Abstract
Since the first record of the five founder members of the group of Natterin proteins in the venom of the medically significant fish Thalassophryne nattereri, new sequences have been identified in other species. In this work, we performed a detailed screening using available genome databases across a wide range of species to identify sequence members of the Natterin group, sequence similarities, conserved domains, and evolutionary relationships. The high-throughput tools have enabled us to dramatically expand the number of members within this group of proteins, which has a remote origin (around 400 million years ago) and is spread across Eukarya organisms, even in plants and primitive Agnathans jawless fish. Overall, the survey resulted in 331 species presenting Natterin-like proteins, mainly fish, and 859 putative genes. Besides fish, the groups with more species included in our analysis were insects and birds. The number and variety of annotations increased the knowledge of the obtained sequences in detail, such as the conserved motif AGIP in the pore-forming loop involved in the transmembrane barrel insertion, allowing us to classify them as important constituents of the innate immune defense system as effector molecules activating immune cells by interacting with conserved intracellular signaling mechanisms in the hosts.
Highlights
The Natterin proteins were first revealed in the venom of the medically significant Brazilian toadfish Thalassophryne nattereri (VTn) in five orthologs named Natterin (1–4, and -P) [1]
Natterins-1–4 share a similar monomeric architecture, with two DM9 membranebinding domains, which were primarily found in Diptera proteins with unknown functions, in the N-terminal region and an aerolysin domain in the C-terminal, similar to the common core of the aerolysin produced by Aeromonas species [4], which are essential for toxicity [2,3] and membrane penetration [5]
We performed a detailed screening using available genome databases across a wide range of species to identify sequence members of the group of Natterin-like proteins to create phylogenetic relationships with T. nattereri, multiple sequence alignment, and conserved domain analysis. This is the first study that describes the overall distribution of Natterin-like proteins and extends the information about the domain architectures, conserved motifs located in the aerolysin domain for pore formation, and reveals and clarifies specific biological roles
Summary
The Natterin proteins were first revealed in the venom of the medically significant Brazilian toadfish Thalassophryne nattereri (VTn) in five orthologs named Natterin (1–4, and -P) [1]. We performed a detailed screening using available genome databases across a wide range of species to identify sequence members of the group of Natterin-like proteins to create phylogenetic relationships with T. nattereri, multiple sequence alignment, and conserved domain analysis. This is the first study that describes the overall distribution of Natterin-like proteins and extends the information about the domain architectures, conserved motifs located in the aerolysin domain for pore formation, and reveals and clarifies specific biological roles
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