HETEROGENEOUS PATTERNS OF ACID-PHOSPHATASES CONTAINING LOW-MOLECULAR-MASS POLYPEPTIDES IN MEMBERS OF THE FAMILY ENTEROBACTERIACEAE

We investigated expression of acid phosphatases containing low-molecul ar-mass (25 to 27-kDa) polypeptides (Lmmp-APs) similar to those descri bed previously for Salmonella enterica serovar typhimurium and Morgane lla morganii in strains that were representatives of 43 different ente robacterial species by using a zymogram technique developed for detect ion of Lmmp-AP activities and for analysis of some of the properties o f these enzymes. Under conditions that were suitable for detection of the previously described Lmmp-APs, production of similar enzymes appea red to be widespread but not universal among enteric bacteria, and het erogeneous patterns of expression were found among strains belonging t o different genera and, in some cases, among strains belonging to diff erent species of the same genus. We found that class A Lmmp-APs (i.e., Lmmp-Aps similar to the Morganella morganii PhoC and Salmonella enter ica serovar typhimurium PhoN acid phosphatases) were also expressed in Cedecea spp., Enterobacter aerogenes, Hafnia alvei, Klebsiella spp., Providencia stuartii, Serratia plymuthica, and Yokenella regensburgei strains and that class B Lmmp-APs (i.e., Lmmp-APs similar to the Morga nella morganii NapA and Salmonella enterica serovar typhimurium NapII acid phosphatases) were also expressed in strains of Citrobacter spp., Escherichia coli, Escherichia. fergusonii, Hafnia alvei, Proteus mira bilis, Providencia spp., Salmonella enterica serovar typhi, Shigella d ysenteriae, and Shigella flexneri. No Lmmp-AP activity was detected in strains of Enterobacter spp, other than Enterobacter aerogenes, Esche richia hermanii, Kluyvera ascorbata, Leclercia adecarboxylata, Leminor ella grimontii, Moellerella wisconsensis, Proteus vulgaris, Proteus pe nneri, Serratia spp. other than Serratia plymuthica, and Yersinia spp. Because of the heterogeneous patterns of expression of Lmmp-APs, anal ysis of these enzymes could be useful for evolutionary studies of the enterobacterial genome and for precise phylogenetic positioning of ent eric bacteria.