TY - JOUR
T1 - The crucial amino acid residue related to inactivation of Vibrio vulnificus hemolysin
AU - Senoh, Mitsutoshi
AU - Okita, Yuka
AU - Shinoda, Sumio
AU - Miyoshi, Shin ichi
N1 - Funding Information:
This study was supported by a Grant-in-Aid for Scientific Research from Japan Society for the Promotion of Sciences.
PY - 2008/1
Y1 - 2008/1
N2 - 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.
AB - 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.
KW - Hemolysin
KW - In vitro translation
KW - Site-directed mutagenesis
KW - Vibrio vulnificus
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U2 - 10.1016/j.micpath.2007.07.002
DO - 10.1016/j.micpath.2007.07.002
M3 - Article
C2 - 17897806
AN - SCOPUS:36849080922
VL - 44
SP - 78
EP - 83
JO - Microbial Pathogenesis
JF - Microbial Pathogenesis
SN - 0882-4010
IS - 1
ER -
