The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin.

The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin. Research Abstract Details 

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The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin. Abstract Text:

Mitsutoshi Senoh,Yuka Okita,Sumio Shinoda,Shin-Ichi Miyoshi,

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 (Leu(281), Ser(415), Asn(435)/Asp(435), Asn(438)) and type 2 (Ile(281), Asn(415), Asn(435), Thr(438)). 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 degrees C and to specific inactivation by cholesterol. On the other hand, a variant of type 2 toxin (Asp(435), Asn(438)) 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, Thr(438), may be critical for higher stability of type 2 toxin.

The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin. Publishing Authors By Initials

M Senoh,Y Okita,S Shinoda,S Miyoshi,

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The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Microbial pathogenesis

VOLUME: 44

Page Numbers: 78-83

Journal Abbreviation: Microb. Pathog.

ISSN: 0882-4010

DAY: 14

MONTH: 08

YEAR: 2007

The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin. Information

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LANGUAGE: eng

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Grant and Affiliation Information for The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin.

AFFILIATION: Graduate School of Natural Science and Technology, Okayama University, Tsushima-Naka, Okayama 700-8530, Japan.

Country: England

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MEDLINETA: Microb Pathog

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