Mouse/Rat HSV-1 IgG ELISA Kit (DEIA3555)

Regulatory status: For research use only, not for use in diagnostic procedures.

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serum, plasma
Species Reactivity
Mouse, Rat
Intended Use
HSV1 IgG (Mouse/Rat) ELISA Kit is an indirect enzyme immunoassay for the measurement of mouse/rat HSV-1 specific IgG class antibodies in serum and plasma.
Contents of Kit
1. Microwell coated with HSV-1 antigen
2. Sample Diluent
3. Calibrator
4. positive Control
5. Negative Control
6. Enzyme conjugate
7. TMB Substrate
8. Stop Solution
9. Wash Concentrate 20X
Store the kit at 2-8°C. For more detailed information, please download the following document on our website.


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Hsv-1 Endocytic Entry into a Human Oligodendrocytic Cell Line Is Mediated by Clathrin and Dynamin but Not Caveolin


Authors: Praena, Beatriz; Bello-Morales, Raquel; Antonio Lopez-Guerrero, Jose

Endocytosis is a pathway used by viruses to enter cells that can be classified based on the proteins involved, such as dynamin, clathrin or caveolin. Although the entry of herpes simplex type 1 (HSV-1) by endocytosis has been documented in different cell types, its dependence on clathrin has not been described whereas its dependence on dynamin has been shown according to the cell line used. The present work shows how clathrin-mediated endocytosis (CME) is one way that HSV-1 infects the human oligodendroglial (HOG) cell line. Partial dynamin inhibition using dynasore revealed a relationship between decrease of infection and dynamin inhibition, measured by viral titration and immunoblot. Co-localization between dynamin and HSV-1 was verified by immunofluorescence at the moment of viral entry into the cell. Inhibition by chlorpromazine revealed that viral progeny also decreased when clathrin was partially inhibited in our cell line. RT-qPCR of immediately early viral genes, specific entry assays and electron microscopy all confirmed clathrin's participation in HSV-1 entry into HOG cells. In contrast, caveolin entry assays showed no effect on the entry of this virus. Therefore, our results suggest the participation of dynamin and clathrin during endocytosis of HSV-1 in HOG cells.

The HSV-1 ubiquitin ligase ICP0: Modifying the cellular proteome to promote infection


Authors: Rodriguez, Milagros Collados; Dybas, Joseph M.; Hughes, Joseph; Weitzman, Matthew D.; Boutell, Chris

Herpes simplex virus 1 (HSV-1) hijacks ubiquitination machinery to modify the cellular proteome to create an environment permissive for virus replication. HSV-1 encodes its own RING-finger E3 ubiquitin (Ub) ligase, Infected Cell Protein 0 (ICP0), that directly interfaces with component proteins of the Ub pathway to inactivate host immune defences and cellular processes that restrict the progression of HSV-1 infection. Consequently, ICP0 plays a critical role in the infectious cycle of HSV-1 that is required to promote the efficient onset of lytic infection and productive reactivation of viral genomes from latency. This review will describe the current knowledge regarding the biochemical properties and known substrates of ICP0 during HSV-1 infection. We will highlight the gaps in the characterization of ICP0 function and propose future areas of research required to understand fully the biological properties of this important HSV-1 regulatory protein.

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