Bacteria Bordetella pertussis

Cytotoxin that inactivates G proteins involved in cellular metabolism. It is a solid obtained from bacteria (Bordetella pertussis). 

Killing. The proeess by which the live bacteria in the culture are killed and thus rendered harmless. Heat and disinfectants are employed. Heat and/or formalin are required to kill the cells of Bordetella pertussis used to make whooping-cough vaccines, and phenol is used to kill the Vibrio cholerae in cholera vaccine and the Salmonella typhi in typhoid vaeeine. 

The observed adjuvanticity of Bordetella pertussis is largely attributable to the presence of pertussis toxin and lipopolysaccharide (LPS). LPS, a constituent of the cell envelope of Gramnegative bacteria (Chapter 3), essentially consists of polysaccharide moieties to which lipid (lipid A) is covalently attached. 

As a component of a natural glycoconjugate, the best-known example is 3-deoxy-D-m<2 o-oct-2-ulosonic acid (123), commonly known as Kdo. Compound 123 is part of the core linking the polysaccharide to lipid A in the LPS that is characteristic of Gram-negative bacteria.308 Kdo is usually found in the a-pyranosic configuration, but it may exist as furanoside as in the LPS of Bordetella pertussis.309... 

A1(0H)3] suspension has also been used in conjunction with the addition of bacteria, such as Bordetella pertussis. 

Bronchiectasis is the irreversible dilation of parts of the bronchi that results in the formation of pockets where secretions can accumulate. These pockets create an environment that fosters the growth of bacteria and infection. Bacteria commonly found in bronchiectasis are Staphylococcus, Klebsiella, and Bordetella pertussis. These are treated with antibiotics (see chapter 13). 

The answer is a. (Murray, pp 452-467. Scriver, pp 3-45. Sack, pp 1-40. Wilson, pp 101—120.) Virulent strains of bacteria that cause severe, life-threatening respiratory tract infections can often be successfully treated with erythromycin. These include Mycoplasma pneumoniae, various Legionella species, and Bordetella pertussis. The mechanism of action of erythromycin is to specifically bind the 50S subunit of bacterial ribosomes. Under normal conditions, after mRNA attaches to the initiation site of the 30S subunit, the 50S subunit binds to the 30S complex and forms the 70S complex that allows protein chain elongation to go forward. Elongation is prevented in the presence of erythromycin. 

Dirithromycin is a 14-membered macrolide antibiotic approved for clinical use in the United States. Its in vitro activities are two- to fourfold less than those of erythromycin against gram-positive bacteria and a variety of clinical isolates, but it is fourfold more active than erythromycin against Bordetella pertussis [1,8,... 

Thus the ability of bacteria in culture to bind to sulfatide may be a reflection of the degree of stress these organism experience in vitro. Other organisms for which sulfatide binding has been reported include Bordetella pertussis [36], Mycoplasma pneumoniae [37], M. hyopneumoniae [75]. 

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