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Templeton, C.

Publications and source records attributed to Templeton, C..

2 recordsLinked to original sources

Swainson's thrushes vary song structure and singing behavior across ambient noise gradients and rapidly adjust songs in response to experimental traffic noise

Anthropogenic noise pollution has a variety of negative consequences for animals, with observed effects ranging from physiological processes to community structures. Sound waves from anthropogenic noise can mask animal signals, creating challenges for animal communication. Songbirds have been observed to combat noise pollution by changing their song rate, duration, frequency, or amplitude, with different species employing different strategies. We examined whether Swainsons thrushes (Catharus usulatus) adjust their song structure under different traffic noise regimens using both population level surveys and individual level noise playback experiments. Swainsons thrushes song frequency varied with background traffic noise levels across the surveyed population, but other song parameters did not. When confronted with realistic levels of experimental traffic noise playback, individual thrushes rapidly changed their song structure, increasing both the duration and the minimum frequency of their songs, before quickly returning towards baseline levels after the noise playback ended. Together, these results suggest that Swainsons thrushes are adjusting their singing to reduce acoustic masking in noisy areas and further indicate that some songbirds might continually assess ambient noise levels and only adjust their signals when necessary.

animal behavior and cognition↗

Role of Long-range Allosteric Communication in Determining the Stability and Disassembly of SARS-COV-2 in Complex with ACE2

Severe acute respiratory syndrome (SARS) and novel coronavirus disease (COVID-19) are caused by two closely related beta-coronaviruses, SARS-CoV and SARS-CoV-2, respectively. The envelopes surrounding these viruses are decorated with spike proteins, whose receptor binding domains (RBDs) initiate invasion by binding to the human angiotensin-converting enzyme 2 (ACE2). Subtle changes at the interface with ACE2 seem to be responsible for the enhanced affinity for the receptor of the SARS-CoV-2 RBD compared to SARS-CoV RBD. Here, we use Elastic Network Models (ENMs) to study the response of the viral RBDs and ACE2 upon dissassembly of the complexes. We identify a dominant detachment mode, in which the RBD rotates away from the surface of ACE2, while the receptor undergoes a conformational transition which stretches the active-site cleft. Using the Structural Perturbation Method, we determine the network of residues, referred to as the Allostery Wiring Diagram (AWD), which drives the large-scale motion activated by the detachment of the complex. The AWD for SARS-CoV and SARS-CoV-2 are remarkably similar, showing a network that spans the interface of the complex and reaches the active site of ACE2, thus establishing an allosteric connection between RBD binding and receptor catalytic function. Informed in part by the AWD, we used Molecular Dynamics simulations to probe the effect of interfacial mutations in which SARS-CoV-2 residues are replaced by their SARS-CoV counterparts. We focused on a conserved glycine (G502 in SARS-CoV-2, G488 in SARS-CoV) because it belongs to a region that initiates the dissociation of the complex along the dominant detachment mode, and is prominent in the AWD. Molecular Dynamics simulations of SARS-CoV-2 wild-type and G502P mutant show that the affinity for the human receptor of the mutant is drastically diminished. Our results suggest that in addition to residues that are in direct contact with the interface those involved in long range allosteric communication are also a determinant of the stability of the RBD-ACE2 complex.

biophysics↗