Biological Earth observation with animal sensors

Space-based tracking technology using low-cost miniature tags is now delivering data on fine-scale animal movement at near-global scale. Linked with remotely sensed environmental data, this offers a biological lens on habitat integrity and connectivity for conservation and human health; a global network of animal sentinels of environmental change.Publisher PDFPeer reviewe

Introducing a unique animal ID and digital life history museum for wildlife metadata

Funding: C.R. acknowledges funding from the Gordon and Betty Moore Foundation (GBMF9881) and the National Geographic Society (NGS-82515R-20). G.B., R.K., S.C.D. and D.E.-S. acknowledge funding from NASA. A.S. and F.I. acknowledge support from the European Commission through the Horizon 2020 Marie Skłodowska-Curie Actions Individual Fellowships (grant no. 101027534 and no. 101107666, respectively). S.C.D. acknowledges funding from NASA Ecological Forecasting Program Grant 80NSSC21K1182. A.M.M.S. was supported by an ARC DP DP210103091. This project is funded in part by the Gordon and Betty Moore Foundation through Grant GBMF10539 to M.W., as well as the Academy for the Protection of Zoo Animals and Wildlife e.V., Germany.1. Over the past five decades, a large number of wild animals have been individually identified by various observation systems and/or temporary tracking methods, providing unparalleled insights into their lives over both time and space. However, so far there is no comprehensive record of uniquely individually identified animals nor where their data and metadata are stored, for example photos, physiological and genetic samples, disease screens, information on social relationships. 2. Databases currently do not offer unique identifiers for living, individual wild animals, similar to the permanent ID labelling for deceased museum specimens. 3. To address this problem, we introduce two new concepts: (1) a globally unique animal ID (UAID) available to define uniquely and individually identified animals archived in any database, including metadata archived at the time of publication; and (2) the digital ‘home’ for UAIDs, the Movebank Life History Museum (MoMu), storing and linking metadata, media, communications and other files associated with animals individually identified in the wild. MoMu will ensure that metadata are available for future generations, allowing permanent linkages to information in other databases. 4. MoMu allows researchers to collect and store photos, behavioural records, genome data and/or resightings of UAIDed animals, encompassing information not easily included in structured datasets supported by existing databases. Metadata is uploaded through the Animal Tracker app, the MoMu website, by email from registered users or through an Application Programming Interface (API) from any database. Initially, records can be stored in a temporary folder similar to a field drawer, as naturalists routinely do. Later, researchers and specialists can curate these materials for individual animals, manage the secure sharing of sensitive information and, where appropriate, publish individual life histories with DOIs. The storage of such synthesized lifetime stories of wild animals under a UAID (unique identifier or ‘animal passport’) will support basic science, conservation efforts and public participation.Peer reviewe

Biological Earth observation with animal sensors

Space-based tracking technology using low-cost miniature tags is now delivering data on fine-scale animal movement at near-global scale. Linked with remotely sensed environmental data, this offers a biological lens on habitat integrity and connectivity for conservation and human health; a global network of animal sentinels of environmen-tal change

Biological Earth observation with animal sensors

Space-based tracking technology using low-cost miniature tags is now delivering data on fine-scale animal movement at near-global scale. Linked with remotely sensed environmental data, this offers a biological lens on habitat integrity and connectivity for conservation and human health; a global network of animal sentinels of environmental change.Correction published in: Walter Jetz, Grigori Tertitski, Roland Kays, Uschi Mueller, Martin Wikelski. Biological Earth observation with animal sensors: (Trends in Ecology and Evolution 37, 293–298; 2022), Trends in Ecology &amp; Evolution, Volume 37, Issue 8, 2022, Pages 719-724, https://doi.org/10.1016/j.tree.2022.04.012</p

Identification of a Novel TGF-beta-Binding Site in the Zona Pellucida C-terminal (ZP-C) Domain of TGF-β\beta-Receptor-3 (TGFR-3)

The zona pellucida (ZP) domain is present in extracellular proteins such as the zona pellucida proteins and tectorins and participates in the formation of polymeric protein networks. However, the ZP domain also occurs in the cytokine signaling co-receptor transforming growth factor beta (TGF-$\beta$) receptor type 3 (TGFR-3, also known as betaglycan) where it contributes to cytokine ligand recognition. Currently it is unclear how the ZP domain architecture enables this dual functionality. Here, we identify a novel major TGF-beta-binding site in the FG loop of the C-terminal subdomain of the murine TGFR-3 ZP domain (ZP-C) using protein crystallography, limited proteolysis experiments, surface plasmon resonance measurements and synthetic peptides. In the murine 2.7 angstrom crystal structure that we are presenting here, the FG-loop is disordered, however, well-ordered in a recently reported homologous rat ZP-C structure. Surprisingly, the adjacent external hydrophobic patch (EHP) segment is registered differently in the rat and murine structures suggesting that this segment only loosely associates with the remaining ZP-C fold. Such a flexible and temporarily-modulated association of the EHP segment with the ZP domain has been proposed to control the polymerization of ZP domain-containing proteins. Our findings suggest that this flexibility also extends to the ZP domain of TGFR-3 and might facilitate co-receptor ligand interaction and presentation via the adjacent FG-loop. This hints that a similar C-terminal region of the ZP domain architecture possibly regulates both the polymerization of extracellular matrix proteins and cytokine ligand recognition of TGFR-3

Data and refinement statistics of mouse TGFR-3-ZP-C.

<p>+ Numbers in parenthesis are for the highest-resolution shell. # 5% of reflections have been chosen as <i>R</i>_free set. <i>R</i>_sym is calculated as where <i>I_i</i> is the <i>i^th</i> observation of the n^th reflection and <<i>I</i>> the mean of all observations of the n^th reflection. ## Calculated with program COOT <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0067214#pone.0067214-Emsley1" target="_blank">[35]</a>.</p

Crystal structure of murine TGFR-3-ZP-C.

<p>(<b>A</b>) Stereographic ribbon representation of the murine TGFR-3-ZP-C structure (in blue and red). The ZP-C domain in the crystals extends from Thr591 to Asp757. No density is visible for residues 730 to 744. The FG loop connecting β-strands F to G (residues 711 to 746) and β-strand G are shown in red. The EHP segment that is part of β-strand G is marked. For comparison reason the structure of rat ZP-C (PDB entry 3QW9, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0067214#pone.0067214-Lin1" target="_blank">[13]</a>) that was used to solve the structure of murine ZP-C is shown in transparent grey and light red. In contrast to the murine ZP-C structure, the entire FG loop is visible in the rat ZP-C structure. Chain breaks in the murine ZP-C structure are marked with black dots. (<b>B</b>) Stereographic representation of the rat and murine ZP-C structure identical to that in panel (A) but after application of an approximately 110° rotation around a vertical axis.</p

Domain organization and features of murine TGFR-3 and variants.

<p>First line: Domain representation of wild-type full-length TGFR-3 emphasizing the membrane-distal and –proximal domain in the TGFR-3 ectodomain. The transmembrane-domain (TM), the signal sequence (S), GAG chains (circles) and potential N-glycosylation sites (hexagons) are also indicated. Second line: The recombinant variant TGFR-3-ZP used in this study comprises residues 438–782 of murine TGFR-3, includes the EHP and features a thrombin-cleavable N-terminal His-tag. The bioinformatically delineated ZP core domain (residues 454–728) is highlighted by a shaded area <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0067214#pone.0067214-Bork1" target="_blank">[9]</a>. In variant TGFR-3-ZP(234) (not shown) the asparagine residues from three out of four potential N-glycosylation sites were mutated to glutamines. Third line: In variant TGFR-3-ZP(ΔC) C-terminal residues were cleaved-off by limited proteolysis. Fourth line: ZP-C fragment as observed in the crystal structure. Subsequent lines display the sequences of the C-terminus mimetic peptides P1 to P5 of human and murine receptor mimetic peptides of TGFR-3-ZP investigated in this study.</p