Advancing Discovery of Snail Mucins Function and Application

Abstract

Mucins are a highly glycosylated protein family that are secreted by animals for adhesion, hydration, lubrication, and other functions. Despite their ubiquity, animal mucins are largely uncharacterized. Snails produce mucin proteins in their mucous for a wide array of biological functions, including microbial protection, adhesion and lubrication. Recently, snail mucins have also become a lucrative source of innovation with wide ranging applications across chemistry, biology, biotechnology, and biomedicine. Specifically, snail mucuses have been applied as skin care products, wound healing agents, surgical glues, and to combat gastric ulcers. Recent advances in integrated omics (genomic, transcriptomic, proteomic, glycomic) technologies have improved the characterization of gastropod mucins, increasing the generation of novel biomaterials. This perspective describes the current research on secreted snail mucus, highlighting the potential of this biopolymer, and also outlines a research strategy to fulfill the unmet need of examining the hierarchical structures that lead to the enormous biological and chemical diversity of snail mucus genes.

Keywords: biopolymer; biotechnology; cosmetics; mucins; mucus; snails.

FIGURE 1

(A) Applications of snail mucus. Snail mucus has been used for skin care, wound healing and rejuvenation, and drug delivery. Snail mucus is being explored in food science, implant coatings, and other biotechnical sectors are currently researching mucins to be explored for potential use. (B) A 2-dimensional representation of the mucin structures. Mucins are characterized by two parts of their structure, their protein core, and their glycan branching. The protein core is a protein sequence of variable length depending on the mucin gene, which has been further modified with glycosylation branches. The Protein structure, however has multiple domains, and these domains vary depending on the function and the cellular location of the mucin. The glycan branches are sugar branches ranging from 3 to 18 sugars, and make up the majority of the mucin mass. Shown are 2 dimensional representations of the different types of mucins, and their stereotypical features. (C) Applying an integrated omics approach to identify snail mucin sequence, structure, and function. Path 1(left) extract crude mucin proteins and separate from the cellular debris to obtain sequence masses from spectroscopic and mass spectrometric analyses. Path 2(right) RNA extraction from mucus glands or whole animal followed by de novo assembly of mucin gene sequences to generate a database to BLAST against by a comparison of assembled sequences to a known mucin database, we obtain putative mucin sequences. Combining the proteomic and RNA pipelines we confirm the native type mucin sequence for further analysis.