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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/32962
Title: Yellow head virus binding to cell surface proteins from Penaeus monodon hemocytes
Authors: Phattara orn Havanapan
Suparat Taengchaiyaphum
Apichai Bourchookarn
Albert J. Ketterman
Chartchai Krittanai
Mahidol University
Prince of Songkla University
Keywords: Agricultural and Biological Sciences;Environmental Science;Medicine
Issue Date: 1-Dec-2014
Citation: Fish and Shellfish Immunology. Vol.41, No.2 (2014), 126-136
Abstract: © 2014 Elsevier Ltd. Our previous data revealed that viral particles of yellow head virus (YHV) specifically interacted with granule-containing hemocytes. After isolation of targeted hemocytes, biotinylation was performed using Biotin-NSH-LC. Biotinylated protein was extracted and separated by 2-D PAGE. Electro-transferred proteins on a nitrocellulose membrane were probed with streptavidin-HRP complex to detect biotinylated proteins. The data from 2-D PAGE combined with affinity pull down purification revealed 8 and 6 biotinylated proteins specific to hyaline and granule containing hemocytes, respectively. Four proteins were found in common for both two hemocytes. The majority of proteins detected in granular hemocytes are membrane-associated proteins and immune-related proteins such as alpha-2-macroglobulin (A2M), kazal-type serine protease inhibitor (SPI) and crustin. Crustin. Pm1 was found to bind to YHV as shown with biotinylation pull-down assay and confirmed with two-dimensional virus overlay protein binding assay (2-D VOPBA). The expression of crustin. Pm1 was observed in semigranular and granular hemocytes whereas very low or no expression occurred in hyaline hemocytes. Crustin. Pm1 appears to either be directly involved in cellular binding or mediating virus internalization into permissive hemocytes.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84907689141&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/32962
ISSN: 10959947
10504648
Appears in Collections:Scopus 2011-2015

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