Thank you for considering to present your work as a poster at this event.
Please prepare your poster in A1 portrait format (59cm wide x 84cm long). Please do not laminate your poster or use heavy printing material. Further information about poster sizes can be found on the following link:
Posters larger than A1, or those in landscape orientation, will only be displayed subject to the availability of space.
Maximum capacity 15 A1 potrait posters
Please ensure you have appropriate permissions for the publication of your abstract from the original copyright holders. Should you wish your abstract not to be published, please notify us in writing at the time of abstract submission.
Poster presenters will be required to send us their poster as PDF at least two weeks before the event. The posters will be made available via the event website or other electronic media after the event (see copyright terms).
Posters will be displayed for the full duration of the event. Titles of accepted poster abstracts will be displayed below.
(Presenters in Bold)
If your abstract has been accepted for presentation but it does not appear in the list below, please let us know as soon as possible by email on FluOxford@gmail.com.
Investigating membrane viral bending proteins in coronavirus replication
Entedar A Alsaadi1, Benjamin, W Neuman2, Ian M Jones1
1 Biological Sciences, University of Reading, Whiteknights, RG6 6AH, UK
2 Biological Sciences, texas A&M, University of Texarkana, USA
The coronavirus envelope spike (S) glycoprotein causes fusion between virus and host cell membranes. The fusion peptide has yet to be definitively identified but bioinformatics analysis suggests that it may be located near the amino terminus of the S2 region. In addition, the coronavirus nonstructural proteins (nsp) 3, 4, and 6 are thought to have fundamental functions in the rearrangement of the membranes that are required for the establishment of the viral replication–transcription complexes (RTCs). Nsp3, nsp4 and nsp6 may also have roles in the creation of double-membrane vesicles (DVMs) that are considered the site for viral RNA synthesis but their precise role is not well understood. Thus, S, nsp3, nsp4 and nsp6 potentially all contain membrane-modifying peptides…
Assessment of a pseudotyped virus neutralisation assay for Ebola virus
Kimberley Steeds1, Yper Hall1, Edward Wright2, Thomas Strecker3, Julian A Hiscox4, Georgios Pollakis4 and Miles W Carroll1
1 Public Health England (PHE), Porton Down, Salisbury, Wiltshire, SP4 0JG, UK
2 Viral Pseudotype Unit (VPU), University of Westminster, London, W1W 6UW, UK
3 Institute of Virology, University of Marburg, 35043, Marburg, Germany
4 Institute of Infection and Global Health (IGH), University of Liverpool, Liverpool, L69 7BE, UK
Ebola virus (EBOV), a member of the family Filoviridae, is an enveloped, single stranded RNA virus that can cause Ebola virus disease (EVD), a highly lethal illness with up to 90% mortality. The viral surface glycoprotein (GP1,2) mediates host cell attachment and fusion, and is the primary target for neutralising antibodies. Serological studies are vital to assess the neutralising ability of antibodies targeted to GP1,2, however handling of EBOV is limited to containment level 4 laboratories. Pseudotyped viruses (PVs) are increasingly being used in serological assays for the investigation of viral infection or vaccine seroconversion. The aim of this study was to assess the suitability of an EBOV GP PV system to measure neutralising antibody titres in plasma derived from EVD convalescent volunteers. EBOV GP PVs were generated by co-transfection of…