Scientists at Rutgers University and Emory University have identified the structure of a hepatitis C virus surface protein, a finding that could potentially further the development of a vaccine.
A report published in Nature describes the structure of E2, one of two surface glycoproteins, which the virus uses to bind to human cells. Identification of the structure of the virus’s outer protein will allow scientists more insight into the development of a vaccine that targets the immune system to vulnerable regions of the virus to prevent infection.
According to the findings, the E2 surface glycoprotein binds to the host cell via interactions with scavenger receptor class B type 1 and CD81. It serves as a target for neutralizing antibodies. E2 is predicted to be a class II viral fusion protein. The structure of the E2 core domain is described as compact and consisting mostly of β-strands and random coil with two small α-helices.
“The strands are arranged in two, perpendicular sheets (A and B), which are held together by an extensive hydrophobic core and disulphide bonds. Sheet A has an IgG-like fold that is commonly found in viral and cellular proteins, whereas sheet B represents a novel fold. Solution-based studies demonstrate that the full-length E2 ectodomain has a similar globular architecture and does not undergo significant conformational or oligomeric rearrangements on exposure to low pH. Thus, the IgG-like fold is the only feature that E2 shares with class II membrane fusion proteins,” the researchers wrote.
Source: Khan AG. Nature. 2014