The structures of secretory and dimeric IgA reveal pseudosymmetric assemblies of two antibody monomers, in which possible positions of antigen-binding fragments and accessibility to receptor-binding sites are limited.
The ectodomain of the human polymeric Ig receptor maintains a closed triangular shape that binds and excludes bacteria in mucosa, or opens to bind and transport polymeric Ig ligands across epithelial cells.
An attenuated Herpes simplex type 2 virus deleted in glycoprotein D can be used as an effective vaccine to provide robust transferable humoral immunity and complete protection in murine intravaginal and skin infection models.
The extent of (proteotoxic) endoplasmic reticulum stress, and the ensuing unfolded protein response activation, are commensurate with the extent of the chaperone BiP being sequestered by its client proteins.
The substrate for evolutionary divergence does not lie in changes in neuronal cell number or targeting, but rather in sensory perception and synaptic partner choice within invariant, prepatterned neuronal processes.
Endoplasmic reticulum proteostasis factors enhance the mutational tolerance of influenza hemagglutinin, a model secretory pathway protein and therapeutic target, particularly improving the fitness of temperature-sensitive variants.