Titlebook: Herpes Simplex Virus; Methods and Protocol Russell J. Diefenbach,Cornel Fraefel Book 2014 Springer Science+Business Media New York 2014 Can

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,Affinity Purification Combined with Mass Spectrometry to Identify Herpes Simplex Virus Protein–Prottics tools have greatly increased the quantity and quality of protein–protein interaction datasets. In this chapter, detailed and reliable methods that can easily be implemented are presented for the identification of protein–protein interactions using cryogenic cell lysis, affinity purification, trypsin digestion, and mass spectrometry.

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Expression, Purification, and Crystallization of HSV-1 Glycoproteins for Structure Determination,can be used for generating milligram amounts of wild-type (WT) or mutant gB and gH/gL ectodomains or can be adapted to produce purified ectodomains of other HSV glycoproteins for biochemical and structural studies.

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Herpes Simplex Virus Growth, Preparation, and Assay, stocks. Many different protocols are available from different research groups working with herpes simplex virus type 1 or 2 (HSV-1 or HSV-2). This chapter describes the procedures used in our laboratory.

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Herpes Simplex Virus Mutant Generation and Dual-Detection Methods for Gaining Insight into Latent/Lhat limits undesired mutation and retains full replication competency in vivo and (2) an efficient system to detect and quantify viral promoter activity in rare cells in vivo. Our strategy and protocols for generating, characterizing, and employing HSV viral promoter/reporter mutants in vivo are provided in this two-part chapter.

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Russell J. Diefenbach,Cornel FraefelIncludes cutting-edge methods and protocols for the study of the complex interactions between herpes viruses and the host.Provides step-by-step detail essential for reproducible results.Contains key n

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