Protein Composition of the Bovine Herpesvirus 1.1 Virion

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Abstract

Bovine herpesvirus (BoHV) type 1 is an important agricultural pathogen that infects cattle and other ruminants worldwide. Acute infection of the oro-respiratory tract leads to immune suppression and allows commensal bacteria to infect an otherwise healthy lower respiratory tract. This condition is known as the Bovine Respiratory Disease (BRD). BoHV-1 latently infects the host for life and periodical stress events re-initiate BRD, translating into high morbidity and large economic losses. To gain a better understanding of the biology of BoHV-1 and the disease it causes, we elucidated the protein composition of extracellular virions using liquid chromatography-mass spectrometry analysis. We detected 33 viral proteins, including the expected proteins of the nucleocapsid and envelope as well as other regulatory proteins present in the viral tegument. In addition to viral proteins, we have also identified packaged proteins of host origin. This constitutes the first proteomic characterization of the BoHV virion.

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Bacterial pathogens of the bovine respiratory disease complex.

Dee Griffin, M.M Chengappa, Jennifer Kuszak … (2010)

Pneumonia caused by the bacterial pathogens discussed in this article is the most significant cause of morbidity and mortality of the BRDC. Most of these infectious bacteria are not capable of inducing significant disease without the presence of other predisposing environmental factors, physiologic stressors, or concurrent infections. Mannheimia haemolytica is the most common and serious of these bacterial agents and is therefore also the most highly characterized. There are other important bacterial pathogens of BRD, such as Pasteurella multocida, Histophulus somni, and Mycoplasma bovis. Mixed infections with these organisms do occur. These pathogens have unique and common virulence factors but the resulting pneumonic lesions may be similar. Although the amount and quality of research associated with BRD has increased, vaccination and therapeutic practices are not fully successful. A greater understanding of the virulence mechanisms of the infecting bacteria and pathogenesis of pneumonia, as well as the characteristics of the organisms that allow tissue persistence, may lead to improved management, therapeutics, and vaccines. Copyright 2010 Elsevier Inc. All rights reserved.

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Microtubule-mediated Transport of Incoming Herpes Simplex Virus 1 Capsids to the Nucleus

Beate Sodeik, Melanie Ebersold, Ari Helenius (1997)

Herpes simplex virus 1 fuses with the plasma membrane of a host cell, and the incoming capsids are efficiently and rapidly transported across the cytosol to the nuclear pore complexes, where the viral DNA genomes are released into the nucleoplasm. Using biochemical assays, immunofluorescence, and immunoelectron microscopy in the presence and absence of microtubule depolymerizing agents, it was shown that the cytosolic capsid transport in Vero cells was mediated by microtubules. Antibody labeling revealed the attachment of dynein, a minus end–directed, microtubule-dependent motor, to the viral capsids. We propose that the incoming capsids bind to microtubules and use dynein to propel them from the cell periphery to the nucleus.

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Comprehensive characterization of extracellular herpes simplex virus type 1 virions.

Sandra Loret, Ginette Guay, Roger Lippé (2008)

The herpes simplex virus type 1 (HSV-1) genome is contained in a capsid wrapped by a complex tegument layer and an external envelope. The poorly defined tegument plays a critical role throughout the viral life cycle, including delivery of capsids to the nucleus, viral gene expression, capsid egress, and acquisition of the viral envelope. Current data suggest tegumentation is a dynamic and sequential process that starts in the nucleus and continues in the cytoplasm. Over two dozen proteins are assumed to be or are known to ultimately be added to virions as tegument, but its precise composition is currently unknown. Moreover, a comprehensive analysis of all proteins found in HSV-1 virions is still lacking. To better understand the implication of the tegument and host proteins incorporated into the virions, highly purified mature extracellular viruses were analyzed by mass spectrometry. The method proved accurate (95%) and sensitive and hinted at 8 different viral capsid proteins, 13 viral glycoproteins, and 23 potential viral teguments. Interestingly, four novel virion components were identified (U(L)7, U(L)23, U(L)50, and U(L)55), and two teguments were confirmed (ICP0 and ICP4). In contrast, U(L)4, U(L)24, the U(L)31/U(L)34 complex, and the viral U(L)15/U(L)28/U(L)33 terminase were undetected, as was most of the viral replication machinery, with the notable exception of U(L)23. Surprisingly, the viral glycoproteins gJ, gK, gN, and U(L)43 were absent. Analyses of virions produced by two unrelated cell lines suggest their protein compositions are largely cell type independent. Finally, but not least, up to 49 distinct host proteins were identified in the virions.

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Contributors

Ellen (Liz) Sparger: Role: Academic Editor

Journal

Journal ID (nlm-ta): Vet Sci

Journal ID (iso-abbrev): Vet Sci

Journal ID (publisher-id): vetsci

Title: Veterinary Sciences

Publisher: MDPI

ISSN (Electronic): 2306-7381

Publication date (Electronic): 20 February 2017

Publication date Collection: March 2017

Volume: 4

Issue: 1

Electronic Location Identifier: 11

Affiliations

[1 ]Department of Biochemistry, Molecular Biology, Entomology & Plant Pathology, Mississippi State University, Mississippi State, MS 39762, USA; kaleyabarber@ 123456gmail.com (K.A.B.); hecdaugherty@ 123456gmail.com (H.C.D.); stephanie.e.ander@ 123456gmail.com (S.E.A.); vajefferson77@ 123456yahoo.com (V.A.J.)

[2 ]Department of Basic Sciences, College of Veterinary Science, Mississippi State University, Mississippi State, MS 39762, USA; Shack@ 123456cvm.msstate.edu (A.S.); BNanduri@ 123456cvm.msstate.edu (B.N.)

[3 ]Institute for Genomics, Biocomputing and Biotechnology, Mississippi State University, Mississippi State, MS 39762, USA; pechan@ 123456ra.msstate.edu

Author notes

[* ]Correspondence: florencia.meyer@ 123456msstate.edu ; Tel.: +1-662-325-7734

Article

Publisher ID: vetsci-04-00011

DOI: 10.3390/vetsci4010011

PMC ID: 5606624

SO-VID: 2b043c02-9023-49a8-8f7a-84ed09ac1081

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Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

Protein Composition of the Bovine Herpesvirus 1.1 Virion

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Journal of Circulating Biomarkers

Most cited references 77

Bacterial pathogens of the bovine respiratory disease complex.

Microtubule-mediated Transport of Incoming Herpes Simplex Virus 1 Capsids to the Nucleus

Comprehensive characterization of extracellular herpes simplex virus type 1 virions.

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