MOMP (major outer membrane protein) of Campylobacter jejuni; a versatile pore-forming protein.
FEBS Lett
; 469(1): 93-7, 2000 Mar 03.
Article
em En
| MEDLINE
| ID: mdl-10708763
ABSTRACT
The great majority of trimeric porins of Gram-negative bacteria cannot be dissociated into monomers without disrupting their folded conformation. The porin of Campylobacter jejuni, however, displays two folded structures, a classical oligomer and a monomer resistant to detergent denaturation. We probed the transition of trimer to monomer using light scattering experiments and examined the secondary structures of these two molecular states by infra-red spectroscopy. The channel-forming properties of both trimer and monomer were studied after incorporation into artificial lipid bilayers. In these conditions, the trimer induced ion channels with a conductance value of 1200 pS in 1 M NaCl. The pores showed marked cationic selectivity and sensitivity to low voltage. Analysis of the isolated monomer showed nearly the same single-channel conductance and the same selectivity and sensitivity to voltage. These results indicate that the folded monomer form of C. jejuni MOMP displays essentially the same pore-forming properties as the native trimer.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas da Membrana Bacteriana Externa
/
Campylobacter jejuni
/
Porinas
/
Proteínas de Membrana
/
Antígenos de Bactérias
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
França