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Titolo:
Difference in cholesterol-binding and cytolytic activities between listeriolysin O and seeligeriolysin O: a possible role of alanine residue in tryptophan-rich undecapeptide
Autore:
Ito, Y; Kawamura, I; Kohda, C; Baba, H; Kimoto, T; Watanabe, I; Nomura, T; Mitsuyama, M;
Indirizzi:
Kyoto Univ, Grad Sch Med, Dept Microbiol, Sakyo Ku, Kyoto 6068501, Japan Kyoto Univ Kyoto Japan 6068501 Microbiol, Sakyo Ku, Kyoto 6068501, Japan Nagoya Univ, Sch Med, Dept Internal Med 1, Nagoya, Aichi 4668550, Japan Nagoya Univ Nagoya Aichi Japan 4668550 ed 1, Nagoya, Aichi 4668550, Japan
Titolo Testata:
FEMS MICROBIOLOGY LETTERS
fascicolo: 2, volume: 203, anno: 2001,
pagine: 185 - 189
SICI:
0378-1097(20010925)203:2<185:DICACA>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
INTRACELLULAR GROWTH; HEMOLYTIC-ACTIVITY; PERFRINGOLYSIN-O; MAMMALIAN-CELLS; MONOCYTOGENES; IVANOVII; GENE; COMPLEMENTATION; PNEUMOLYSIN; VIRULENCE;
Keywords:
listeriolysin O; seeligeriolysin O; undecapeptide; cholesterol bindings; cytolysis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Mitsuyama, M Kyoto Univ, Grad Sch Med, Dept Microbiol, Sakyo Ku, Yoshidakonoe Cho, Kyoto 6068501, Japan Kyoto Univ Yoshidakonoe Cho Kyoto Japan 6068501 68501, Japan
Citazione:
Y. Ito et al., "Difference in cholesterol-binding and cytolytic activities between listeriolysin O and seeligeriolysin O: a possible role of alanine residue in tryptophan-rich undecapeptide", FEMS MICROB, 203(2), 2001, pp. 185-189

Abstract

We have constructed recombinant listeriolysin O (rLLO) and seeligeriolysinO (rLSO) from Listeria monocytogenes and Listeria seeligeri, respectively. In hemolysis and cholesterol-binding assays, the specific activity of recombinant toxin was lower for LSO as compared to LLO. To understand the molecular basis of this difference, in particular with respect to the conserved Trp-rich undecapeptide, a naturally occurring Ala To Phe substitution in LSO was introduced into rLLO. The rLLO:A488F hemolysin exhibited a reduced activity in both hemolysis and cholesterol-binding. The reverse mutation, inserted into rLSO, also increased the hemolytic activity of this mutant LSO. These results suggested that the natural replacement of Ala to Phe is involved in the weak cytolytic activity of LSO. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 00:33:48