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Major Capsid Proteins (major + capsid_protein)
Selected AbstractsApplication of in situ detection techniques to determine the systemic condition of lymphocystis disease virus infection in cultured gilt-head seabream, Sparus aurata L.JOURNAL OF FISH DISEASES, Issue 2 2009I Cano Abstract Immunohistochemistry (IHC) and in situ hybridization (ISH) techniques have been used for the detection of lymphocystis disease virus (LCDV) in formalin-fixed, paraffin-embedded tissues from gilt-head seabream, Sparus aurata L. Diseased and recovered fish from the same population were analysed. IHC was performed with a polyclonal antibody against a 60-kDa viral protein. A specific digoxigenin-labelled probe, obtained by PCR amplification of a 270-bp fragment of the gene coding the LCDV major capsid protein, was used for ISH. LCDV was detected in skin dermis and gill lamellae, as well as in several internal organs such as the intestine, liver, spleen and kidney using both techniques. Fibroblasts, hepatocytes and macrophages seem to be target cells for virus replication. The presence of lymphocystis cells in the dermis of the skin and caudal fin, and necrotic changes in the epithelium of proximal renal tubules were the only histological alterations observed in fish showing signs of the disease. [source] Protection of red sea bream Pagrus major against red sea bream iridovirus infection by vaccination with a recombinant viral proteinMICROBIOLOGY AND IMMUNOLOGY, Issue 3 2010Hajime Shimmoto ABSTRACT Megalocytivirus infections cause serious mass mortality in marine fish in East and Southeast Asian countries. In this study the immunogenicity of crude subunit vaccines against infection by the Megalocytivirus RSIV was investigated. Three capsid proteins, 18R, 351R and a major capsid protein, were selected for use as crude subunit vaccines. High homology among Megalocytivirus types was found in the initial sequence examined, the 351R region. Red sea bream (Pagrus major) juveniles were vaccinated by intraperitoneal injection of recombinant formalin-killed Escherichia coli cells expressing these three capsid proteins. After challenge infection with RSIV, fish vaccinated with the 351R-recombinant bacteria showed significantly greater survival than those vaccinated with control bacteria. The 351R protein was co-expressed with GAPDH from the bacterium Edwardsiella tarda in E. coli; this also protected against viral challenge. A remarkable accumulation of RSIV was observed in the blood of vaccinated fish, with less accumulation in the gills and spleen tissues. Thus, the 351R-GAPDH fusion protein is a potential vaccine against Megalocytivirus infection in red sea bream. [source] Beet yellows virus: the importance of being differentMOLECULAR PLANT PATHOLOGY, Issue 2 2003Valerian V. Dolja SUMMARY Taxonomic relationship: Type member of the genus Closterovirus, family Closteroviridae. A member of the alphavirus-like supergroup of positive-strand RNA viruses. Physical properties: Virions are flexuous filaments of ,1300 nm in length and ,12 nm in diameter that are made up of a ,15.5 kb RNA and five proteins. The major capsid protein forms virion body of helical symmetry that constitutes ,95% of the virion length. The short virion tail is assembled by the minor capsid protein, Hsp70-homologue, ,64-kDa protein, and ,20-kDa protein. Viral proteins: The 5,-most ORFs 1a and 1b encode leader proteinase and RNA replicase. The remaining ORFs 2,8 are expressed by subgenomic mRNAs that encode 6-kDa membrane protein, Hsp70 homologue, ,64-kDa protein, minor and major capsid proteins, ,20-kDa protein, and ,21-kDa protein, respectively. Hosts: The principal crop plants affected by Beet yellows virus (BYV) are sugar beet (Beta vulgaris) and spinach (Spinacea oleracea). In addition, BYV was reported to infect ,120 species in 15 families. Most suitable propagation species are Nicotiana benthamiana, Tetragonia expansa, and Claytonia perfoliata. [source] Enhanced matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis of bacteriophage major capsid proteins with , -mercaptoethanol pretreatmentRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 1 2010Casey R. McAlpin Bacteriophage (phage) proteins have been analyzed previously with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). However, analysis of phage major capsid proteins (MCPs) has been limited by the ability to reproducibly generate ions from MCP monomers. While the acidic conditions of MALDI-TOF MS sample preparation have been shown to aid in disassembly of some phage capsids, many require further treatment to successfully liberate MCP monomers. The findings presented here suggest that , -mercaptoethanol reduction of the disulfide bonds linking phage MCPs prior to mass spectrometric analysis results in significantly increased MALDI-TOF MS sensitivity and reproducibility of Yersinia pestis -specific phage protein profiles. Copyright © 2009 John Wiley & Sons, Ltd. [source] | ||||||||||