Investigating the biology of alpha herpesviruses with MS‐based proteomics

Abstract

Viruses are intracellular parasites that can only replicate and spread in cells of susceptible hosts. Alpha herpesviruses (α-HVs) contain double stranded DNA genomes of at least 120 kb, encoding for 70 or more genes. The viral genome is contained in an icosahedral capsid that is surrounded by a proteinaceous tegument layer and a lipid envelope. Infection starts in epithelial cells and spreads to the peripheral nervous system (PNS). In the natural host, α-HVs establish a chronic latent infection that can be reactivated, rarely spread to the central nervous system (CNS). In the non-natural host, viral infection will in most cases spread to the CNS with often fatal outcome. The host response plays a crucial role in the outcome of viral infection. α-HVs do not encode all the genes required for viral replication and spread. They need a variety of host gene products including RNA polymerase, ribosomes, dynein, and kinesin. As a result, the infected cell is dramatically different from the uninfected cell revealing a complex and dynamic interplay of viral and host components required to complete the virus life cycle. In this review, we describe the pivotal contribution of mass spectrometry-based proteomics (MSBP) studies over the past 15 years to understanding the complicated life cycle and pathogenesis of four α-HV species from the alphaherpesvirinae subfamily: Herpes simplex virus-1 (HSV-1), varicella zoster virus (VZV), pseudorabies virus (PRV) and bovine herpes virus (BHV-1). We describe the viral proteome dynamics during host infection and the host proteomic response to counteract such pathogens.

Glycomics and Proteomics Approaches to Investigate Early Adenovirus–Host Cell Interactions

“…Previously, AE-MS has successfully identified host factor interactions with viral non-structural proteins of virus families ranging from flaviviruses to herpesviruses (reviewed in Refs. [133,[147][148][149]). The application to virus receptor discovery is now in reach (Fig.…”

iTRAQ-based Proteomic Analysis of Porcine Kidney Epithelial PK15 cells Infected with Pseudorabies virus

“…Among these were the heat shock proteins hsp 90-beta (hsp90ab1), 90 kDa beta member 1(hsp90b1), 70 kDa protein 5(hspa5) and 105 kDa (hsph1). Similarly, hsp27 was also significant altered at 4 h of PRV infction in Madin-Darby bovine kidney cells using SILAC mass spectrometry methods, since only a small number of host cell proteins changed during early stages of PRV infection, other stress-related proteins did not show significant variations 7,8 . Heat-shock proteins can facilitate protein folding, heat-shock response activation might be a virus-specific function ensuring proper protein synthesis and; therefore, ER stress proteins may also be important for virus replication 37,39,40 .…”

“…The pathogenesis of PRV infection and the interactions between PRV and porcine cells are not fully understood at present [7][8][9] . Proteomic approaches provide effective tools for facilitating a comprehensive characterization of virus-host interactions, for example, two-dimensional gel electrophoresis (2DE) and matrix-assisted laser desorption ionization-time-of-flight mass spectrometry (MALDI-TOF/MS) approaches have been used to provide the proteomic expression profiles of host cells in response to viral infections, including classical swine fever virus 10 , severe acute respiratory syndrome 11 , H1N1 influenza virus 12 and spleen and kidney necrosis virus 13 .…”

Omics approaches to investigate host–pathogen interactions in mass mortality outbreaks of Crassostrea gigas

“…; Engel et al . ). However, no such studies have been reported for OsHV‐1, which is a clear gap that needs to be addressed in future investigations.…”