Skip to main content
. 2013 Mar;195(5):977–989. doi: 10.1128/JB.01274-12

Table 2.

S-layer and S-layer-associated protein distribution in B. anthracis wild-type and mutant strains

Protein and fraction Amt of protein in the indicated strain (%)a
Wild type csaB mutant patA1 mutant patA2 mutant patA1 patA2 mutant
Sap
    Medium 45 (±5) 99 (±1) 38 (±9) 37 (±4) 47 (±2)
    S-layer 41 (±4) 0 (±0) 44 (±3) 41 (±5) 44 (±8)
    Cell 13 (±7) 1 (±1) 17 (±9) 22 (±3) 9 (±10)
EA1
    Medium 55 (±12) 100 (±0) 85 (±5) 71 (±7) 88 (±9)
    S-layer 43 (±12) 0 (±0) 12 (±4) 24 (±7) 7 (±4)
    Cell 2 (±1) 0 (±0) 3 (±0) 5 (±2) 5 (±7)
BslA
    Medium 55 (±1) 100 (±0) 95 (±6) 83 (±6) 90 (±7)
    S-layer 44 (±1) 0 (±0) 3 (±4) 15 (±8) 9 (±6)
    Cell 1 (±1) 0 (±0) 1 (±2) 2 (±2) 1 (±1)
BslO
    Medium 19 (±6) ND 22 (±13) 24 (±16) 55 (±10)
    S-layer 77 (±9) ND 72 (±2) 67 (±26) 45 (±9)
    Cell 4 (±3) ND 7 (±6) 10 (±10) 1 (±1)
a

The immunoblot signals of two S-layer proteins (Sap, surface array protein, and EA1 extractable antigen 1) and two S-layer-associated proteins (BslA and BslO, S-layer-associated proteins A and O, respectively) in the medium, S-layer, and cell fraction of B. anthracis cultures were quantified in triplicate (Fig. 2). The mean and associated standard deviation of the percent amount in each fraction is presented here. The percentage of Sap that was retained in the S-layer did not change in strains with mutations in patA1 or patA2. These strains showed defects in the S-layer retention of EA1, BslA, and BslO. ND, not detected.