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. 2010 Jan 22;192(7):1902–1911. doi: 10.1128/JB.01542-09

TABLE 3.

Binding properties of LT and CTB mutants

Mutant GM1 bindinga
Blood sugar bindingc
E. coli surface bindingd
% P valueb % P value % P value
LT[L25E] 69.3 ± 5.3e <0.005 64.2 ± 7.2 <0.01 35.2 ± 10.9 <0.005
LT[Q3K]f 96.0 ± 4.6 0.43 0.67 ± 0.43 <0.005 33.8 ± 8.8 <0.005
LT[Q3A] 95.5 ± 14.4 0.77 4.0 ± 4.0 2.3 × 10−6 36.5 ± 4.7 <0.0005
LT[E11K] 90.9 ± 4.6 0.08 109.6 ± 17.8 0.65 19.6 ± 9.3 <0.001
LT[E11A] 81.5 ± 6.5 0.07
CTB[Q3K] 93.1 ± 1.9 <0.05
CTB[E11K] 94.7 ± 2.5 0.08
CTB[E11A] 106.7 ± 1.8 <0.05
a

Purified toxin binding to GM1 was determined by ELISA; values are expressed as mean percentages of wild-type LT or CTB binding ±SEM (n ≥ 3).

b

P values are for comparison to wild-type binding as determined by Student's t test.

c

Purified toxin binding to blood group A trisaccharide conjugated to BSA was determined by ELISA; values are expressed as mean percentages of wild-type binding ±SEM (n ≥ 2).

d

Purified toxin binding to the surface of DH5α E. coli cells was determined by a previously described immunoblot-based binding assay (26); values are expressed as mean percentages of wild-type LT binding ±SEM (n ≥ 3).

e

Significant differences from wild-type (P < 0.05) are in bold.

f

Data for this mutant were reported previously (26).