© 2015 Ligabue-Braun et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The major cat allergen, Fel d 1, is a structurally complex protein with two N-glycosylation sites that may be filled by different glycoforms. In addition, the protein contains three putative Ca<sup>2+</sup> binding sites. Since the impact of these Fel d 1 structure modifications on the protein dynamics, physiology and pathology are not well established, the present work employed computational biology techniques to tackle these issues. While conformational effects brought upon by glycosylation were identified, potentially involved in cavity volume regulation, our results indicate that only the central Ca<sup>2+</sup>ion remains coordinated to Fel d 1 in biological solutions, impairing its proposed role in modulating phospholipase A<inf>2</inf> activity. As these results increase our understanding of Fel d 1 structural biology, they may offer new support for understanding its physiological role and impact into cat-promoted allergy.
Ligabue-Braun, R., Sachett, L. G., Pol-Fachin, L., & Verli, H. V. (2015). The calcium goes meow: Effects of ions and glycosylation on Fel d 1, the major cat allergen. PLoS ONE, 10(7). https://doi.org/10.1371/journal.pone.0132311