Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism

Purification of a recombinant baculovirus of Autographa californica M nucleopolyhedrovirus by ion exchange membrane chromatography

“…This may support particle aggregation due to hydrogen bonding. Enveloped viruses are known to be sensitive to low H 3 O + activities (Gaudin et al, 1995). Also, pH changes resulting in virus particle aggregation have been correlated previously with decreased baculovirus infectivity (Jorio et al, 2006b).…”

Characterization of a Slow‐Migrating Component of the Rabies Virus Matrix Protein Strongly Associated with the Viral Glycoprotein

“…Concerning similar conformational changes of the rabies virus proteins, we also reported previously the structural changes of viral N and P proteins that were recognized by our anti-N and P mAbs (#5-2-26, #1-7-11, and #402-13; 22, 39). Viral G protein is also known to undergo conformational changes when exposed to acidic pH to perform the acid-induced membrane fusion in the endosome function (8,9,(11)(12)(13)(14).…”

Two Different Conformations of Rabies Virus Glycoprotein Taken under Neutral pH Conditions

“…It takes at least three different states (11): the native (N) state detected at the virion surface, which is responsible for the receptor binding, the activated hydrophobic state (A), which is competent for interacting with the target membrane as the first step in the fusion process, and the fusion inactive conformation (I). It has also been proposed that the G protein is transported through the Golgi apparatus in an I-like conformation to avoid undesirable fusion during its transport through the acidic Golgi vesicles (10). At present, however, there is insufficient knowledge to correlate structural relationships between the antigenic sites and different states or conformations.…”