Ession of midgut proteins induced by blood feeding, we compared the
Ession of midgut proteins induced by blood feeding, we compared the abundance of transcripts in the sugar fed and the blood fed libraries using chi-square statistical analysis. We found several transcripts that were significantly more abundant after blood feeding and several that were underrepresented in the blood fed library (see tables 3 and 4). As expected, we observed some transcripts putatively involved in blood digestion and peritrophic matrix formation more abundant after blood feeding. These included the putative peritrophin with four chitin-binding domains, PperPer1. Similar to the putative orthologues in P. papatasi and L. longipalpis, PpPer1 [GenBank:EU031912] and LuloPer1 [GenBank: EU124588], PperPer1 was only detected in the blood fed midgut library. With regard to peritrophin sequence abundance, it is interesting to note that we did not detect any peritrophin sequence highly represented before blood feeding. This is in contrast with the situation described in P. papatasi, where high numbers of a putative peritrophin with one chitin binding domain, PpPer2 [GenBank:EU047543], were detected in sugar fed midguts. In this respect, the observed profile is more similar to peritrophins in the midgut of a more distantly related species L. longipalpis. Transcripts coding for proteolytic enzymes, namely the chymotrypsins PperChym1 and PperChym2 and the trypsin PperTryp3, were also found more abundant in the blood fed library and thus likely represent digestiveTable 3 ESTs overrepresented in the blood fed library (BF) in comparison to the sugar fed library (SF)Cluster # 45 97 81 52 63 139 40 79 102 Putative function microvillar protein (PperMVP1) peritrophin (PperPer1) chymotrypsin (PperChym1) microvillar protein (PperMVP5) trypsin (PperTryp3) microvillar protein (PperMVP4) microvillar protein (SP600125MedChemExpress SP600125 PperMVP2) unknown (lipid recognition) chymotrypsin (PperChym2) SF 0 0 0 0 0 0 0 0 2 BF 681 94 82 35 31 28 26 9 11 P value 7.49E-185 4.46E-23 2.83E-20 2.10E-09 1.76E-08 8.67E-08 2.52E-07 2.47E-03 1.14E-Dost ov?et al. BMC Genomics 2011, 12:223 http://www.biomedcentral.com/1471-2164/12/Page 17 ofTable 4 ESTs overrepresented in the sugar fed library (SF) in comparison to the blood fed library (BF)Cluster # 46 249 1033 16 852 174 18 652 183 Putative function trypsin (PperTryp1) unknown chymotrypsin (PperChym3) trypsin (PperTryp2) catalase (PperCat) glycoside hydrolase (PperGH13) microvillar protein (PperMVP3) 40S ribosomal protein SA glycoside hydrolase (PperGH31) SF 513 25 12 10 10 23 18 8 12 BF 20 3 0 0 0 9 6 1 3 P value 3.16E-115 3.60E-05 5.76E-04 1.68E-03 2.88E-03 1.46E-02 1.56E-02 2.07E-02 2.16E-652) [GenBank:HQ015442] and an unknown, probably non-coding, sequence (cluster 249) [GenBank: GW817178] represented by the clone in the sugar fed midgut, remains unknown.enzymes induced by the intake of blood. On the other hand, three other putative proteases, PperTryp1, PperTryp2 and PperChym3 were significantly less abundant in the blood fed library. We speculate that these molecules may be post-transcriptionally regulated digestive enzymes that are stored in the midgut prior to blood feeding. The most striking differences in sequence abundance before and after blood feeding were observed for the microvillar proteins. PubMed ID:https://www.ncbi.nlm.nih.gov/pubmed/28914615 Four of the five identified putative microvillar proteins (PperMVP1, 2, 4 and 5) were only detected in the blood fed library and in high abundance. This indicates a strong up-regulation of these proteins after the intake of blood. In con.
