Publication: Binding of shrimp cellular proteins to Taura syndrome viral capsid proteins VP1, VP2 and VP3
Issued Date
2006-12-01
Resource Type
ISSN
01681702
Other identifier(s)
2-s2.0-33750319867
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Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Virus Research. Vol.122, No.1-2 (2006), 69-77
Suggested Citation
Saengchan Senapin, Amornrat Phongdara Binding of shrimp cellular proteins to Taura syndrome viral capsid proteins VP1, VP2 and VP3. Virus Research. Vol.122, No.1-2 (2006), 69-77. doi:10.1016/j.virusres.2006.06.013 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/22937
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Title
Binding of shrimp cellular proteins to Taura syndrome viral capsid proteins VP1, VP2 and VP3
Author(s)
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 β-actin, elongation factor 1α (EF1α), lysozyme (Lys) and laminin receptor/ribosomal protein p40 (Lamr/p40) containing a putative palindromic laminin binding region LMWWML. VP2 interacted with β-actin and EF1α, 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. © 2006 Elsevier B.V. All rights reserved.