S. Lory, SECRETION OF PROTEINS AND ASSEMBLY OF BACTERIAL SURFACE ORGANELLES - SHARED PATHWAYS OF EXTRACELLULAR PROTEIN TARGETING, CURRENT OPINION IN MICROBIOLOGY, 1(1), 1998, pp. 27-35
Extracellular or surface localization of virulence determinants is an
important attribute of pathogenic microorganisms. The past decade has
seen significant research advances in defining the steps and identifyi
ng the necessary machinery for protein secretion from bacterial cells.
In Gram-negative pathogens, four distinct classes of secretion pathwa
ys have been identified that deliver virulence factors to their sites
of action. These pathways are responsible for the delivery of soluble
extracellular enzymes into the surrounding medium, or for specifically
targeting proteins to the host cell. In several instances protein sec
retion pathways are similar to those involved in assembly of bacterial
appendage. Combination of biochemical and genetic analyses has recent
ly revealed that the pathways of protein secretion and surface localiz
ation of various organelles are mechanistically similar which was not
apparent simply by comparing amino acid sequences of related proteins.
The choice of the pathway that a protein will utilize may not be dict
ated only by the specific requirement of the secreted protein to trave
rse the cell envelope in the functional form, but also by the need to
assure its delivery to the correct site of action outside the bacteria
l cell.