Key result
Two amino acids in the membrane-distal face of the HSV-1 NEC are required for efficient NEC binding to nucleocapsids and their incorporation into vesicles during primary envelopment.
Why the study?
Data directly supporting the hypothesis that HSV-1 NEC binding to nucleocapsids promotes budding and incorporation into vesicles during nuclear egress had not been reported.
This study provides the first direct evidence linking HSV-1 NEC binding to nucleocapsids with increased nucleocapsid incorporation into vesicles during primary envelopment.
No immediate implications for HSV-1 therapy; hypothesis-generating for NEC-targeted antivirals in primary envelopment.
Binding of HSV-1 NEC to nucleocapsids has been thought to promote nucleocapsid budding at the inner nuclear membrane and subsequent incorporation of nucleocapsids into vesicles during nuclear egress of nucleocapsids. However, data to directly support this hypothesis have not been reported thus far. In this study, we have present data showing that two amino acids in the membrane-distal face of the HSV-1 NEC, which contains the putative capsid binding site based on the solved NEC structure, were in fact required for efficient NEC binding to nucleocapsids and for efficient incorporation of nucleocapsids into vesicles during primary envelopment. This is the first report showing direct linkage between NEC binding to nucleocapsids and an increase in nucleocapsid incorporation into vesicles during herpesvirus primary envelopment.
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Takeshima et al. (2019) studied Herpes Simplex Virus 1 (HSV-1). Mutation of two amino acids in the membrane-distal face of the HSV-1 NEC was evaluated on NEC binding to nucleocapsids and incorporation into vesicles during primary envelopment. Two amino acids in the membrane-distal face of the HSV-1 NEC are required for efficient NEC binding to nucleocapsids and their incorporation into vesicles during primary envelopment.
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