Dynamics Rationalize Proteolytic Susceptibility of the Major Birch Pollen Allergen Bet v 1.

ABSTRACT: Proteolytic susceptibility during endolysosomal degradation is decisive for allergic sensitization. In the major birch pollen allergen Bet v 1 most protease cleavage sites are located within its secondary structure elements, which are inherently inaccessible to proteases. The allergen thus must unfold locally, exposing the cleavage sites to become susceptible to proteolysis. Hence, allergen cleavage rates are presumed to be linked to their fold stability, i.e., unfolding probability. Yet, these locally unfolded structures have neither been captured in experiment nor simulation due to limitations in resolution and sampling time, respectively. Here, we perform classic and enhanced molecular dynamics (MD) simulations to quantify fold dynamics on extended timescales of Bet v 1a and two

SUBMITTER: Kamenik AS 

PROVIDER: S-EPMC7045072 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature