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

• Published in: PeerJ (San Francisco, CA) CA), 2020-07, Vol.8, p.e9489-e9489, Article e9489
• Main Authors: Espinosa-Gómez, Fabiola Carolina, Ruíz-May, Eliel, Serio-Silva, Juan Carlos, Chapman, Colin A
• Format: Article
• Language: English
• Subjects: Amylases; Animal Behavior; Anthropology; Antimicrobial agents; Antiviral agents; Carbonic anhydrases; Chitinase; Cystatins; Diet; Fatty acid-binding protein; Fatty acids; Food; Gel electrophoresis; Glycoproteins; Health aspects; Heat shock proteins; Histidine; Host-defense; Howler monkeys; Immunoglobulin A; Immunoglobulin G; Immunoglobulin M; Metabolites; Pathogens; Peptides; Physiological aspects; Polyphenols; Primates; Protein binding; Protein S; Proteins; Proteomes; Saliva; Salivary proteome; Scientific equipment industry; Sodium lauryl sulfate; Starch; Taste perception; Veterinary Medicine; Zoology
• ISSN: 2167-8359; 2167-8359
• DOI: 10.7717/peerj.9489

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. We analyzed the salivary proteins of wild black howler monkeys ( ), by SDS-PAGE-1-D and Nano LC-MS/MS and categorized them by their function involved in host defense and oral food perception. 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.