An integrative structural and biophysical workflow indicates engagement of VRC01 germline antibodies can occur with a gp120 426c core construct containing all wild-type N-linked glycosylation sites, including the Asn276 glycan.
Controlled neo-glycosylation of antigens can influence intracellular routing of antigens and the nature and strength of immune response, and should therefore be considered as a major determinant in the design of vaccines against cancer and infectious diseases.
R-spondins 2 and 3 can potentiate WNT signaling in the absence of LGRs through interactions with ZNRF3/RNF43 E3 ubiquitin ligases and heparan sulfate proteoglycans, defining two alternative modes of R-spondin-mediated signaling.
The recently discovered peptide editor TAPBPR binds to UDP-glucose:glycoprotein glucosyltransferase 1 to provide quality control in the antigen presentation pathway by facilitating the reglucosylation of the glycan on MHC class I molecules.
Post-phosphoryl modification of α-dystroglycan requires the glucuronyltransferase B4GAT1; this enzyme synthesizes the acceptor glycan that serves as a primer for the glycosyltransferase LARGE to synthesize the laminin-binding glycan.