Expression of Chemosensory Protein (CSP) Structures in Pediculus humanis corporis and Acinetobacter baumannii

We parsed the microbial genome database using Bombyx mori chemosensory proteins (BmorCSPs) as templates. We extracted eleven bacterial CSPs (B-CSPs) from various microorganisms such as Kitasatospora griseola, K. purpeofusca, K. CB01950, K. MBT66, Escherichia coli, Macrococcus caseolyticus and Acinetobacter baumannii, a known infectious prokaryotic symbiont of various insects, particularly the human body louse. We then parsed the body louse Pediculus humanis corporis genomic database for CSPs. We found six P. humanis corporis (Phum) CSPs all grouped in the same gene cluster. Sequence alignment, structure modeling and phylogenetic analysis of CSP proteins in bacteria and insects reveal duplication, conservation, gene loss, but also diversification and neofunctionalization that took place at a common stage in this ancestral gene family. Phylogenetic analysis of the amino acid sequences also reveals association of CSPs with other prokaryotic gene families, mainly enzymes and secondary metabolites transporters. Their ability to bind lipids and their proved existence and diversity in infectious bacterial prokaryote systems strongly argue for some important general functions in the cellular metabolism process.