The arrangement of some of these genes in A. pleuropneumoniae, however, differs from that found in E. coli. As in E. coli, MalT appears to be a positive transcriptional
regulator of lamB in A. pleuropneumoniae as demonstrated by a two-fold decrease in the expression of lamB in the isogenic malT mutant of A. pleuropneumoniae CM5 in BHI supplemented with maltose (Table 5). This finding is consistent with an earlier phenotypic study  which reported that A. pleuropneumoniae expresses a LamB-like outer membrane protein when maltose is added to BHI agar. Moreover, the A. pleuropneumoniae MalT and LamB has a high degree of amino acid similarity with MalT and LamB homologs of a number of other Gram-negative organisms. Also, MalT has a conserved DNA-binding (LuxR-like C-terminal containing helix-turn-helix) motif INK1197 such as found in the E. coli MalT protein. To further examine the effect of the malT mutation on the regulation of the maltose regulon, both the wild-type organism and the malT mutant were grown in the presence of acarbose. Acarbose is a pseudo-oligosaccharide similar in structure to maltotetraose and it is a competitive inhibitor of maltose transport in E. coli. It can inhibit maltose uptake only if maltose-transport system is first activated by A-1155463 in vivo maltose. Acarbose also Sepantronium in vitro inhibits α-amylases and α-glucosidases and is not degraded by E. coli . In BHI supplemented with maltose, acarbose reduced the growth of the wild-type organism as well as that
of the malT mutant (Figure 3). The reduction in the Farnesyltransferase growth might have been caused either by accumulation of toxic levels of acarbose by the bacterial cells or by the inhibition of bacterial glucosidases by the accumulating acarbose, or both. The reduction was, however, significantly (P < 0.05) greater in the wild-type organism than in the mutant. This is perhaps due to the increased uptake of acarbose by the wild-type organism, owing to its higher
activation of the maltose regulon by the intact malT. On the other hand, the reduction in the growth of the malT mutant could have been due to the non-specific entry of acarbose into the bacterial cells. As A. pleuropneumoniae CM5 is not amenable to complementation it should be noted that we can not rigorously exclude the possibility that the phenotype exhibited by the malT negative strain was affected by some alteration of another gene that occurred during strain construction, but this is very unlikely. That said, taken together, the above findings suggest that A. pleuropneumoniae has a functional maltose regulon similar to that of E. coli. malT is required for optimum survival of A. pleuropneumoniae CM5 in serum and high concentrations of sodium chloride In comparison with the wild-type A. pleuropneumoniae CM5 and lamB mutant, the malT mutant had a significantly decreased ability to survive following incubation in fresh porcine serum for 1 h; the wild-type organism, however, grew in serum to a significantly higher number (Figure 4).