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Prolixicin: a novel antimicrobial peptide isolated from Rhodnius prolixus with differential activity against bacteria and Trypanosoma cruzi
Article first published online: 12 SEP 2011
© 2011 The Authors. Insect Molecular Biology © 2011 The Royal Entomological Society
Insect Molecular Biology
Volume 20, Issue 6, pages 775–786, December 2011
How to Cite
Ursic-Bedoya, R., Buchhop, J., Joy, J. B., Durvasula, R. and Lowenberger, C. (2011), Prolixicin: a novel antimicrobial peptide isolated from Rhodnius prolixus with differential activity against bacteria and Trypanosoma cruzi. Insect Molecular Biology, 20: 775–786. doi: 10.1111/j.1365-2583.2011.01107.x
- Issue published online: 2 NOV 2011
- Article first published online: 12 SEP 2011
Fig. S1. Prolixicin alignment with members of the Diptericin family of antimicrobial peptides. Multiple sequence analysis was performed using Clustal W with Lasergene's MegAlign module (DNAstar, Madison, WI, USA). Sequences used in the alignment were: Protophormia terraenovae Diptericin (CAB57822.1); Mayetiola destructor Diptericin (ABG21230.1); Drosophila melanogaster Diptericin A (NP_476808.1), B (NP_523787.2) Glossina morsitans morsitans Diptericin A (AAL34111.1) Stomoxys calcitrans Diptericin A (AAY98016.1), and Rhodnius prolixus Prolixicin (bankit1060780 EU448993). Boxed amino acids represent identities to the consensus and residue numbering is based on Prolixicin.
Fig. S2. Expression of Prolixicin tissue in different tissues of Rhodnius prolixus. 1: Egg; 2: Salivary glands; 3: Thorax; 4: Fat body; 5: Fat body 24 h after bacterial injection; 6: Midguts; 7: Midguts 24 h after bacterial injection; 8: No template control.
Fig. S3. Recombinant purified Prolixicin. Sodium dodecyl sulphate polyacrylamide gel electrophoresis containing 1 μg of protein per lane. M: Marker (Precision Plus Protein Standard, Bio-Rad); 1: Elution from the chitin binding column; 2: Retentate after filtration through 5 MWCO cut-off filter; 3: Resuspended protein used in the MIC assays (batch 8.05.2009); 4: Resuspended protein used in the MIC assays (batch 5.06.2009). The band at ≅36 kDa is the fusion protein (expected size 36.6 kDa). Just above 25 kDa one can see the fusion partner (expected size 28 kDa), the strongest band at the bottom of the gel is Prolixicin (expected size ≅11 kDa).
Table S1. Prolixicin's promoter putative transcription factor binding sites. Putative transcription binding sites were identified using Alibaba 2.1 software, which predicts transcription factor binding sites by context dependent matrices generated from TRANSFAC public sites. Putative binding sites' location is given relative to the start methionine codon.
Table S2. Sources of sequences of insect Antimicrobial Peptides used in Phylogenetic analyses.
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