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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Structure of a major immunogenic site on foot-and-mouth disease virus

Article Abstract:

A characterization of the structure of a major immunogenic site on foot-and-mouth disease virus (FMDV) is reported. A previous effort to characterize the crystal structure of FMDV was hampered by poor visibility of the Arg-Gly-Asp-containing loop which attaches the virus to its cellular receptor and which is also highly antigenic. The difficulty was resolved by reducing a particular disulphide bond which enabled the description of an unambiguous infective crystal structure. The correlation of this crystal structure to key biological properties of FMDV were presented and discussed.

Author: Newman, John, Lewis, Richard, Logan, Derek, Abu-Ghazaleh, Robin, Blakemore, Wendy, Curry, Stephen, Jackson, Terry, King, Andrew, Lea, Susan, Parry, Nigel, Rowlands, David, Stuart, David, Fry, Elizabeth
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
Analysis, Structure-activity relationships (Biochemistry), Foot-and-mouth disease virus, Foot and mouth disease virus

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The crystal structure of bluetongue virus VP7

Article Abstract:

Viral structural proteins reveal a new type of molecular architecture, the crystal structure of VP7 found in bluetongue virus (BTV), an orbivirus gene of the Reoviridae family. The viruses possess a double-stranded segmented RNA genomic structure inside a capsid, with a VP2 outer layer and an alpha VP5 layer which is removed when the virus enters the host cell. The occurrence of VP7 is a strange phenomena in this virus and the VP7 strands are formed as trimers when the virus enters the host cell. The VP7 consists of two domains of alpha helices.

Author: Stuart, David, Roy, Polly, Grimes, Jonathan, Basak, Ajit K.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
Viruses, Morphology (Biology), Reoviruses

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Crystal structure of SIV matrix antigen and implications for virus assembly

Article Abstract:

The crystal structure of simian immunodeficiency virus (SIV) matrix antigen (MA) indicates the formation of a trimer with many biological properties of MA. SIV is similar to the human immunodeficiency virus (HIV) and their matrix antigens are identical in about half of the sequences. MA is a part of the Pr55Gag protein that is necessary for assembly of the virion shell. MA helps in the incorporation of virus envelope protein and assembly of the Pr55Gag shell.

Author: Stuart, David I., Jones, Ian M., Fry, Elizabeth, Roy, Polly, Rao, Zihe, Belyaev, Alexander S.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
Proteins, Protein structure, Simian immunodeficiency virus

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Subjects list: Research
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