title: Binding of shrimp cellular proteins to Taura syndrome viral capsid proteins VP1, VP2 and VP3.
abstract: 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.
authors.affiliation: National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Pathumthani 12120, Thailand. saengchan@biotec.or.th
authors.forename: Saengchan
authors.initials: S
authors.lastname: Senapin
authors.forename: Amornrat
authors.initials: A
authors.lastname: Phongdara
mesh_terms: D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015153:Blotting, Western; D036022:Capsid Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009113:Muramidase / Q000378:metabolism; D033561:Penaeidae / Q000737:chemistry*; D020648:Peptide Elongation Factor 1 / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D012328:RNA Viruses; D017474:Receptors, Laminin / Q000378:metabolism; D016415:Sequence Alignment; D020798:Two-Hybrid System Techniques
chemical_list: D000199:Actins; D036022:Capsid Proteins; D020648:Peptide Elongation Factor 1; D011506:Proteins; D017474:Receptors, Laminin; D009113:Muramidase