Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 2011 Mar;193(5):1291–1292. doi: 10.1128/JB.01489-10

Membrane Topology and Identification of Critical Amino Acid Residues in the Wzx O-Antigen Translocase from Escherichia coli O157:H7

Cristina L Marolda 1, Bo Li 1, Michael Lung 1, Mei Yang 1, Anna Hanuszkiewicz 1, Amanda Roa Rosales 1, Miguel A Valvano 1
PMCID: PMC3067600

Volume 192, no. 23, p. 6160-6171, 2010. Page 6160: The title should appear as shown above.

Page 6165: Fig. 3 should appear as shown below. (The wzxEcO157 gene was obtained by PCR cloning from genomic DNA of strain UWO934-88, a clinical isolate of E. coli O157:H7 [Marolda et al., Microbiology 150:4095-4105, 2004], and its amino acid sequence is identical to that of GenBank accession no. AE005429_8. The amino acid sequence of WzxEcO157 includes an N-terminal fusion to the FLAG epitope. To construct this fusion, the first Met of wild-type WzxEcO157 was changed to Gly [position 1/13]. The amino acid numbers in the figure correspond to the original positions in the wild-type protein [Gly-13 corresponds to Met-1]. The tyrosine residue at position 319 in the original figure was misplaced, and its normal location is at position 253. The methionine at position 405 was displaced graphically but is actually located at the end of cytosolic loop 5.)

FIG. 3.

FIG. 3.

Page 6168: Table 3 should appear as shown below (column heads have been corrected).

TABLE 3.

Plasmid Biotinylationa
Location of amino acid residueb O-antigen expressionc
Whole cells Vesicles
pML203-K144C + ND P 100
pML203-K176C ND + C 40
pML203-H209C + ND P 90
pML203-K244C + C 60
pML203-P254C ND TM 100
pML203-F264C ND TM 100
pML203-D277C + + P 100
pML203-G286C ND ? 100
pML203-F293C ? 100
pML203-R298C + ND P 0
pML203-P306C TM 70
pML203-P313C TM 50
pML203-D320C + C 30
pML203-R324C + C 90
pML203-K331C + C 70
pML203-K367C + + P 90
pML203-K402C ND ND C 80

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES