Determination of functional regions of Clostridium perfringens enterotoxin through deletion analysis

Clinical Infectious Diseases

Volumn 25, Issue 2 SUPPL., 1997, Pages

  Kokai Kun, John F ^a   McClane, Bruce A ^a  

^a UNIVERSITY OF PITTSBURGH SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROTOXIN;

ANIMAL CELL; ANIMAL TISSUE; CLOSTRIDIUM PERFRINGENS; CONFERENCE PAPER; CYTOTOXICITY; GENE DELETION; MOLECULAR MODEL; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; RECEPTOR BINDING; STRUCTURE ACTIVITY RELATION; TOXIN ANALYSIS;

CLOSTRIDIUM PERFRINGENS; ENTEROTOXINS; GENE DELETION; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0030865956     PISSN: 10584838     EISSN: None     Source Type: Journal    
DOI: 10.1086/516246     Document Type: Article

References (5)

1. McCIane B A. Clostridium perfringens enterotoxin acts by producing small molecule permeability alterations in plasma membranes. Toxicology 1994;87:43-67.
2. McClane BA. An overview of the Clostridium perfringens enterotoxin. Toxicon 1996;34:1335-43.
3. Kokai-Kun JF, McClane BA. The Clostridium perfringens enterotoxin. In: Rood JI, McCiane BA, Titball R, Songer JG, eds. The clostridia: molecular genetics and pathogenesis. London: Academic Press, 1997:325-57.
4. Hanna PC, MietznerTA, Schoolnik GK, McClane BA. Localization of the receptor-binding region of Clostridium perfringens enterotoxin utilizing cloned toxin fragments and synthetic peptides. The 30 C-terminal amino acids define a functional binding region. J Biol Chem 1991;266:11037-43.
5. Kokai-Kun JF, McClane BA. Evidence that region(s) of the Clostridium perfringens enterotoxin molecule remain exposed on the external surface of the mammalian plasma membrane when the toxin is sequestered in small or large complex. Infect Immun 1996;64:1020-5.