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Salivary proteome of a Neotropical primate: potential roles in host defense and oral food perception

BACKGROUND: Saliva contains a very complex mixture of proteins for defense against microbiological pathogens and for oral food perception. Howler monkeys are Neotropical primates that can consume a mostly leaf diet. They are well known to thrive in highly disturbed habitats where they may cope with...

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Autores principales: Espinosa-Gómez, Fabiola Carolina, Ruíz-May, Eliel, Serio-Silva, Juan Carlos, Chapman, Colin A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7382365/
https://www.ncbi.nlm.nih.gov/pubmed/32765966
http://dx.doi.org/10.7717/peerj.9489
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author Espinosa-Gómez, Fabiola Carolina
Ruíz-May, Eliel
Serio-Silva, Juan Carlos
Chapman, Colin A.
author_facet Espinosa-Gómez, Fabiola Carolina
Ruíz-May, Eliel
Serio-Silva, Juan Carlos
Chapman, Colin A.
author_sort Espinosa-Gómez, Fabiola Carolina
collection PubMed
description BACKGROUND: Saliva contains a very complex mixture of proteins for defense against microbiological pathogens and for oral food perception. Howler monkeys are Neotropical primates that can consume a mostly leaf diet. They are well known to thrive in highly disturbed habitats where they may cope with a diversity of dietary challenges and infection risks. We aimed to describe the salivary proteome of howlers to contribute to better understanding of their physiology. METHODS: We analyzed the salivary proteins of wild black howler monkeys (Alouatta pigra), by SDS-PAGE-1-D and Nano LC-MS/MS and categorized them by their function involved in host defense and oral food perception. RESULTS: Our proteomic analysis identified 156 proteins in howler saliva including a number of host defense peptides that are the first line of defense in mammals, such as defensin, cathelicidin, dermcidin, and lactotransferrin, and proteins with anti-bacterial, anti-fungal, and anti-viral capacity, such as IgA, IgG, IgM, BPI, salivary heat shock 70 kDa protein, beta-2-microbulin, and protein S-100. We also identified key proteins necessary for taste perception, including salivary carbonic anhydrase VI, cystatin D, IgA, and fatty acid-binding protein. Proteins to detect astringent foods were identifying, including four members of cystatins (A, B, C and D), lactoperoxidase, and histidine-rich proteins. No chitinase and amylase were identified as would be expected because howlers do not eat insects and little starch. These findings provide basic information to future studies in oral biology, ingestive physiology, and physiological ecology of mammals and non-human primates.
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spelling pubmed-73823652020-08-05 Salivary proteome of a Neotropical primate: potential roles in host defense and oral food perception Espinosa-Gómez, Fabiola Carolina Ruíz-May, Eliel Serio-Silva, Juan Carlos Chapman, Colin A. PeerJ Animal Behavior BACKGROUND: Saliva contains a very complex mixture of proteins for defense against microbiological pathogens and for oral food perception. Howler monkeys are Neotropical primates that can consume a mostly leaf diet. They are well known to thrive in highly disturbed habitats where they may cope with a diversity of dietary challenges and infection risks. We aimed to describe the salivary proteome of howlers to contribute to better understanding of their physiology. METHODS: We analyzed the salivary proteins of wild black howler monkeys (Alouatta pigra), by SDS-PAGE-1-D and Nano LC-MS/MS and categorized them by their function involved in host defense and oral food perception. RESULTS: Our proteomic analysis identified 156 proteins in howler saliva including a number of host defense peptides that are the first line of defense in mammals, such as defensin, cathelicidin, dermcidin, and lactotransferrin, and proteins with anti-bacterial, anti-fungal, and anti-viral capacity, such as IgA, IgG, IgM, BPI, salivary heat shock 70 kDa protein, beta-2-microbulin, and protein S-100. We also identified key proteins necessary for taste perception, including salivary carbonic anhydrase VI, cystatin D, IgA, and fatty acid-binding protein. Proteins to detect astringent foods were identifying, including four members of cystatins (A, B, C and D), lactoperoxidase, and histidine-rich proteins. No chitinase and amylase were identified as would be expected because howlers do not eat insects and little starch. These findings provide basic information to future studies in oral biology, ingestive physiology, and physiological ecology of mammals and non-human primates. PeerJ Inc. 2020-07-22 /pmc/articles/PMC7382365/ /pubmed/32765966 http://dx.doi.org/10.7717/peerj.9489 Text en ©2020 Espinosa-Gómez et al. https://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Animal Behavior
Espinosa-Gómez, Fabiola Carolina
Ruíz-May, Eliel
Serio-Silva, Juan Carlos
Chapman, Colin A.
Salivary proteome of a Neotropical primate: potential roles in host defense and oral food perception
title Salivary proteome of a Neotropical primate: potential roles in host defense and oral food perception
title_full Salivary proteome of a Neotropical primate: potential roles in host defense and oral food perception
title_fullStr Salivary proteome of a Neotropical primate: potential roles in host defense and oral food perception
title_full_unstemmed Salivary proteome of a Neotropical primate: potential roles in host defense and oral food perception
title_short Salivary proteome of a Neotropical primate: potential roles in host defense and oral food perception
title_sort salivary proteome of a neotropical primate: potential roles in host defense and oral food perception
topic Animal Behavior
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7382365/
https://www.ncbi.nlm.nih.gov/pubmed/32765966
http://dx.doi.org/10.7717/peerj.9489
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