The effects of phosphorylation during bovine herpesvirus-1 (BHV-1) infection
Phosphorylation is a major means of post-translational modification and has previously shown to be tightly regulated throughout the course of BHV-1 infection. Our goals included to study the effects of phosphorylation manipulation on viral replication and infection, to purify the BHV-1 virion, and to analyze the virion for its phosphoproteome. Wild-type virions and virions produced in an over-phosphorylated environment will be compared to identify any differences in constituents due to phosphorylation manipulation.
Currently, we have concluded there is very little difference in viral replication and infection in wild-type and over-phosphorylated BHV-1; although, a slight downward trend was seen in viral production when phosphatase inhibitors were added before infection. This lack of a significant difference in viral titer reinforces our belief that BHV-1 is regulating exactly what is incorporated into progeny virions. On the same note, the trend in decreased viral titer seen with phosphatase inhibitors added before infection, suggests a possible difference in the constituents of progeny virions produced normally and under over-phosphorylated conditions. We are purifying virus in preparation for enrichment of phosphoproteins and subsequent analysis using mass spectrometry. After identification of viral constituents via mass spectrometry, proteomics databases such as Proteome Discoverer will be used to deduce phosphorylation levels of predicted and identified phosphoproteins to determine any variance between the two types of virions.
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