2014
DOI: 10.7554/elife.04389.017
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Author response: Sequential conformational rearrangements in flavivirus membrane fusion

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“…In the mature virus particle, these form an outer shell of 90 E protein and 90 M protein homo-dimers, arranged with icosahedral symmetry (Mukhopadhyay et al, 2005). Receptor-mediated endocytosis and exposure to low pH triggers the E proteins to undergo a large, irreversible conformational change, and rearrangement into 60 trimers (Chao et al, 2014). This is followed by fusion of the viral and host cell membranes, and subsequent release of the capsid and RNA genome into the cell (Mukhopadhyay et al, 2005).…”
Section: Introductionmentioning
confidence: 99%
“…In the mature virus particle, these form an outer shell of 90 E protein and 90 M protein homo-dimers, arranged with icosahedral symmetry (Mukhopadhyay et al, 2005). Receptor-mediated endocytosis and exposure to low pH triggers the E proteins to undergo a large, irreversible conformational change, and rearrangement into 60 trimers (Chao et al, 2014). This is followed by fusion of the viral and host cell membranes, and subsequent release of the capsid and RNA genome into the cell (Mukhopadhyay et al, 2005).…”
Section: Introductionmentioning
confidence: 99%