Abstract
Shrimp White Spot Syndrome Virus (WSSV) is the major pathogen causing huge economic losses to the industry worldwide. This virus infected several crustacean species including shrimps, crabs and crayfish and the clinical signs of the disease include a red color to the entire body and appendages along with small subcutaneous white spots. Present project focuses on the structural elucidation of the envelope proteins of WSSV by X-ray crystallography, including VP26, VP28. These structure proteins are of major importance to determine the taxonomic position of the virus and provide important information on the design of specific inhibitors or drugs to make the shrimp disease caused by WSSV under control. VP26 is one of the major envelope proteins of WSSV. Because N-terminus is a strong hydrophobic transmembrane domain, the N terminal 34 aa have been truncated from the VP26. The 3D structure of truncated VP26 has been determined by multiwavelength anomalous dispersion (MAD) phasing and refined to 2.2Ǻ. Overall, the structure is predominantly beta strands and only contains a small á helix. A search of overall structural similarities against the DALI database failed to reveal any significant matchs. However, VP26 shows a beta barrel with jellyroll topology that is the most common fold found in viral capsid proteins.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
