Expression of viral capsid protein antigen against Epstein-Barr virus in plastids ofNicotiana tabacum cv. SR1

Some authors have suggested that the syndrome of transient headache and neurological deficits with cerebrospinal fluid lymphocytosis (HaNDL) results from an immunological response directed against a viral agent. Here we report a case of HaNDL in an immunocompetent 19-year-old male that could support this hypothesis.

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Performance of an immunofiltration assay detecting IgM antibodies against ZEBRA and viral capsid p18 proteins (Immunoquick® filtration EBV M) for the diagnosis of heterophile antibody-negative primary Epstein-Barr virus infection in children

Journal of Clinical Virology ◽

10.1016/j.jcv.2011.12.008 ◽

2012 ◽

Vol 53 (3) ◽

pp. 270-271 ◽

Cited By ~ 1

Author(s):

Luis David Meza ◽

Silvia Sancho-Tello ◽

Beatriz Muñoz-Cobo ◽

Elisa Costa ◽

Dayana Bravo ◽

...

Keyword(s):

Virus Infection ◽

Epstein Barr Virus ◽

Viral Capsid ◽

Epstein Barr Virus Infection ◽

Heterophile Antibody ◽

Barr Virus ◽

Igm Antibodies ◽

Epstein Barr ◽

Barr Virus Infection

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Self-Assembly of Epstein-Barr Virus Capsids

Journal of Virology ◽

10.1128/jvi.01733-08 ◽

2009 ◽

Vol 83 (8) ◽

pp. 3877-3890 ◽

Cited By ~ 39

Author(s):

Brandon W. Henson ◽

Edward M. Perkins ◽

Jonathan E. Cothran ◽

Prashant Desai

Keyword(s):

Amino Acids ◽

Capsid Protein ◽

Self Assembly ◽

Epstein Barr Virus ◽

Major Capsid Protein ◽

Mutational Analysis ◽

Capsid Assembly ◽

Barr Virus ◽

Capsid Shell ◽

Epstein Barr

ABSTRACT Epstein-Barr virus (EBV), a member of the Gammaherpesvirus family, primarily infects B lymphocytes and is responsible for a number of lymphoproliferative diseases. The molecular genetics of the assembly pathway and high-resolution structural analysis of the capsid have not been determined for this lymphocryptovirus. As a first step in studying EBV capsid assembly, the baculovirus expression vector (BEV) system was used to express the capsid shell proteins BcLF1 (major capsid protein), BORF1 (triplex protein), BDLF1 (triplex protein), and BFRF3 (small capsid protein); the internal scaffold protein, BdRF1; and the maturational protease (BVRF2). Coinfection of insect cells with the six viruses expressing these proteins resulted in the production of closed capsid structures as judged by electron microscopy and sedimentation methods. Therefore, as shown for other herpesviruses, only six proteins are required for EBV capsid assembly. Furthermore, the small capsid protein of EBV (BFRF3), like that of Kaposi's sarcoma-associated herpesvirus, was found to be required for assembly of a stable structure. Localization of the small capsid protein to nuclear assembly sites required both the major capsid (BcLF1) and scaffold proteins (BdRF1) but not the triplex proteins. Mutational analysis of BFRF3 showed that the N-terminal half (amino acids 1 to 88) of this polypeptide is required and sufficient for capsid assembly. A region spanning amino acids 65 to 88 is required for the concentration of BFRF3 at a subnuclear site and the N-terminal 65 amino acids contain the sequences required for interaction with major capsid protein. These studies have identified the multifunctional role of the gammaherpesvirus small capsid proteins.

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