Summary: Transmission of species from ectoparasites to the mammalian host involves adaptation to thermal and other forms of stress. In order to better understand this process, the heat shock response of and was studied. Cellular proteins synthesized after shift to higher temperatures were intrinsically labelled with [S]methionine and analysed by gel electrophoresis and fluorography. The apparent molecular masses of three of the major heat shock proteins produced by the two species were virtually identical, migrating at 70, 60 and 10 kDa. A fourth major heat shock protein was larger in (20 kDa) than in (17 kDa). The maximum heat shock response in and was observed at 39 °C and 42 °C, respectively. The genes of both species were amplified, sequenced and compared to other known genes. The phylogenetic tree based on the alignment places and in a monophyletic group with . The deduced amino acid sequences of GroEL homologues contain signature sequences that are uniquely shared by members of the Gram-negative α-purple subdivision of bacteria, which live within eukaryotic cells. Recombinant His-GroEL fusion proteins were expressed in to generate specific rabbit antisera. The GroEL antisera were used to confirm the identity of the 60 kDa heat shock protein. These studies provide a foundation for evaluating the role of the heat shock response in the pathogenesis of infection.


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