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McMahon, C.

Publications and source records attributed to McMahon, C..

2 recordsLinked to original sources

Movement behaviour responses to environment: fast inference of individual variation with a mixed effects model

Like many species, movement patterns of southern elephant seals (Mirounga leonina) are being influenced by long-term environmental change. These seals migrate up to 4000 km from their breeding colonies, foraging for months in a variety of Southern Ocean habitats. Understanding how movement patterns vary with environmental features and how these relationships differ among individuals employing different foraging strategies can provide insight into foraging performance at a population level. We apply new fast-estimation tools to fit mixed effects within a random walk movement model, rapidly inferring among-individual variability in southern elephant seal environment-movement relationships. We found that seals making foraging trips to the sea-ice on or near the Antarctic continental shelf consistently reduced speed and directionality (move persistence) with increasing sea ice coverage and had variable responses to chlorophyll a concentration, whereas seals that foraged pelagically reduced move persistence in regions where circumpolar deep water shoaled. Given future climate scenarios, pelagic foragers may encounter more productive habitat but sea-ice foragers may see reduced habitat availability. Our approach is scalable to large telemetry data sets and allows flexible combinations of mixed effects to be evaluated via model selection, thereby illuminating the ecological context of animal movements that underlie habitat use.

ecology

Platform for rapid nanobody discovery in vitro

Camelid single-domain antibody fragments (\"nanobodies\") provide the remarkable specificity of antibodies within a single immunoglobulin VHH domain. This unique feature enables applications ranging from their use as biochemical tools to therapeutic agents. Virtually all nanobodies reported to date have been obtained by animal immunization, a bottleneck restricting many applications of this technology. To solve this problem, we developed a fully in vitro platform for nanobody discovery based on yeast surface display of a synthetic nanobody scaffold. This platform provides a facile and cost-effective method for rapidly isolating nanobodies targeting a diverse range of antigens. We provide a blueprint for identifying nanobodies starting from both purified and non-purified antigens, and in addition, we demonstrate application of the platform to discover rare conformationally-selective nanobodies to a lipid flippase and a G protein-coupled receptor. To facilitate broad deployment of this platform, we have made the library and all associated protocols publicly available.

biochemistry