Binding of shrimp cellular proteins to Taura syndrome viral capsid proteins VP1, VP2 and VP3.

Viruses are a major cause of production losses in the world shrimp-farming industry. Despite this, little is known about viral-host interactions in shrimp due in part to the lack of continuous shrimp cell lines. Here, the yeast two-hybrid assay system was employed to study interactions between three Taura syndrome viral capsid proteins (VP1-VP3) and proteins from a cDNA library of the black tiger shrimp Penaeus monodon. VP1 interacted with beta-actin, elongation factor 1alpha (EF1alpha), lysozyme (Lys) and laminin receptor/ribosomal protein p40 (Lamr/p40) containing a putative palindromic laminin binding region LMWWML. VP2 interacted with beta-actin and EF1alpha, while VP3 bound to the same proteins as VP1 except for Lamr/p40. In vitro pull-down assays confirmed these interactions. The most interesting interaction was specific binding between VP1 and Lamr/p40 since Lamr/p40 has been identified as the mammalian cell receptor for several arthropod-borne viruses (arboviruses). A search of mosquito vector and Drosophila sequences at available databases revealed the presence of putative Lamr/p40 proteins with high homology to the Lamr/p40 from shrimp.