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The Lepidopteran endoribonuclease-U domain protein P102 displays dramatically reduced enzymatic activity and forms functional amyloids
Hemocytes of Heliothis virescens (F.) (Lepidoptera, Noctuidae) larvae produce a protein, P102, with a putative endoribonuclease-U domain. In previous works we have shown that P102 is involved in Lepidopteran immune response by forming amyloid fibrils, which catalyze and localize melanin deposition a...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Ltd.
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7124382/ https://www.ncbi.nlm.nih.gov/pubmed/25043263 http://dx.doi.org/10.1016/j.dci.2014.07.009 |
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author | Pascale, Mariarosa Laurino, Simona Vogel, Heiko Grimaldi, Annalisa Monné, Magnus Riviello, Lea Tettamanti, Gianluca Falabella, Patrizia |
author_facet | Pascale, Mariarosa Laurino, Simona Vogel, Heiko Grimaldi, Annalisa Monné, Magnus Riviello, Lea Tettamanti, Gianluca Falabella, Patrizia |
author_sort | Pascale, Mariarosa |
collection | PubMed |
description | Hemocytes of Heliothis virescens (F.) (Lepidoptera, Noctuidae) larvae produce a protein, P102, with a putative endoribonuclease-U domain. In previous works we have shown that P102 is involved in Lepidopteran immune response by forming amyloid fibrils, which catalyze and localize melanin deposition around non-self intruders during encapsulation, preventing harmful systemic spreading. Here we demonstrate that P102 belongs to a new class of proteins that, at least in Lepidoptera, has a diminished endoribonuclease-U activity probably due to the lack of two out of five catalytically essential residues. We show that the P102 homolog from Trichoplusia ni (Lepidoptera, Noctuidae) displays catalytic site residues identical to P102, a residual endoribonuclease-U activity and the ability to form functional amyloids. On the basis of these results as well as sequence and structural analyses, we hypothesize that all the Lepidoptera endoribonuclease-U orthologs with catalytic site residues identical to P102 form a subfamily with similar function. |
format | Online Article Text |
id | pubmed-7124382 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Elsevier Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71243822020-04-06 The Lepidopteran endoribonuclease-U domain protein P102 displays dramatically reduced enzymatic activity and forms functional amyloids Pascale, Mariarosa Laurino, Simona Vogel, Heiko Grimaldi, Annalisa Monné, Magnus Riviello, Lea Tettamanti, Gianluca Falabella, Patrizia Dev Comp Immunol Article Hemocytes of Heliothis virescens (F.) (Lepidoptera, Noctuidae) larvae produce a protein, P102, with a putative endoribonuclease-U domain. In previous works we have shown that P102 is involved in Lepidopteran immune response by forming amyloid fibrils, which catalyze and localize melanin deposition around non-self intruders during encapsulation, preventing harmful systemic spreading. Here we demonstrate that P102 belongs to a new class of proteins that, at least in Lepidoptera, has a diminished endoribonuclease-U activity probably due to the lack of two out of five catalytically essential residues. We show that the P102 homolog from Trichoplusia ni (Lepidoptera, Noctuidae) displays catalytic site residues identical to P102, a residual endoribonuclease-U activity and the ability to form functional amyloids. On the basis of these results as well as sequence and structural analyses, we hypothesize that all the Lepidoptera endoribonuclease-U orthologs with catalytic site residues identical to P102 form a subfamily with similar function. Elsevier Ltd. 2014-11 2014-07-18 /pmc/articles/PMC7124382/ /pubmed/25043263 http://dx.doi.org/10.1016/j.dci.2014.07.009 Text en Copyright © 2014 Elsevier Ltd. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Pascale, Mariarosa Laurino, Simona Vogel, Heiko Grimaldi, Annalisa Monné, Magnus Riviello, Lea Tettamanti, Gianluca Falabella, Patrizia The Lepidopteran endoribonuclease-U domain protein P102 displays dramatically reduced enzymatic activity and forms functional amyloids |
title | The Lepidopteran endoribonuclease-U domain protein P102 displays dramatically reduced enzymatic activity and forms functional amyloids |
title_full | The Lepidopteran endoribonuclease-U domain protein P102 displays dramatically reduced enzymatic activity and forms functional amyloids |
title_fullStr | The Lepidopteran endoribonuclease-U domain protein P102 displays dramatically reduced enzymatic activity and forms functional amyloids |
title_full_unstemmed | The Lepidopteran endoribonuclease-U domain protein P102 displays dramatically reduced enzymatic activity and forms functional amyloids |
title_short | The Lepidopteran endoribonuclease-U domain protein P102 displays dramatically reduced enzymatic activity and forms functional amyloids |
title_sort | lepidopteran endoribonuclease-u domain protein p102 displays dramatically reduced enzymatic activity and forms functional amyloids |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7124382/ https://www.ncbi.nlm.nih.gov/pubmed/25043263 http://dx.doi.org/10.1016/j.dci.2014.07.009 |
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