PMC:7464876 / 51143-52208 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PMC/sourceid/7464876","sourcedb":"PMC","sourceid":"7464876","source_url":"https://www.ncbi.nlm.nih.gov/pmc/7464876","text":"Such alterations in ERGIC-53 trafficking could not be detected in HBV-replicating cells unless the ER export was blocked. Moreover, we were unable to verify a colocalization between ERGIC-53 and the viral envelope under natural settings, which was unanticipated given its pro-viral role in HBV propagation. ERGIC-53 is known to capture its cargoes in a pH- and Ca2+-dependent manner at the ER and releases them in the ERGIC, where the lower pH and Ca2+ concentrations diminish its affinity for glycoproteins [50,53]. Hence, within the ERGIC, the HBV envelope may rapidly dissociate from ERGIC-53, thereby rendering their colocalization below the limit of detection. Similarly, we failed to detect HBV envelope structures within Golgi stacks, although the N-glycan pattern of the extracellular virions implicate a transit through this compartment. One likely interpretation may be that HBV assembly and budding are inextricably linked and rate-limiting processes. Once disseminated from the host membrane, HBV viral particles may be rapidly exported out of the cell.","tracks":[{"project":"2_test","denotations":[{"id":"32806600-19609866-20296270","span":{"begin":509,"end":511},"obj":"19609866"},{"id":"32806600-14718532-20296271","span":{"begin":512,"end":514},"obj":"14718532"}],"attributes":[{"subj":"32806600-19609866-20296270","pred":"source","obj":"2_test"},{"subj":"32806600-14718532-20296271","pred":"source","obj":"2_test"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"2_test","color":"#c293ec","default":true}]}]}}