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Figure 3 - LPS profile of strains by SDS-PAGE. Mutant phenotype of ∆rfaF (lane 2) was restored to wildtype by complementing with an rfaF plasmid (lane 1).

Figure 5 - LPS profile of strains by SDS-PAGE. Mutant phenotype of ∆rfaC (lane 4) was restored to wildtype by complementing with an rfaC plasmid (lane 5).

Table 6 shows the dipeptidase activity of enterococci with VanD.

Table 2 shows that enterococci with VanD have high minimum inhibitory concentrations (MIC) of vancomycin.

Table 2 shows that cells transformed with plasmids containing vanY have higher minimum inhibitory concentrations (MIC) of vancomycin than cells without vanY.

Table 2 shows that cells with plasmids containing the vanZ gene have a higher minimum inhibitory concentration of teicoplanin than cells without the vanZ gene.

Fig. 2 shows the production of penicillin binding protein (PBP) in strains of Staphylococcus aureus transformed with pSP53 with the mecA gene.

Table 2 shows that in cells transformed with mecI, the beta-galactosidase activity of mecA-lacZ transcriptional fusion can be induced with the presence of CBAP. Furthermore, it is shown in Fig. 2 that mecI binds to a region of DNA between the mecA and mecR1 genes and protects it from DNase.

Fig. 2 shows that expression PBP 2a and beta-lactamase was repressed in cells transformed with blaI, but PBP 2a and beta-lactamase were expressed constitutively in untransformed cells. Furthermore, expression in transformed cells could be induced.

Figure 3 - Gas chromatograph of expressed core oligosaccharide. waaQ (3c) mutant expresses a truncated core, missing the terminal heptose (peak 6) as compared to wildtype (3a).

Figure 3 - Gas Chromatograph of core oligosaccharide. Compared to wildtype (3a), waaQ mutant (3c) is missing peak 6 (terminal heptose).

Figure 4a - LPS profile of strains by SDS-PAGE. Mutant phenotype of rfa-2 mutant strain (lane 3) was restored to wildtype by complementing with an rfa-2 plasmid (lane 1).

Figure 3 - Product in the presence of RfaF contains an additional heptose attached to Hep-Kdo2. Product in the absence of RfaF only contains Hep-Kdo2.

Figure 3 - Product in the presence of RfaC contains an additional heptose attached to Kdo2. Product in the absence of RfaC only contains Kdo2.

Fig. 2 is a TLC showing the D-alanine-D-alanine ligase activity of VanA. In the presence of VanA, the TLC shows that [14C]D-alanine is converted to [14C]D-alanine-D-alanine. In the absence of VanA, [14C]D-alanine does not form [14C]D-alanine-D-alanine.