Login | Create Account (DAF staff only)

Characterization of the banana streak virus capsid protein and mapping of the immunodominant continuous B-cell epitopes to the surface-exposed N terminus

Vo, Jenny N. and Campbell, Paul R. and Mahfuz, Nur N. and Ramli, Ras and Pagendam, Daniel and Barnard, Ross and Geering, Andrew D. W. (2016) Characterization of the banana streak virus capsid protein and mapping of the immunodominant continuous B-cell epitopes to the surface-exposed N terminus. Journal of General Virology, 97 (12). pp. 3446-3457.

Full text not currently attached. Access may be available via the Publisher's website or OpenAccess link.

Article Link(s): http://dx.doi.org/10.1099/jgv.0.000643

Publisher URL: http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/jgv.0.000643

Abstract

This study identified the structural proteins of two badnavirus species, Banana streak MY virus (BSMYV) and Banana streak OL virus (BSOLV), and mapped the distribution of continuous B-cell epitopes. Two different capsid protein (CP) isoforms of about 44 and 40 kDa (CP1 and CP2) and the virion-associated protein (VAP) were consistently associated with purified virions. For both viral species, the N terminus of CP2 was successfully sequenced by Edman degradation but that of CP1 was chemically blocked. De novo peptide sequencing of tryptic digests suggested that CP1 and CP2 derive from the same region of the P3 polyprotein but differ in the length of either the N or the C terminus. A three-dimensional model of the BSMYV-CP was constructed, which showed that the CP is a multi-domain structure, containing homologues of the retroviral capsid and nucleocapsid proteins, as well as a third, intrinsically disordered protein region at the N terminus, henceforth called the NID domain. Using the Pepscan approach, the immunodominant continuous epitopes were mapped to the NID domain for five different species of banana streak virus. Anti-peptide antibodies raised against these epitopes in BSMYV were successfully used for detection of native virions and denatured CPs in serological assays. Immunoelectron microscopy analysis of the virion surface using the anti-peptide antibodies confirmed that the NID domain is exposed on the surface of virions, and that the difference in mass of the two CP isoforms is due to variation in length of the NID domain.

Item Type:Article
Business groups:Horticulture and Forestry Science
Keywords:intrinsically disordered domain virion structure Badnavirus capsid protein synthetic peptides epitope mapping
Subjects:Plant culture > Fruit and fruit culture > Culture of individual fruits or types of fruit > Bananas
Plant pests and diseases
Plant pests and diseases > Plant pathology
Deposited On:19 Jan 2017 02:26
Last Modified:19 Jan 2017 02:26

Repository Staff Only: item control page