Daylight saving time ends in the U.S. and Canada on November 5, 2023, where most individuals will adjust their clocks back by one hour. There has been an ongoing debate regarding the benefits of this time change due to its disruption of humans’ circadian rhythms and the resulting short-term stress and fatigue it causes. Furthermore, this time change poses risks on the road as more people drive during dusk, which coincides with an active time of year for deer, resulting in a higher number of deer-vehicle accidents.
Deer are responsible for over 1 million motor vehicle accidents in the U.S. each year, leading to more than $1 billion in damages. The collision rates increase during daylight saving time due to the greater number of vehicles on the road during twilight hours, when visibility is reduced. This, combined with the heightened deer activity during mating season and their tendency to migrate, contributes to the rise in accidents.
Interestingly, the human immune system has the capacity to produce its own antiviral molecules in response to viral infections. This discovery challenges the notion that antiviral drugs are solely a product of modern scientific advancements. A protein called viperin, present in human cells, synthesizes natural chain-terminating antiviral molecules, which work similarly to the COVID-19 antiviral drug remdesivir.
Viruses rely on host cells to provide the necessary building blocks for their replication. Antiviral drugs exploit the differences in how cells and viruses replicate to disrupt the virus’s life cycle. One key distinction is seen in how genetic information is stored. While cells use DNA, many viruses use RNA. Antiviral drugs target the RNA replication process by mimicking chemical letters without the necessary connection points, effectively halting the copying process.
Viperin, as an antiviral producer, chemically removes the connection point from one of the viral RNA building blocks, transforming it into a chain-terminating antiviral. This approach has demonstrated great efficacy in treating viral infections, as the incomplete genome lacks the necessary instructions for the production of new viruses. Furthermore, this selective inhibition of viral replication reduces unwanted side effects.
Viperin’s function initially posed a challenge for researchers due to its resemblance to ancient proteins found in bacteria and molds. However, further investigation revealed its role in modifying RNA building blocks. Viperin-like proteins have been identified across various life forms, indicating its ancient origins and integration into the immune systems of modern animals. Thus, this newly discovered arm of the immune system serves as an ancient defense mechanism against viruses.
This article was written by Neil Marsh from the University of Michigan and is republished from The Conversation, a trusted news source that shares insights from academic experts. To receive reliable news from experts, sign up for our free newsletters. Neil Marsh’s laboratory’s work on viperin is supported by funding from the National Institute of General Medical Sciences.
