, 2003; Giles et al., 2009). Due to the early truncation of the C. trachomatis serovar L2 AaxB, the anti-AaxB antibody, which was developed against a conserved peptide after the truncation, would not recognize this serovar if truncated protein is produced. However, previous data using an E. coli surrogate Alectinib price expression system indicate that this protein may not be produced (Giles et al., 2009). The total protein level of AaxB in C. trachomatis serovar E also appeared to be lower than the non-C. trachomatis variants

(possibly indicating decreased expression levels), and the acid resistance phenotype of the serovar E AaxB-producing strain was the weakest of the complementing strains. As the only C. trachomatis serovar expressing active AaxB, it is possible that the serovar E strains represent an intermediate phenotype between isolates

that have maintained or lost UK-371804 mw enzyme functionality. Several studies suggest that there is no association between infections with C. trachomatis serovar E and presence or absence of clinical infection or specific symptoms, although this serovar is one of the most prevalent worldwide (Van der Laar et al., 1996; Morré et al., 2000; review, Byrne, 2010). As the other genital serovars (D, F–K) occupy the same niche, it is unlikely that serovar E requires active AaxB when the other serovars have lost functionality. This, coupled with the low AaxB levels detected during in vitro infection, suggests that although C. trachomatis serovar E currently retains active AaxB, this serovar may be in the process of inactivating this enzyme. While C. pneumoniae

and many of the non-C. trachomatis serovars retain an active ArgDC, the function of this DCLK1 enzyme in Chlamydia remains obscure. Although ArgDCs in other bacteria play roles in acid resistance and/or polyamine metabolism, neither function appears relevant to Chlamydia. The Chlamydia inclusion remains at neutral pH throughout infection, so encounters with acidic environments are unlikely (Schramm et al., 1996; Al-Younes et al., 1999; Grieshaber et al., 2002). Additionally, there are no known Chlamydia enzymes able to metabolize agmatine, such as the agmatine ureohydrolase, and therefore AaxB cannot contribute to polyamine synthesis. Finally, in certain cell lines, addition of exogenous agmatine alone may provide protection against cellular apoptosis (Arndt et al., 2009), but investigation in our laboratory suggests that this is likely not a factor during Chlamydia infection (data not shown). As Giles & Graham (2007) have speculated previously, the most likely function for the arginine decarboxylase system during Chlamydia infection is depletion of host cell arginine reserves.