TheEnv-like Open Reading Frame of the Baculovirus-Integrated Retrotransposon TED Encodes a Retrovirus-like Envelope Protein

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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A novel envelope protein involved in White spot syndrome virus infection

Journal of General Virology ◽

10.1099/vir.0.80923-0 ◽

2005 ◽

Vol 86 (5) ◽

pp. 1357-1361 ◽

Cited By ~ 28

Author(s):

Ru Huang ◽

Yunli Xie ◽

Jianhong Zhang ◽

Zhengli Shi

Keyword(s):

Escherichia Coli ◽

Virus Infection ◽

Envelope Protein ◽

White Spot Syndrome Virus ◽

Open Reading Frame ◽

White Spot ◽

Structural Protein ◽

Reading Frame ◽

Intact Virion ◽

White Spot Syndrome

One open reading frame (designated vp76) from the White spot syndrome virus (WSSV) genome has the motif of a cytokine I receptor and has been identified as a structural protein. In this paper, vp76 was expressed in Escherichia coli and used to prepare a specific antibody to determine the location of the corresponding protein in the intact virion, the nucleocapsids and the envelope of WSSV. Western blotting with the VP76 antiserum confirmed that VP76 was an envelope protein of WSSV. To investigate the function of the VP76, WSSV was neutralized with the VP76-specific antiserum at different concentrations and injected intramuscularly into crayfish. The mortality curves showed that the VP76 antiserum could partially attenuate infection with WSSV, suggesting that VP76 is an envelope protein involved in WSSV infection.

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Identification of envelope protein ORF10 of channel catfish herpesvirus

Canadian Journal of Microbiology ◽

10.1139/w11-128 ◽

2012 ◽

Vol 58 (3) ◽

pp. 271-277

Author(s):

Yulin Liu ◽

Junfa Yuan ◽

Weimin Wang ◽

Xiaoxuan Chen ◽

Rong Tang ◽

...

Keyword(s):

Channel Catfish ◽

Envelope Protein ◽

Viral Protein ◽

Protein A ◽

Neutralization Assay ◽

Open Reading Frame ◽

Viral Pathogen ◽

Ovary Cells ◽

Viral Neutralization ◽

Reading Frame

Channel catfish virus (CCV) is a viral pathogen of fry and fingerling channel catfish and can cause significant commercial loss. Previous studies have shown that the CCV virion contains at least 25 predicted structural proteins, including viral protein 10, which is encoded by the orf10 gene of the CCV. In this paper, the orf10 gene was expressed in Escherichia coli and used to produce a specific antibody. Western blot analysis confirmed that open reading frame 10 is an envelope protein. A viral neutralization assay demonstrated that open reading frame 10 antiserum was able to inhibit CCV infection of channel catfish ovary cells, suggesting that viral protein 10 is likely to play an important role in the CCV infection of channel catfish ovary cells.

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Disulfide Bonds and Membrane Topology of the Vaccinia Virus A17L Envelope Protein

Journal of Virology ◽

10.1128/jvi.74.5.2438-2442.2000 ◽

2000 ◽

Vol 74 (5) ◽

pp. 2438-2442 ◽

Cited By ~ 17

Author(s):

Tatiana Betakova ◽

Bernard Moss

Keyword(s):

Vaccinia Virus ◽

Envelope Protein ◽

Disulfide Bonds ◽

Recombinant Vaccinia Virus ◽

Open Reading Frame ◽

Membrane Topology ◽

Recombinant Vaccinia ◽

Reading Frame ◽

Virion Assembly ◽

Intramolecular Disulfide Bond

ABSTRACT The envelope protein encoded by the vaccinia virus A17L open reading frame is essential for virion assembly. Our mutagenesis studies indicated that cysteines 101 and 121 form an intramolecular disulfide bond and that cysteine 178 forms an intermolecular disulfide linking two A17L molecules. This arrangement of disulfide bonds has important implications for the topology of the A17L protein and supports a two-transmembrane model in which cysteines 101 and 121 are intraluminal and cysteine 178 is cytoplasmic. The structure of the A17L protein, however, was not dependent on these disulfide bonds, as a recombinant vaccinia virus with all three cysteine codons mutated to serines retained infectivity.

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