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- W2996972654 abstract "The neurotropic herpes simplex virus type 2 (HSV 2) is a highly prevalent human virus. After primary infection, the virus establishes latency in neurons of the peripheral nervous system. HSV-1 and HSV-2 glycoprotein G (gG1 and gG2, respectively) are type I transmembrane proteins. They bind chemokines with high affinity and enhance chemokine-dependent leukocyte migration. Similarly, gG1 and gG2 bind NGF with high affinity, but only gG2 enhances NGF-dependent neurite outgrowth. Finally, both gG1 and gG2 bind to the cell plasma membrane through glycosaminoglycans (GAGs). On the structural level gG2 is proteolytically cleaved, releasing an N terminal domain to the supernatant of infected cells. It is not known whether cleavage and secretion of gG2 have any functional relevance on gG2 activities compared to gG1. The first objective was to identify the gG2 cleavage site. After mutagenesis studies and we conclude that the amino acids from 314 and 343 are responsible for gG2 cleavage. Furthermore, deletion or replacement of the cleavage sequence with a linker (GSm) inhibited nearly completely the cleavage. The second objective determined whether gG2 cleavage is relevant for gG2 activities. Our results indicate that deletion of H2S sequence did not dramatically affect gG2 functions. However, its substitution with the linker abrogated gG2 activities. We conclude that gG2 cleavage in the context of the SgG2 construct seems to be not necessary for gG2 activity since leukocytes migration was increased compared to chemokine alone. Further, inhibition of the cleavage site in the context of the full-length protein led to longer neurites compared to the cleaved protein. This may be due to the secretion of the full-length gG2.The final objective was to identify binding sites for GAG, chemokine and NGF. To do so, we successfully generated truncated gG2 constructs." @default.
- W2996972654 created "2020-01-10" @default.
- W2996972654 creator A5088553880 @default.
- W2996972654 date "2019-01-01" @default.
- W2996972654 modified "2023-09-27" @default.
- W2996972654 title "Identification of the cleavage site of herpes simplex virus type 2 glycoprotein G (gG) and its involvement in gG activities" @default.
- W2996972654 hasPublicationYear "2019" @default.
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