Vibrio cholerae strains with mutations in an atypical type I secretion system accumulate RTX toxin intracellularly.
This study shows that the Vibrio cholerae RTX toxin is secreted by a four-component type I secretion system (TISS) encoded by rtxB, rtxD, rtxE, and tolC. ATP-binding site mutations in both RtxB and RtxE blocked secretion, demonstrating that this atypical TISS requires two transport ATPases that may function as a heterodimer.
Boardman
Bethany Kay
BK
Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Satchell
Karla J Fullner
KJ
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000502:physiology; D001427:Bacterial Toxins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D008969:Molecular Sequence Data; D009154:Mutation; D009876:Operon; D014734:Vibrio cholerae / Q000378:metabolism* / Q000472:pathogenicity*
D001425:Bacterial Outer Membrane Proteins; D001427:Bacterial Toxins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; C434464:RtxA protein, Vibrio cholerae; C073126:tolC protein, E coli; D000251:Adenosine Triphosphatases