Hristo L. Svilenov

Apr 12, 2024 | onlinelibrary.wiley.com | Johannes Buchner |Hristo L. Svilenov |Johanna Trommer |Florian Lesniowski

1 INTRODUCTION In most mammalian antibodies, the complementarity-determining regions (CDRs) from both the heavy chain (HC) and the light chain (LC) form the antigen-binding site. There are only a few exceptions to this paradigm such as the HC-only antibodies in camelids (Hamers-Casterman et al., 1993) and the antibodies with ultra-long CDR-H3s in cattle (Wang et al., 2013).

Apr 8, 2023 | nature.com | Hristo L. Svilenov |Florent Delhommel |Grzegorz M. Popowicz

AbstractThe angiotensin-converting enzyme 2 (ACE2) is a viral receptor used by sarbecoviruses to infect cells. Fusion proteins comprising extracellular ACE2 domains and the Fc part of immunoglobulins exhibit high virus neutralization efficiency, but the structure and stability of these molecules are poorly understood. We show that although the hinge between the ACE2 and the IgG4-Fc is highly flexible, the conformational dynamics of the two ACE2 domains is restricted by their association.