TY - JOUR
T1 - Insight into the salivary transcriptome and proteome of dipetalogaster maxima
AU - Assumpção, Teresa C.F.
AU - Charneau, Sébastien
AU - Santiago, Paula B.M.
AU - Francischetti, Ivo M.B.
AU - Meng, Zhaojing
AU - Araújo, Carla N.
AU - Pham, Van M.
AU - Queiroz, Rayner M.L.
AU - De Castro, Cleudson Nery
AU - Ricart, Carlos André
AU - Santana, Jaime M.
AU - Ribeiro, Jose M.C.
PY - 2011/2/4
Y1 - 2011/2/4
N2 - Dipetalogaster maxima is a blood-sucking Hemiptera that inhabits sylvatic areas in Mexico. It usually takes its blood meal from lizards, but following human population growth, it invaded suburban areas, feeding also on humans and domestic animals. Hematophagous insect salivary glands produce potent pharmacologic compounds that counteract host hemostasis, including anticlotting, antiplatelet, and vasodilatory molecules. To obtain further insight into the salivary biochemical and pharmacologic complexity of this insect, a cDNA library from its salivary glands was randomly sequenced. Salivary proteins were also submitted to one-and two-dimensional gel electrophoresis (1DE and 2DE) followed by mass spectrometry analysis. We present the analysis of a set of 2728 cDNA sequences, 1375 of which coded for proteins of a putative secretory nature. The saliva 2DE proteome displayed approximately 150 spots. The mass spectrometry analysis revealed mainly lipocalins, pallidipins, antigen 5-like proteins, and apyrases. The redundancy of sequence identification of saliva-secreted proteins suggests that proteins are present in multiple isoforms or derive from gene duplications.
AB - Dipetalogaster maxima is a blood-sucking Hemiptera that inhabits sylvatic areas in Mexico. It usually takes its blood meal from lizards, but following human population growth, it invaded suburban areas, feeding also on humans and domestic animals. Hematophagous insect salivary glands produce potent pharmacologic compounds that counteract host hemostasis, including anticlotting, antiplatelet, and vasodilatory molecules. To obtain further insight into the salivary biochemical and pharmacologic complexity of this insect, a cDNA library from its salivary glands was randomly sequenced. Salivary proteins were also submitted to one-and two-dimensional gel electrophoresis (1DE and 2DE) followed by mass spectrometry analysis. We present the analysis of a set of 2728 cDNA sequences, 1375 of which coded for proteins of a putative secretory nature. The saliva 2DE proteome displayed approximately 150 spots. The mass spectrometry analysis revealed mainly lipocalins, pallidipins, antigen 5-like proteins, and apyrases. The redundancy of sequence identification of saliva-secreted proteins suggests that proteins are present in multiple isoforms or derive from gene duplications.
KW - D. maxima
KW - Hematophagy
KW - Proteome
KW - Saliva
KW - Transcriptome
KW - Triatomine
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U2 - 10.1021/pr100866h
DO - 10.1021/pr100866h
M3 - Article
C2 - 21058630
AN - SCOPUS:79955421119
SN - 1535-3893
VL - 10
SP - 669
EP - 679
JO - Journal of proteome research
JF - Journal of proteome research
IS - 2
ER -