Guwahati: Researchers from the Indian Institute of Technology Guwahati (IITG) have investigated the biochemistry of the African Swine Fever Virus (ASFV) protein focusing on understanding the biochemical processes of infection to devise effective control strategies.
Prof Sachin Kumar from IITG’s Department of Biosciences and Bioengineering, and his research scholars have studied the proteins found in the outer membrane (capsule) of ASFV, with a particular focus on the p30 protein.
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This protein plays a crucial role in the attachment of the virus to host cells by binding to specific receptors on the cell surface and facilitating the merging of viral and cell membranes.
Membrane proteins also help viruses evade detection by the host cell’s immune system. Understanding the biochemistry behind these processes enhances our knowledge of how viruses infect cells and can guide the development of treatments and vaccines that target these points of entry.
Speaking about the research, Prof Kumar said, “Our ongoing research into ASFV aims to uncover the functional roles of proteins like p30, which are integral to the virus’s ability to infect and evade the host’s immune response.”
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The research team has also completed technology transfer to roll out the first recombinant vaccine for Swine Fever Virus in the recent past. They had previously identified specific regions on the p30 protein called epitopic domains that can activate the immune system in the host.
These domains are important as they help the immune system recognise and respond to the virus potentially aiding in developing ways to fight the infection. The researchers recently studied this protein in greater detail to understand its other functionalities, particularly its RNase-like activity.
An RNase (ribonuclease) is an enzyme that catalyses the degradation of Ribonucleic acid (RNA) into smaller components. In viruses, RNases are rare but significant as they help the virus by breaking down the host’s RNA to evade immune defenses.
Emphasising the methodology, Prof Kumar said, “In our study, RNA extracted from mammalian cells was exposed to the p30 protein to analyse its RNase activity. We employed methods such as electrophoresis and fluorimetry to quantify the extent of RNA degradation by p30.”
The researchers observed that the p30 protein’s degradation of host cell RNA depends on its concentration and duration of exposure. This protein is released in a soluble form in ASFV-infected cells and its RNA-degrading ability could assist the virus in altering host cell functions thereby promoting its survival.
The researchers also found that altering the amino acid from cysteine to alanine in p30 resulted in the loss of its RNA-degrading activity. Understanding how the p30 protein in ASFV affects host cell RNA helps illustrate how the virus manipulates cellular functions to survive and spread.
This insight could inform future research into therapies that target these viral mechanisms potentially leading to new ways to combat ASFV infections.
The researchers however acknowledged that critical questions remain unanswered, including the precise role of p30 in ASFV infection in pigs, and whether its RNase activity targets specific host RNA molecules. They intend to study these aspects in the future.