Poster Presentation 9th General Meeting of the International Proteolysis Society 2015

Multiple legumains in ticks (#124)

David Hartmann 1 2 , Radek Šíma 1 , Jan Perner 1 , Petr Kopacek 1 , Daniel Sojka 1
  1. BC ASCR, v.v.i., Ceske Budejovice, CZECH REPUBLIC, Czech Republic
  2. Faculty of Science, University of South Bohemia, České Budějovice, Czech Republic
Ixodes ricinus asparaginyl endopeptidase (IrAE1) was the first legumain identified from arthropods. IrAE1 has been characterized as a pivotal cysteine endopeptidase of the multienzyme hemoglobinolytic machinery in ticks. Genomic and EST data from closely related American tick Ixodes scapularis complement IrAE1 with a full–set of nine legumain-like peptidases, IsAE1-9. IsAE1-3 possess the active site triad and are thus capable of protein bond hydrolysis. Following recent discussion, we propose that isoforms with the active site cysteine replaced by serine (IsAE4, 5, 8), and those with modified active site histidine (IsAE4, 7, 9.), may function as protein ligases or carboxylases rather than peptidases. Expressional qRT-PCR profiling over I. scapularis lifestages and tissues demonstrates that predominant abundance of IsAE1 in female guts is accompanied by three other legumains tagged as IsAE2, IsAE4, and IsAE9. Interestingly, IsAE2 replaces IsAE1 as the dominant gut tissue legumain in tick males not feeding on hosts and instead living from blood reserves stored from nymphal feeding. Additionally, IsAE9 with modified active site histidine is also upregulated by bloodfeeding and could possess regulatory roles. IrAE1 and IrAE2 have nearly identical in-silico 3D model structures, yet have distinct properties. IrAE1 recombinantly expressed in yeast is self-catalytically activatable in acidic conditions, and shows a strong preference for asparagine in P1 position as seen from combinational peptidyl substrate library screenings. It is also capable of endopeptidolytic activation (in-trans) of Schistosoma mansoni cathepsin B (SmCB1). In contrast, IrAE2 expressed in yeast does not exhibit self-catalytic activation as seen from fluorescent peptidyl assays and is instead activated by IrAE1 in-trans. In order to ascertain if IrAE1 and IrAE2 have fuctional differences, qRT-PCR, in-vivo LE-28 activity probe labeling (Laura Edgington, Matthew Bogyo) and RNAi experiments are performed. E. coli expressed IrAE1 and IrAE2 are also used for rabbit immunization and tested as anti-tick vaccines.