Abstract
HSV glycoproteins play important roles in the viral life cycle, particularly viral cell entry. Here we describe the protocol for expression, purification, and crystallization of full-length HSV-1 glycoprotein B. The protocol provides a framework for incorporating transmembrane domain-stabilizing amphipols into the crystallization setup and can be adapted to isolate other complete HSV glycoproteins.
Keywords:
Crystallography; Ectodomain; Glycoproteins; Herpes simplex viruses; Membrane protein; Protein purification; Viral entry.
MeSH terms
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Animals
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Crystallography, X-Ray
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Gene Expression*
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Herpesvirus 1, Human* / chemistry
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Herpesvirus 1, Human* / genetics
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Herpesvirus 1, Human* / metabolism
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Protein Domains
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Sf9 Cells
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Spodoptera
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Viral Envelope Proteins* / biosynthesis
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Viral Envelope Proteins* / chemistry
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Viral Envelope Proteins* / genetics
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Viral Envelope Proteins* / isolation & purification
Substances
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Recombinant Proteins
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Viral Envelope Proteins
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glycoprotein B, Simplexvirus