Identification of immuno-reactive capsid proteins of malignant catarrhal fever viruses

Bartley, Kathryn; Deane, David; Percival, Ann; Dry, Inga; Grant, Dawn M.; Inglis, Neil F.; McLean, Kevin; Manson, Erin; Imrie, Lisa; Haig, David M.; Lankester, Felix; Russell, George C.

doi:10.1016/j.vetmic.2014.07.004

Cited by 5 publications

(5 citation statements)

References 36 publications

(50 reference statements)

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“…It is unclear why these cattle failed to produce neutralizing antibodies but host genetic or immunological factors could focus virus-specific immune responses on antigens or epitopes that were non-neutralizing. Indeed, two AlHV-1 capsid proteins, which are unlikely to be neutralizing antigens, are strongly recognized by AlHV-1 vaccinated or infected cattle sera [2] . Analysis of NS VNA data from the vaccinated cattle showed that the correlation between the presence of VNA antibodies and protection from infection approached, but did not achieve, statistical significance ( p < 0.07).…”

Section: Discussionmentioning

confidence: 99%

A field vaccine trial in Tanzania demonstrates partial protection against malignant catarrhal fever in cattle

Lankester

Russell

Lugelo

et al. 2016

Vaccine

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Section: Discussionmentioning

confidence: 99%

A field vaccine trial in Tanzania demonstrates partial protection against malignant catarrhal fever in cattle

Lankester

Russell

Lugelo

et al. 2016

Vaccine

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“…It is notable that a recombinant OvHV-2 gB fusion polypeptide expressed in transfected cells was also subject to proteolysis, revealing bands of about 110 and 50 kDa 24 when blotted with an epitope tag antibody. Recombinant gB (in addition to other MCF virus antigenic proteins 14,24 ) has been suggested as a good candidate for a recombinant vaccine for MCF and the observation that AlHV-1 gB is recognized by OvHV-2-specific antiserum suggests that crossprotection might occur.…”

Section: Discussionmentioning

confidence: 99%

“…The identification of recombinant AlHV-1 gB fractionated by gel electrophoresis was done by liquid chromatography-electrospray ionization-tandem mass spectrometry (LC-ESI-MS/MS) as described previously 13,14 . Briefly, protein bands excised from PAGE gels were subjected to standard in-gel destaining, reduction, alkylation and trypsinolysis, followed by liquid chromatography interfaced with a 3-D high capacity ion trap mass spectrometer (Esquire HCTplusTM, Bruker Daltonics).…”

Section: Proteomic Analysismentioning

confidence: 99%

“…As part of our studies to understand the basis of MCF pathology in cattle we have been studying the antigenic capsid proteins of AlHV-1 14 . However, interactions between the virus and host are also likely to be influenced by the membrane glycoproteins of the virus, which are responsible for interactions with cell surface receptors on target cell types and fusion of virus and cell membranes.…”

Section: Introductionmentioning

confidence: 99%

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Alcelaphine herpesvirus 1 glycoprotein B: recombinant expression and antibody recognition

et al. 2015

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The gammaherpesvirus alcelaphine herpesvirus 1 (AlHV-1) causes fatal malignant catarrhal fever (MCF) in susceptible species including cattle, but infects its reservoir host, wildebeest, without causing disease. Pathology in cattle may be influenced by virus-host cell interactions mediated by the virus glycoproteins. Cloning and expression of a haemagglutinin-tagged version of the AlHV-1 glycoprotein B (gB) was used to demonstrate that the AlHV-1-specific monoclonal antibody 12B5 recognised gB and that gB was the main component of the gp115 complex of AlHV-1, a glycoprotein complex of five components identified on the surface of AlHV-1 by immunoprecipitation and radiolabelling. Analysis of AlHV-1 virus particles showed that the native form of gB was detected by mAb 12B5 as a band of about 70 kDa, whilst recombinant gB expressed by transfected HEK293T cells appeared to be subject to additional cleavage and incomplete post-translational processing. Antibody 12B5 recognised an epitope on the N-terminal furin-cleaved fragment of gB on AlHV-1 virus particles. It could be used to detect recombinant and virus-expressed gB on western blots and on the surface of infected cells by flow cytometry, whilst recombinant gB was detected on the surface of transfected cells by immunofluorescence. Recombinant gB has potential as an antigen for ELISA detection of MCF virus infection and as a candidate vaccine antigen.

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“…Based on recent evidence, it can be assumed that the main portal of entry of OvHV-2 into cattle is by the respiratory route and relies on at least a few rounds of lytic replication of OvHV-2 in deep lung tissue (23,40). Later on, OvHV-2 --as well as AlHV- (Fig.…”

Section: Downloaded Frommentioning

confidence: 99%

Ovine Herpesvirus 2 Encodes a Previously Unrecognized Protein, pOv8.25, That Targets Mitochondria and Triggers Apoptotic Cell Death

Shrestha

Tobler

Uster

et al. 2020

J Virol

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Malignant catarrhal fever (MCF) is a rare but frequently lethal disease of certain cloven-hoofed animals. At least 10 different viruses, all members of the Macavirus genus in the subfamily Gammaherpesvirinae, are known as causative agents of MCF. Among these, ovine herpesvirus 2 (OvHV-2) is the most frequent and economically most important MCF agent. Phenotypically, MCF is characterized by severe lymphocytic arteritis-periarteritis, which leads to the accumulation of activated lymphocytes accompanied by apoptosis and necrosis in a broad range of tissues. However, a viral factor that might be responsible for tissue damage has not yet been identified. We have studied a seemingly intergenic locus on the OvHV-2 genome, which was previously shown to be transcriptionally highly active in MCF-affected tissue. We identified by 5′ and 3′ rapid amplification of cDNA ends (RACE) a conserved, double-spliced transcript that encoded a 9.9-kDa hydrophobic protein. The newly detected gene, Ov8.25, and its splicing pattern were conserved among OvHV-2 strains of different origins. Upon transient expression of synthetic variants of this gene in various cell types, including bovine lymphocytes, the protein (pOv8.25) was shown to target mitochondria, followed by caspase-dependent apoptosis and necrosis. Notably, a deletion mutant of the same protein lost these abilities. Finally, we detected pOv8.25 in brain-infiltrating lymphocytes of cattle with MCF. Thus, the cell death-causing properties of pOv8.25 in affected cells may be involved in the emergence of typical MCF-associated apoptosis and necrosis. Thus, we have identified a novel OvHV-2 protein, which might contribute to the phenotype of MCF-related lesions. IMPORTANCE Ovine herpesvirus 2 (OvHV-2) circulates among sheep without causing disease. However, upon transmission to cattle, the same virus instigates a frequently lethal disease, malignant catarrhal fever (MCF). While the cause of death and pathogenesis of tissue lesions are still poorly understood, MCF is characterized by the accumulation of lymphocytes in various tissues, associated with vasculitis and cell death. As infectious virus is hardly present in these lesions, the cause of cell death cannot be explained simply by viral replication. The significance of our research is in identifying and characterizing a previously overlooked gene of OvHV-2 (Ov8.25), which is highly expressed in animals with MCF. Its encoded protein targets mitochondria, causing apoptosis and necrosis, thus contributing to an understanding of the source and nature of cell death. As the corresponding genetic locus is also active in the context of MCF due to a different macavirus, we may have detected a common denominator of the disease phenotype.

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Identification of immuno-reactive capsid proteins of malignant catarrhal fever viruses

Cited by 5 publications

References 36 publications

A field vaccine trial in Tanzania demonstrates partial protection against malignant catarrhal fever in cattle

A field vaccine trial in Tanzania demonstrates partial protection against malignant catarrhal fever in cattle

Alcelaphine herpesvirus 1 glycoprotein B: recombinant expression and antibody recognition

Ovine Herpesvirus 2 Encodes a Previously Unrecognized Protein, pOv8.25, That Targets Mitochondria and Triggers Apoptotic Cell Death

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