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Peptide translocation across MOMP, the major outer membrane channel from Campylobacter jejuni.


ABSTRACT: Here we report on translocation of short poly-arginines across the MOMP porin, the major outer membrane protein in the cell wall of Campylobacter jejuni. MOMP was purified to homogeneity from a pathogenic strain of C. jejuni. Its reconstitution in lipid membranes and measuring the ion-current revealed two main distinct populations of protein channels which we interpreted as mono and trimers. Addition of poly-arginines causes concentration and voltage dependent ion-current fluctuations. Increasing the transmembrane potential decreases the residence time of the peptide inside the channel indicating successful translocation. We conclude that poly-arginines can cross the outer membrane of Campylobacter through the MOMP channel.

SUBMITTER: Dhanasekar NN 

PROVIDER: S-EPMC5614690 | biostudies-other | 2017 Sep

REPOSITORIES: biostudies-other

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Peptide translocation across MOMP, the major outer membrane channel from <i>Campylobacter jejuni</i>.

Dhanasekar Naresh Niranjan NN   Aliouane Soumeya S   Winterhalter Mathias M   Pagès Jean-Marie JM   Bolla Jean-Michel JM  

Biochemistry and biophysics reports 20170623


Here we report on translocation of short poly-arginines across the MOMP porin, the major outer membrane protein in the cell wall of <i>Campylobacter jejuni</i>. MOMP was purified to homogeneity from a pathogenic strain of <i>C. jejuni</i>. Its reconstitution in lipid membranes and measuring the ion-current revealed two main distinct populations of protein channels which we interpreted as mono and trimers. Addition of poly-arginines causes concentration and voltage dependent ion-current fluctuati  ...[more]

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