Recombinant Meleagrid herpesvirus 1 Envelope glycoprotein H (gH)
Description
Introduction to Recombinant Meleagrid Herpesvirus 1 Envelope Glycoprotein H (gH)
Recombinant Meleagrid herpesvirus 1 (MeHV-1) envelope glycoprotein H (gH) is a protein derived from the Meleagrid herpesvirus 1, which is commonly used in the poultry industry for vaccine development. This glycoprotein plays a crucial role in the viral envelope and is essential for viral entry and membrane fusion processes. The recombinant form of gH is often expressed in bacterial systems like Escherichia coli and is used for various research and vaccine development purposes.
Structure and Function of Glycoprotein H (gH)
Glycoprotein H (gH) is a key component of the herpesvirus envelope, functioning in conjunction with glycoprotein L (gL) to facilitate viral entry into host cells. The gH/gL complex acts as a critical part of the viral fusion machinery, working alongside other glycoproteins such as gB and gD to mediate membrane fusion and viral penetration .
| Glycoprotein | Function | Complex Formation |
|---|---|---|
| gH | Essential for viral entry and membrane fusion | Forms complex with gL |
| gL | Acts as a chaperone for gH, stabilizing its structure | Forms complex with gH |
| gB | Initiates membrane fusion | Interacts with gH/gL and gD |
| gD | Binds to host cell receptors, triggering fusion | Interacts with gB and gH/gL |
Recombinant Expression and Applications
Recombinant MeHV-1 gH is typically expressed in Escherichia coli with a His tag for easy purification. This recombinant protein is used in various applications, including vaccine development and research studies focused on viral entry mechanisms .
Recombinant Expression Details:
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Expression System: Escherichia coli
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Protein Length: 18-808 amino acids
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Tag: N-terminal His tag
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Applications: Vaccine development, research on viral entry mechanisms
Research Findings and Implications
Research on herpesvirus glycoproteins, including gH, has highlighted their importance in viral pathogenesis and the potential for targeting these proteins in therapeutic strategies. For instance, understanding the interactions between gH/gL and other viral glycoproteins can inform the development of vaccines or antiviral drugs .
Key Research Findings:
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Viral Entry: gH/gL complex is crucial for viral entry and membrane fusion.
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Complex Formation: gH forms a stable complex with gL, which is essential for its function.
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Therapeutic Potential: Targeting gH/gL interactions could be a strategy for developing antiviral therapies.
Product Specs
Note: While we prioritize shipping the format currently in stock, please specify your format preference during order placement for customized preparation.
Note: Standard shipping includes blue ice packs. Dry ice shipping requires prior arrangement and incurs additional charges.
The tag type is determined during production. If you require a specific tag, please inform us, and we will prioritize its development.
Target Background
The heterodimeric glycoprotein H-glycoprotein L complex is essential for the fusion of viral and host cell plasma membranes, facilitating viral entry. Following initial receptor binding, membrane fusion is mediated by the fusion machinery comprising gB and the gH/gL heterodimer. This complex may also play a role in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis.
