1887

Abstract

Type 4 fimbriae (pili) are surface appendages that are expressed by many species of Gram-negative bacteria. Previous studies have demonstrated that can express and assemble pilin subunits from several unrelated species, indicating a common mechanism for biogenesis of type 4 pili whereby structural subunits from one system may be interchanged with those of another. In this study, an isogenic mutant of enteropathogenic (EPEC) was constructed containing the entire gene from O395, which encodes the major structural subunit of the toxin-coregulated pilus (TCP), in place of , which encodes the major structural subunit of the bundle-forming pilus (BFP). Surprisingly, expression of type 4 pilin structures and the associated phenotype of bacterial autoaggregation in culture media were not observed for cells of the EPEC strain containing nor for those containing an additional mutation in , which otherwise is associated with a hyperfimbriate phenotype. In addition, cells of a mutant EPEC strain containing plasmids designed to express either of two different chimeric type 4 pilin subunits containing segments of BfpA and TcpA also failed to form bacterial aggregates and express type 4 pilin structures. Collectively, these results indicate that the type 4 pilin assembly system of EPEC exhibits specificity with regard to pilin subunit recognition and assembly.

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2000-03-01
2024-04-18
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