Meeting Abstract
Matrix Metalloproteinases (MMPs) are conserved zinc-dependent endopeptidases found across all kingdoms of life. They are members of a diverse protein family characterized by their catalytic domain, Metzincin, and are divided into subfamilies based on domain architecture and functional properties. Other major functional domains found in MMPs are the N-terminus propepetide domain which plays a regulatory role and the hemopexin domain. MMPs play roles in tissue remodeling events, such as wound repair and regeneration, and activate other proteins through proteolytic activity, namely signaling pathways regulating immunity. This class of metalloproteinases has been widely studied in vertebrate model systems but less so in early diverging metazoans that lack “complex” extracellular matrix structures. Thus, MMP’s ancestral role in metazoans has yet to be determined. Ctenophores are planktonic, marine invertebrates which recent molecular studies have placed as the earliest diverging extant group of animals. Furthermore, ctenophores have been shown to exhibit rapid wound repair and regenerative properties suggesting involvement of MMPs. In this study, we analyze transcriptomic and genomic data through bioinformatics pipelines to reveal the presence of putative MMPs amongst ctenophore and other non-bilaterian taxa. Primary putative homologs were filtered through a series of inclusion criteria including size and domain presence. Each of the MMP amino acid sequences include: a highly conserved cysteine switch motif in the N-terminus indicating the presence of the propeptide domain, a zinc-dependent catalytic domain, and the signature hemopexin. Phylogenetic relationships amongst MMP homologs were inferred through the construction of gene trees.
