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      A new pathway for the secretion of virulence factors by bacteria: the flagellar export apparatus functions as a protein-secretion system.

      Proceedings of the National Academy of Sciences of the United States of America
      Anti-Bacterial Agents, pharmacology, Bacterial Proteins, biosynthesis, Enterobacteriaceae, pathogenicity, physiology, Flagella, Genes, Bacterial, Movement, drug effects, Mutagenesis, Phospholipases, genetics, metabolism, Regulon, Virulence, Yersinia enterocolitica

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          Abstract

          Biogenesis of the flagellum, a motive organelle of many bacterial species, is best understood for members of the Enterobacteriaceae. The flagellum is a heterooligomeric structure that protrudes from the surface of the cell. Its assembly initially involves the synthesis of a dedicated protein export apparatus that subsequently transports other flagellar proteins by a type III mechanism from the cytoplasm to the outer surface of the cell, where oligomerization occurs. In this study, the flagellum export apparatus was shown to function also as a secretion system for the transport of several extracellular proteins in the pathogenic bacterium Yersinia enterocolitica. One of the proteins exported by the flagellar secretion system was the virulence-associated phospholipase, YplA. These results suggest type III protein secretion by the flagellar system may be a general mechanism for the transport of proteins that influence bacterial-host interactions.

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