Glycosylation and Folding of HA Authored: Steel, J, 2007-04-30 20:49:24 Pubmed10679029 Pubmed10764645 Pubmed12535523 Pubmed1321156 Pubmed1331514 Pubmed2178922 Pubmed3359486 Pubmed7541532 Pubmed8302866 Pubmed8497042 Pubmed8534914 Pubmed9348279 Reactome Database ID Release 43169921 Reactome, http://www.reactome.org ReactomeREACT_6177 Reviewed: Squires, B, Rush, MG, 2007-04-30 20:48:45 The ectodomain of HA is translocated into the ER lumen, where it undergoes a series of folding events mediated by the formation of disulfide bonds and glycosylation reactions. The formation of a discrete intermediate species of highly folded monomeric protein preceeds trimerisation. The folding process is efficient and rapid, with greater than 90% of the protein trafficked to the golgi apparatus; and mature HA0 subunits appearing in a matter of a few minutes. Calnexin and calreticulin have been identified as cellular lectins which interact transiently with newly synthesized HA by attaching to partially trimmed N-linked oligosaccharides (Herbert et al., 1997), facilitating correct folding of the HA molecule.