Inhumane Flu B

Influenza B and human protein NS1B are deadly combination

(RxWiki News) Have you ever wondered why everyone in your home can get the flu and Fido remains uninfected? Now researchers can explain the dog's protection.

The three-dimensional (3D) structure of a site on an influenza B virus protein that disables human defenses to the infection has been discovered by researchers at Rutgers University and the University of Texas at Austin. Knowing this feature is present in humans will help scientists understand how influenza A strains can cross species.

"Scientists are getting to the bottom of influenza B pandemics."

Gaetano Montelione, PhD, a lead author and professor of biochemistry and molecular biology, School of Arts and Sciences at Rutgers reports that their study shows how protein 1 (NS1B), present in influenza B is able to bind to a human host protein that, in turn, doesn't allow the body to fight the flu.

The human protein, called interferon-stimulated gene 15 protein (ISG15), is a key mechanism that human cells engage to naturally fight viral infections. It appears that chemicals that are able to block this inhibiting binding of NS1B to ISG15 will enable the body to fight the virus on its own.

Interestingly, the researchers discovered that this binding doesn't occur in other species like dogs or cats because only humans and other primates have ISG15 molecules for the NS1B to bind to.

Robert Krug, PhD, AB, professor and chair of molecular genetics and microbiology at the University of Texas at Austin reports that the 3D structure of the NS1B-ISG15 complex, which was viewed using X-ray crystallography, has given us a clearer understanding of the molecular basis for this species specifically.

Aaron Shatkin, PhD, director of the Center for Advanced Biotechnology and Medicine (CABM) at Rutgers and an eminent virologist explains that flu infections are a major health problem that needs more drugs to control future pandemics. He also reports this newly observed binding relationship opens up new avenues for research and new drug development.

The findings are detailed in a paper published in Proceedings of the National Academy of Sciences.

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Review Date: 
August 27, 2011