The Outer Membrane Protein VhOmp of <Emphasis Type="Italic">Vibrio harveyi</Emphasis>: Pore-Forming Properties in Black Lipid Membranes |
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Authors: | Albert Schulte Sompong Ruamchan Panida Khunkaewla Wipa Suginta |
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Institution: | (1) Biochemistry–Electrochemistry Research Unit, School of Chemistry and Biochemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima, 30000, Thailand; |
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Abstract: | Vibrio harveyi is known to cause fatal vibriosis in marine animals. Here, an outer membrane protein from V. harveyi, namely, VhOmp, was isolated and functionally characterized in terms of pore-forming contact with artificial lipid membranes.
The native VhOmp exists as a trimer of a molecular weight similar to that of the porin OmpF from Escherichia coli. Reconstitution of VhOmp into black lipid membranes demonstrated its ability to form ion channels. The average pore conductance
of VhOmp was revealed to be about 0.9 and 2 nS in 0.2 and 1 M KCl, respectively. Within transmembrane potentials of ±100 mV,
VhOmp pores behaved as ohmic conduits, and their conductance scaled linearly with voltage. Nonlinear plots of the pore conductance
versus symmetrical salt concentrations at either side of the protein-incorporating membrane suggested the influence of interior
channel functionalities on the passage of charged species. In the presence of Omp-specific polyclonal antibodies, the pore-forming
property of VhOmp was modulated so that the usual step-like current increments were replaced by random transitory current
fluctuations. VhOmp exhibited a strong biological activity by causing hemolysis of human red blood cells, indicating that
VhOmp may act as a crucial determinant during bacterial infection to animal host cells. |
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