, necroses, and ulcerations, especially in the large intestine. In dysentery in man the intestinal lesions predominate, but in severe epidemics paralysis and neuritis have been observed (Osler17). These facts become specially significant from the standpoint of the serum therapy of bacillary dysentery. A potent antidysenteric serum should contain antibodies against the exotoxin as well as the endotoxin. That such a serum can be produced in horses has been experimentally demonstrated.


BMJ ◽  
1941 ◽  
Vol 2 (4207) ◽  
pp. 280-281
Author(s):  
A. Compton
Keyword(s):  

1931 ◽  
Vol 2 (23) ◽  
pp. 714-716 ◽  
Author(s):  
F. M. Burnet ◽  
Margot McKie ◽  
I. Jeffreys Wood
Keyword(s):  

2005 ◽  
Vol 187 (16) ◽  
pp. 5658-5664 ◽  
Author(s):  
Elizabeth E. Wyckoff ◽  
Gregory F. Lopreato ◽  
Kimberly A. Tipton ◽  
Shelley M. Payne

ABSTRACT Shigella dysenteriae serotype 1, a major cause of bacillary dysentery in humans, can use heme as a source of iron. Genes for the transport of heme into the bacterial cell have been identified, but little is known about proteins that control the fate of the heme molecule after it has entered the cell. The shuS gene is located within the heme transport locus, downstream of the heme receptor gene shuA. ShuS is a heme binding protein, but its role in heme utilization is poorly understood. In this work, we report the construction of a chromosomal shuS mutant. The shuS mutant was defective in utilizing heme as an iron source. At low heme concentrations, the shuS mutant grew slowly and its growth was stimulated by either increasing the heme concentration or by providing extra copies of the heme receptor shuA on a plasmid. At intermediate heme concentrations, the growth of the shuS mutant was moderately impaired, and at high heme concentrations, shuS was required for growth on heme. The shuS mutant did not show increased sensitivity to hydrogen peroxide, even at high heme concentrations. ShuS was also required for optimal utilization of heme under microaerobic and anaerobic conditions. These data are consistent with the model in which ShuS binds heme in a soluble, nontoxic form and potentially transfers the heme from the transport proteins in the membrane to either heme-containing or heme-degrading proteins. ShuS did not appear to store heme for future use.


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