Abstract
Acanthamoeba is a ubiquitous free-living amoeba capable of being an opportunistic pathogen in humans and animals. A critical step in infection is the adhesion of the amoeba to host cells and tissues, and two major parasite adhesins, mannose-binding protein (MBP) and laminin-binding protein (LBP), are known to recognize the cell surface glycoproteins and those of the extracellular matrix, respectively. In this study, the available genomes of Acanthamoeba were analysed to recover the sequences of MBP and LBP using previously published genetic data. Genes for both proteins were successfully obtained from strains belonging to various genotypes (T4A, T4D, T4G, T4F, T2, T5, T10, T22, T7 and T18), resulting in a single gene for LBP but identifying two types of MBP, MBP1 and MBP2. Phylogenetic analysis based on deduced amino acid sequences shows that both MBP and LBP have a branching pattern that is consistent with that based on 18S rDNA, indicating that changes in both proteins occurred during diversification of Acanthamoeba lines. Notably, all MBPs possess a conserved motif, shared with some bacterial C-type lectins, which could be the recognition site for mannose binding.