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Herpes simplex virus type 1 (HSV-1) capsids assemble in the nucleus but acquire their teguments from various cellular compartments. Unfortunately, little is known about their exact arrangement and when they coat the newly produced capsids. The complexity of the virions is further highlighted by our recent proteomics analysis that detected the presence of several novel or controversial components in extracellular HSV-1 virions. The present study probes the localization and linkage to the virus particles of some of these incorporated proteins. We confirm the recently reported tight association of infected cell polypeptide (ICP)0 with the capsid and show that this property extends to ICP4. We also confirm our proteomics data and show biochemically that UL7 and UL23 are indeed mature virion tegument components that, unlike ICP0 and ICP4, are salt-extractable. Interestingly, treatment with N-ethylmaleimide, which covalently modifies reduced cysteines, strongly prevented the release of UL7 and UL23 by salts, but did not perturb the interactions of ICP0 and ICP4 with the virus particles. This hitheir at distinct biochemical properties of the virion constituents and the selective implication of reduced cysteines in their organization and dynamics. Finally, the data revealed, by two independent means, the presence of ICP0 and ICP4 on intranuclear capsids, consistent with the possibility that they may at least partially be recruited to the virus particles early on. These findings add significantly to our understanding of HSV-1 virion assembly and to the debate about the incorporation of ICP0 and ICP4 in virus particles.

Biochemical analysis of infected cell polypeptide (ICP)0, ICP4, UL7 and UL23 incorporated into extracellular herpes simplex virus type 1 virions