Host and Virus Protein Interaction Studies in Understanding Shrimp Virus Gene Function

Abstract

Protein-protein interaction studies have been widely used in several fields to characterize an unknown protein. This in turn helps to find out several pathways to understand a complex mechanism or discover a drug for treatment. Among the methods, yeast two-hybrid has widely been used in human, animal and plant research studies. This aspect of research has also been found useful in understanding the shrimp virus gene function. With respect to White spot syndrome virus, interaction studies have been applied to elucidate virus structure, understand the mode of entry of the virus, mechanism of virus replication and also to discover some of the host anti-viral proteins. Interaction studies on other shrimp viruses are scanty and only few reports available on Yellow head virus and Taura syndrome virus. All these findings are still in preliminary stage and lot more studies are necessary to have the clear picture. Protein interaction research on other shrimp viruses are still lacking. Considering all these, it appears that this field of research has a wide scope to understand the virulence mechanism of shrimp viruses where very little information is available till date.

Sulfated galactans isolated from the red seaweed Gracilaria fisheri target the envelope proteins of white spot syndrome virus and protect against viral infection in shrimp haemocytes

“…These results suggest that binding of SG with the virus is both necessary and dependent on the sulfate groups (Talarico et al, 2004;Matsuhiro et al, 2005;Chattopadhyay et al, 2007). (Zhou et al, 2009;Otta, 2012). The envelope protein VP 26 has been identified as a tegument protein which is supposed to be associated with viral penetration due to its actin binding motif that facilitates the attachment of the virus to the shrimp cell membrane Tsai et al, 2006).…”

“…In the current study, Far-Western blot analysis demonstrated that SG bound to the envelope proteins of WSSV, including VP 24, VP 26, VP 28, VP 31 and VP 39, although only the binding of SG with VP 26 and VP 28 was confirmed. It has been revealed that four major WSSV envelope proteins, VP 19, VP 24, VP 26 and VP 28, form a multiprotein complex for the virus infection process (Zhou et al , 2009; Otta, 2012). The envelope protein VP 26 has been identified as a tegument protein which is supposed to be associated with viral penetration due to its actin binding motif that facilitates the attachment of the virus to the shrimp cell membrane (Xie & Yang, 2005; Tsai et al , 2006).…”