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.