HSV type 1 Glycosylated [His] (DAG589)

HSV type 1 Glycosylated (aa 21 - 339) [His], recombinant protein from P. pastoris

Product Overview
Glycosylated recombinant ecto-domain of HSV-1 gD (a.a. 21-339 from KOS strain) representing the external domain of the gD molecule without membrane spanning and cytosolic sequences. It encodes a protein of approximately 30 kDa that contains 3 sites for gl
Nature
Recombinant
Tag/Conjugate
His
Molecular Weight
30 kDa (319aa)
Procedure
None
Purity
Purity verified by SDS-PAGE. Purity compares with reference lot.
Format
Purified, Liquid
Concentration
Lot specific (BCA)
Buffer
0.02M Sodium phosphate, 0.00 - 0.1M Sodium chloride, pH 6.7 to 7.7
Preservative
None
Storage
2-8°C short term, -20°C long term
Introduction
Herpes simplex virus 1 and 2 (HSV-1 and HSV-2), also known as Human herpes virus 1 and 2 (HHV-1 and -2), are two members of the herpes virus family, Herpesviridae, that infect humans. Both HSV-1 (which produces most cold sores) and HSV-2 (which produces most genital herpes) are ubiquitous and contagious. They can be spread when an infected person is producing and shedding the virus.
Antigen Description
Members of this family have a characteristic virion structure. The double stranded DNA genome is contained within an icosahedral capsid embedded in a proteinaceous layer (tegument) and surrounded by a lipid envelope, derived from the nuclear membrane of the last host, which is decorated with virus-specific glycoproteins spikes. These viruses are capable of entering a latent phase where the host shows no visible sign of infection and levels of infectious agent become very low. During the latent phase the viral DNA is integrated into the genome of the host cell. Glycoprotein D (gD) has been implicated in binding to cellular receptors that facilitate virus penetration into cells. Herpes simplex virus type 1 (HSV-1) glycoprotein D (gD) is an essential component of the entry apparatus that is responsible for viral penetration and subsequent cell-cell spread.
Keywords
Herpesviridae; Alphaherpesvirinae; Simplexvirus; Herpes simplex virus 1; HSV-1; Herpes simplex virus 2; HSV-2; Herpes simplex virus; HSV 1&2; Herpes Simplex Virus Type 1 & 2; HSV1 + HSV2 gD; Envelope glycoprotein D; GD; Glycoprotein D; US6

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References


Immuno-metabolic changes in herpes virus infection

CYTOKINE

Authors: Chattopadhyay, Debprasad; Mukhopadhyay, Aparna; Ojha, Durbadal; Sadhukhan, Provash; Dutta, Shanta

Recent evidences indicate that change in cellular metabolic pathways can alter immune response and function of the host; emphasizing the role of metabolome in health and diseases. Human Herpes simplex virus type-1 (HSV1) and type-2 (HSV-2) causes diseases from asymptomatic to highly prevalent oral and genital herpes, recurrent blisters or neurological complications. Immune responses against HSV are complex with delicate interplay between innate signaling pathways and adaptive immune responses. The innate response involves the induction of protective IFN-1; while Natural Killer (NK) cells and plasmacytoid Dendritic Cells (pDC) confer in vivo adaptive anti-HSV response along with humoral and cellular components in controlling infection and latency. Metabolic changes lead to up-/down-regulation of several cytokines and chemokines like IFN-gamma, IL-2, IL-4, IL-10 and MIP1 beta in HSV infection and recurrences. Recently, the viral protein ICP0 has been identified as an attenuator of TLR signaling, that inhibit innate responses to HSV. This review will summarize the role of metabolome in innate and adaptive effectors in infection, pathogenesis and immune control of HSV, highlighting the delicate interplay between the metabolic changes and immunity.

Exocytosis of Progeny Infectious Varicella-Zoster Virus Particles via a Mannose-6-Phosphate Receptor Pathway without Xenophagy following Secondary Envelopment

JOURNAL OF VIROLOGY

Authors: Girsch, James H.; Jackson, Wallen; Carpenter, John E.; Moninger, Thomas O.; Jarosinski, Keith W.; Grose, Charles

The literature on the egress of different herpesviruses after secondary envelopment is contradictory. In this report, we investigated varicella-zoster virus (VZV) egress in a cell line from a child with Pompe disease, a glycogen storage disease caused by a defect in the enzyme required for glycogen digestion. In Pompe cells, both the late autophagy pathway and the mannose-6-phosphate receptor (M6PR) pathway are interrupted. We have postulated that intact autophagic flux is required for higher recoveries of VZV infectivity. To test that hypothesis, we infected Pompe cells and then assessed the VZV infectious cycle. We discovered that the infectious cycle in Pompe cells was remarkably different from that of either fibroblasts or melanoma cells. No large late endosomes filled with VZV particles were observed in Pompe cells; only individual viral particles in small vacuoles were seen. The distribution of the M6PR pathway (trans-Golgi network to late endosomes) was constrained in infected Pompe cells. When cells were analyzed with two different anti-M6PR antibodies, extensive colocalization of the major VZV glycoprotein gE (known to contain M6P residues) and the M6P receptor (M6PR) was documented in the viral highways at the surfaces of non-Pompe cells after maximum-intensity projection of confocal z-stacks, but neither gE nor the M6PR was seen in abundance at the surfaces of infected Pompe cells. Taken together, our results suggested that (i) Pompe cells lack a VZV trafficking pathway within M6PR-positive large endosomes and (ii) most infectious VZV particles in conventional cell substrates are transported via large M6PR-positive vacuoles without degradative xenophagy to the plasma membrane. IMPORTANCE The long-term goal of this research has been to determine why VZV, when grown in cultured cells, invariably is more cell associated and has a lower titer than other alphaherpesviruses, such as herpes simplex virus 1 (HSV1) or pseudorabies virus (PRV). Data from both HSV1 and PRV laboratories have identified a Rab6 secretory pathway for the transport of single enveloped viral particles from the trans-Golgi network within small vacuoles to the plasma membrane. In contrast, after secondary envelopment in fibroblasts or melanoma cells, multiple infectious VZV particles accumulated within large M6PR-positive late endosomes that were not degraded en route to the plasma membrane. We propose that this M6PR pathway is most utilized in VZV infection and least utilized in HSV1 infection, with PRV's usage being closer to HSV1's usage. Supportive data from other VZV, PRV, and HSV1 laboratories about evidence for two egress pathways are included.

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