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The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function

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...

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Autores principales: Lima, Carla, Disner, Geonildo Rodrigo, Falcão, Maria Alice Pimentel, Seni-Silva, Ana Carolina, Maleski, Adolfo Luis Almeida, Souza, Milena Marcolino, Reis Tonello, Mayara Cristina, Lopes-Ferreira, Monica
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402412/
https://www.ncbi.nlm.nih.gov/pubmed/34437409
http://dx.doi.org/10.3390/toxins13080538
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author Lima, Carla
Disner, Geonildo Rodrigo
Falcão, Maria Alice Pimentel
Seni-Silva, Ana Carolina
Maleski, Adolfo Luis Almeida
Souza, Milena Marcolino
Reis Tonello, Mayara Cristina
Lopes-Ferreira, Monica
author_facet Lima, Carla
Disner, Geonildo Rodrigo
Falcão, Maria Alice Pimentel
Seni-Silva, Ana Carolina
Maleski, Adolfo Luis Almeida
Souza, Milena Marcolino
Reis Tonello, Mayara Cristina
Lopes-Ferreira, Monica
author_sort Lima, Carla
collection PubMed
description 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.
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spelling pubmed-84024122021-08-29 The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function Lima, Carla Disner, Geonildo Rodrigo Falcão, Maria Alice Pimentel Seni-Silva, Ana Carolina Maleski, Adolfo Luis Almeida Souza, Milena Marcolino Reis Tonello, Mayara Cristina Lopes-Ferreira, Monica Toxins (Basel) Review 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. MDPI 2021-07-31 /pmc/articles/PMC8402412/ /pubmed/34437409 http://dx.doi.org/10.3390/toxins13080538 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Lima, Carla
Disner, Geonildo Rodrigo
Falcão, Maria Alice Pimentel
Seni-Silva, Ana Carolina
Maleski, Adolfo Luis Almeida
Souza, Milena Marcolino
Reis Tonello, Mayara Cristina
Lopes-Ferreira, Monica
The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function
title The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function
title_full The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function
title_fullStr The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function
title_full_unstemmed The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function
title_short The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function
title_sort natterin proteins diversity: a review on phylogeny, structure, and immune function
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8402412/
https://www.ncbi.nlm.nih.gov/pubmed/34437409
http://dx.doi.org/10.3390/toxins13080538
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