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Characterization of an envelope protein (VP110) of White spot syndrome virus
Author(s) -
Li Li,
Shumei Lin,
Feng Yang
Publication year - 2006
Publication title -
journal of general virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.55
H-Index - 167
eISSN - 1465-2099
pISSN - 0022-1317
DOI - 10.1099/vir.0.81730-0
Subject(s) - white spot syndrome , open reading frame , biology , immunoelectron microscopy , microbiology and biotechnology , blot , virus , fusion protein , peptide sequence , escherichia coli , virology , viral envelope , antibody , biochemistry , recombinant dna , gene , genetics
A protein of 110 kDa (termed VP110) from the envelope fraction of White spot syndrome virus (WSSV) was identified by SDS-PAGE and mass spectrometry. The resulting amino acid sequence matched an open reading frame (wsv035) containing an Arg-Gly-Asp (RGD) motif in the WSSV genome database. To validate the mass-spectrometry result, the C-terminal segment of the wsv035 open reading frame was expressed in Escherichia coli as a fusion protein, which was used to produce specific antibody. Analysis by Western blotting and immunoelectron microscopy demonstrated that VP110 was an envelope protein of WSSV. An interaction analysis was performed between VP110 and the host cells, using a fluorescence assay and a competitive-inhibition assay. The results showed that VP110 was capable of attaching to host cells and that adhesion could be inhibited by synthetic RGDT peptides, suggesting that the RGD motif in the VP110 sequence may play a role in WSSV infection.

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