Format (Microsoft Office Word, See Example)
· Language: English
· Font: Times New Roman 12pt
· Abstract title in bold
· Author names and surnames should be written clearly, with capital letters and in italics. The name of the author who will make the presentation should be underlined. The institutions to which the authors are affiliated should be indicated with indices.
· The e-mail address of the author who will make the presentation should be specified.
· Abstracts should not exceed 250 words. (don't count the title, author names and institutions)
· Abstracts should be justified.
· Single line spacing should be used.
When naming the abstract file (Microsoft Word should be used)
1) Verbal and Poster
2) Line ()
3) your last name
Example: When Özdemir, E. sends two abstracts, one verbal and the other poster.
Verbal-Ozdemir.doc and Poster-Ozdemir.doc
Impact of a baculovirus metalloprotease on Mamestra configurata insect intestinal mucins
Umut Toprak1,2 , Doug Baldwin1, Martin Erlandson1,2 , Cedric Gillott2 ,
Dwayne D. Hegedus1,3
1Agriculture and Agri-Food Canada, Saskatoon Research Centre, 107
Science Place, Saskatoon, SK, Canada S7N 0X2
2 Department of Biology, University of Saskatchewan 112 Science Place, Saskatoon, SK, Canada S7N 5E2
3 Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon, SK, Canada S7N 5A8
Baculoviruses are insect specific pathogens that have the potential to control insect pests. For per os infection, baculovirus virions must cross the peritrophic matrix (PM) to reach the midgut epithelium, the initial site of virus replication. Insect intestinal mucins (IIM) comprise a key subset of PM structural proteins. The IIM are thought to be critical to the protective functions ascribed to the PM, as well as in aiding in the passage of the food bolus through the gut. Some baculoviruses, including Mamestra configurata nucleopolyhedrovirus (MacoNPV), encode metalloproteases, referred to as enhancins, which are thought to facilitate infection by degrading IIM within the PM. In this study we examined the interaction between MacoNPV enhancin and several IIM previously identified from the M. configurata PM by using McIIM specific antibodies and western blots. Per os infection of M. configurata larvae with MacoNPV occulusion bodies (OB) showed that McIIM4 was degraded within 4 hours of OB ingestion while another McIIM, McIIM2, was not affected. Time course experiments indicated that the PM recovered by 8 h post-infection when no McIIM4 degradation was detected. In a series of in vitro assays, OB of MacoNPV and recombinant Autographa californica MNPV expressing MacoNPV enhancin were incubated with dissected PM. Western blots showed that McIIM4 was degraded in the presence of either virus. Degradation of McIIM4 was inhibited by EDTA, an inhibitor of metalloproteases. Thus, MacoNPV enhancin appears capable of degrading a major structural PM protein, but exhibits specificity in the substrates that it targets.
Key words: Baculovirus metalloprotease, Mamestra configurata, intestinal mucin, perithrophic matrix
Posters should include a descriptive title, introduction, materials and methods, results and discussion sections, and a bibliography should be cited. Posters should be prepared in the dimensions of 90cm (length) X 60cm (width). Authors whose abstracts are accepted will be informed.
Participants who will make verbal presentations will be given a total of 15 minutes, including the question-answer part.