Debra C. Tamvakis

La Trobe University

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Michael Foley

La Trobe University

Carl D. Kirkwood

Gates Foundation

Claudia M. Thalmann

Sentinext Therapeutics (Malaysia)

Nicole C. Donker

Royal Children's Hospital

Joanne L. Casey

Monash University

Wojtek P. Michalski

Australian Centre for Disease Preparedness

Richard K.J. Luke

La Trobe University

Jill Vaughan

Monash University

Abdulmonem M. Sanalla

Misurata University

Kathy Parisi

Hexima (Australia)

Cooperative Institutions

La Trobe University

Commonwealth Scientific and Industrial Research Organisation

University of Melbourne

Australian Centre for Disease Preparedness

CS Diagnostics

Murdoch Children's Research Institute

Royal Children's Hospital

Monash University

University of Queensland

Australian Regenerative Medicine Institute

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Peptides specific for Mycobacterium avium subspecies paratuberculosis infection: diagnostic potential

Protein Engineering Design and Selection (2011)

Joanne L. Casey Abdulmonem M. Sanalla Debra C. Tamvakis Claudia M. Thalmann E. L. Carroll

Mycobacterium avium subspecies paratuberculosis (Map) is the causative agent of Johne's disease (JD). Current serological diagnostic tests for JD are limited by their sensitivity when used in sub-clinical stages of the disease. Our objective was to identify peptides that mimic diagnostically important Map epitopes that might be incorporated into a new-generation JD diagnostic. Four peptides were isolated from a phage-displayed random peptide library by screening on antibodies derived from Map-infected goats. The peptides were recognised by antibodies from Map-infected goats but not by antibodies from uninfected goats. The peptides elicited immune responses in rabbits, which reacted strongly with bona fide Map antigens proving the peptides were true epitope mimics. To assess the diagnostic value a panel of goat sera was screened for reactivity's with peptides. The peptides were recognised by antibodies from a proportion of goats infected with Map compared with control animals with a diagnostic specificity of 100% and the sensitivity ranged from 50 to 75%. Combinations of any two peptides improved sensitivity 62.5–87.5% and 100% sensitivity was achieved with three of the four peptides in combination. These data suggest peptides representing diagnostically important Map epitopes could be incorporated into a sensitive diagnostic test.

Epitope mapping

10.1093/protein/gzr026

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Identification of an antibody-binding epitope on the rotavirus A non-structural protein NSP2 using phage display analysis

Journal of General Virology (2011)

Nicole C. Donker Michael Foley Debra C. Tamvakis Ruth F. Bishop Carl D. Kirkwood

The non-structural protein 2 (NSP2) of rotavirus has important roles in rotavirus replication associated with RNA binding, hydrolysis of NTPs and RNA, and helix destabilizing properties. A cell-culture assay using an NSP2-specific mAb and polyclonal antiserum to block virus replication showed a 73 and 96 % reduction in the amount of virus produced during replication, respectively. Phage display technology was used to identify the antibody-binding region on the NSP2 protein with the motif (244)T-(Y/F)-Ø-Ø-Ø-X-K-Ø-G(252), where Ø is a hydrophilic residue and X is any amino acid. This region was mapped to the three-dimensional NSP2 crystal structure to visualize the epitope. Analysis revealed identity to a region on NSP2 that mapped to a site exposed on the surface of the protein, which could possibly interfere with a functionally important region of the protein. Antibody binding to this region could disrupt the essential roles of NSP2, such as the formation of viroplasms with NSP5 or the interaction with viral RNA, thereby indicating a possible mechanism for the observed inhibition of virus replication. Genetic analysis of the putative binding region of NSP2 revealed a high level of conservation, suggesting that the region is under strict control.

Polyclonal antibodies

10.1099/vir.0.032599-0

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Citations (10)