Format

Send to

Choose Destination
FEBS Lett. 2000 Mar 3;469(1):93-7.

MOMP (major outer membrane protein) of Campylobacter jejuni; a versatile pore-forming protein.

Author information

1
UMR 6522, CNRS, IFRMP 23, Faculté des Sciences, 76821, Mont-Saint-Aignan, France.

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.

PMID:
10708763
DOI:
10.1016/s0014-5793(00)01244-8
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center