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The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin
- Source :
-
Microbial Pathogenesis . Jan2008, Vol. 44 Issue 1, p78-83. 6p. - Publication Year :
- 2008
-
Abstract
- Abstract: Vibrio vulnificus, an opportunistic human pathogen causing fetal septicemia, produces a 50-kDa pore-forming toxin as a virulence factor. This toxin consists of 451 amino acid residues; however, there are two types of this toxin on the basis of the difference of some amino acid residues, type 1 (Leu281, Ser415, Asn435/Asp435, Asn438) and type 2 (Ile281, Asn415, Asn435, Thr438). In the present study, two characteristic properties of type 2 toxin that was elaborated by V. vulnificus cells or synthesized by the in vitro system were compared to those of type 1 toxin. Type 2 toxin was found to be more resistant to spontaneous inactivation at 37°C and to specific inactivation by cholesterol. On the other hand, a variant of type 2 toxin (Asp435, Asn438) showed the same properties as type 1 toxin. The replacement of the 438th Asn to Thr (N438T), but not the 435th Asp to Asn (D435N), resulted in reversion of the variant type 2 toxin to typical type 2 toxin. These findings indicate that a single amino acid residue, Thr438, may be critical for higher stability of type 2 toxin. [Copyright &y& Elsevier]
- Subjects :
- *TOXINS
*AMINO acids
*RADIOGENETICS
*COMMUNICABLE diseases
Subjects
Details
- Language :
- English
- ISSN :
- 08824010
- Volume :
- 44
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- Microbial Pathogenesis
- Publication Type :
- Academic Journal
- Accession number :
- 27901137
- Full Text :
- https://doi.org/10.1016/j.micpath.2007.07.002