Identification of a general secretory pathway in a human isolate of Burkholderia vietnamiensis (formerly B. cepacia complex genomovar V) that is required for the secretion of hemolysin and phospholipase C activities.
Members of the Burkholderia cepacia complex can secrete proteases, lipases, and hemolysins. We report in this study the identification of a general secretory pathway present in a B. vietnamiensis (formerly genomovar V) clinical isolate, which is required for the efficient secretion of phospholipase C and hemolysin activities. Southern blot hybridization experiments revealed that this general secretion pathway is highly conserved among the different genomovars of the B. cepacia complex and is homologous to a similar system described in B. pseudomallei. We also show that this pathway appears not to be necessary for intracellular survival of B. vietnamiensis within Acanthamoeba polyphaga.
Fehlner-Gardiner
Christine C
CC
Department of Microbiology and Immunology, University of Western Ontario, London, Ontario, Canada.
Hopkins
Tammy M-H
TM
Valvano
Miguel A
MA
D000595:Amino Acid Sequence; D001483:Base Sequence; D015139:Blotting, Southern; D019121:Burkholderia Infections / Q000382:microbiology; D016956:Burkholderia cepacia / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D004251:DNA Transposable Elements / Q000235:genetics; D004269:DNA, Bacterial / Q000235:genetics; D006460:Hemolysin Proteins / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008969:Molecular Sequence Data; D009154:Mutation; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D010738:Type C Phospholipases / Q000378:metabolism*
D004251:DNA Transposable Elements; D004269:DNA, Bacterial; D006460:Hemolysin Proteins; D010738:Type C Phospholipases