Dataset Information

Chemical characterization of the adhesive secretions of the salamander Plethodon shermani (Caudata, Plethodontidae).

ABSTRACT: Salamanders have developed a wide variety of antipredator mechanisms, including tail autotomy, colour patterns, and noxious skin secretions. As an addition to these tactics, the red-legged salamander (Plethodon shermani) uses adhesive secretions as part of its defensive strategy. The high bonding strength, the fast-curing nature, and the composition of the biobased materials makes salamander adhesives interesting for practical applications in the medical sector. To understand the adhesive secretions of P. shermani, its components were chemically analysed by energy dispersive X-ray spectroscopy (EDX), inductively coupled plasma mass spectrometry (ICP-MS), amino acid analysis, and spectroscopy (ATR-IR, Raman). In addition, proteins were separated by gel-electrophoresis and selected spots were characterised by peptide mass fingerprinting. The salamander secretion contains a high amount of water and predominantly proteins (around 77% in the dry stage). The gel-electrophoresis and peptide mass fingerprint analyses revealed a de novo set of peptides/proteins, largely with a pI between 5.0 and 8.0 and a molecular mass distribution between 10 and 170?kDa. Only low homologies with other proteins present in known databases could be identified. The results indicate that the secretions of the salamander Plethodon clearly differ chemically from those shown for other glue-producing terrestrial or marine species and thus represent a unique glue system.

SUBMITTER: von Byern J

PROVIDER: S-EPMC5532285 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Chemical characterization of the adhesive secretions of the salamander Plethodon shermani (Caudata, Plethodontidae).

von Byern Janek J Grunwald Ingo I Kosok Max M Saporito Ralph A RA Dicke Ursula U Wetjen Oliver O Thiel Karsten K Borcherding Kai K Kowalik Thomas T Marchetti-Deschmann Martina M

Scientific reports 20170727 1

Salamanders have developed a wide variety of antipredator mechanisms, including tail autotomy, colour patterns, and noxious skin secretions. As an addition to these tactics, the red-legged salamander (Plethodon shermani) uses adhesive secretions as part of its defensive strategy. The high bonding strength, the fast-curing nature, and the composition of the biobased materials makes salamander adhesives interesting for practical applications in the medical sector. To understand the adhesive secret ...[more]

PMID: 28751633

Similar Datasets

Project description:In response to pervasive sexual selection, protein sex pheromones often display rapid mutation and accelerated evolution of corresponding gene sequences. For proteins, the general dogma is that structure is maintained even as sequence or function may rapidly change. This phenomenon is well exemplified by the three-finger protein (TFP) superfamily: a diverse class of vertebrate proteins co-opted for many biological functions - such as components of snake venoms, regulators of the complement system, and coordinators of amphibian limb regeneration. All of the >200 structurally characterized TFPs adopt the namesake "three-finger" topology. In male red-legged salamanders, the TFP pheromone Plethodontid Modulating Factor (PMF) is a hypervariable protein such that, through extensive gene duplication and pervasive sexual selection, individual male salamanders express more than 30 unique isoforms. However, it remained unclear how this accelerated evolution affected the protein structure of PMF. Using LC/MS-MS and multidimensional NMR, we report the 3D structure of the most abundant PMF isoform, PMF-G. The high resolution structural ensemble revealed a highly modified TFP structure, including a unique disulfide bonding pattern and loss of secondary structure, that define a novel protein topology with greater backbone flexibility in the third peptide finger. Sequence comparison, models of molecular evolution, and homology modeling together support that this flexible third finger is the most rapidly evolving segment of PMF. Combined with PMF sequence hypervariability, this structural flexibility may enhance the plasticity of PMF as a chemical signal by permitting potentially thousands of structural conformers. We propose that the flexible third finger plays a critical role in PMF:receptor interactions. As female receptors co-evolve, this flexibility may allow PMF to still bind its receptor(s) without the immediate need for complementary mutations. Consequently, this unique adaptation may establish new paradigms for how receptor:ligand pairs co-evolve, in particular with respect to sexual conflict.

Dataset Information

Chemical characterization of the adhesive secretions of the salamander Plethodon shermani (Caudata, Plethodontidae).

Publications

Chemical characterization of the adhesive secretions of the salamander Plethodon shermani (Caudata, Plethodontidae).

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets