The TpsB translocator HMW1B of haemophilus influenzae forms a large conductance channel.

The Journal of Biological Chemistry
Guillaume DuretAnne H Delcour

Abstract

The Haemophilus influenzae HMW1 adhesin is secreted via the two-partner secretion pathway and requires HMW1B for translocation across the outer membrane. HMW1B belongs to the Omp85-TpsB superfamily of transporters and consists of two structural domains, a C-terminal transmembrane beta-barrel and an N-terminal periplasmic domain. We investigated the electrophysiological properties of the purified full-length HMW1B and the C-terminal domain using planar lipid bilayers. Both the full-length and the truncated proteins formed conductive pores with a low open probability, two well defined conductance states, and other substates. The kinetic patterns of the two conductance states were distinct, with rapid and frequent transitions to the small conductance state and occasional and more prolonged openings to the large conductance state. The channel formed by the full-length HMW1B showed selectivity for cations, which decreased when measured at pH 5.2, suggesting the presence of acidic residues in the pore. The C-terminal domain of HMW1B was less stable and required reconstitution into liposomes prior to insertion in the bilayer. It formed a channel of smaller conductance but a similar gating pattern as the full-length protein, demonstrat...Continue Reading

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Citations

Apr 2, 2013·Research in Microbiology·Françoise Jacob-DubuissonBernard Clantin
Oct 24, 2009·The Journal of Biological Chemistry·Owen S MapingireAnne H Delcour
Sep 13, 2013·Annual Review of Microbiology·Anne H Delcour
Aug 8, 2009·Trends in Microbiology·Joseph W St Geme, Hye-Jeong Yeo
Nov 26, 2013·Biochimica Et Biophysica Acta·Peter van UlsenJoen Luirink
May 26, 2017·Frontiers in Cellular and Infection Microbiology·Jeremy GuérinFrançoise Jacob-Dubuisson

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