Toward an understanding of the molecular mechanism for successful blood feeding by coupling proteomics analysis with pharmacological testing of horsefly salivary glands.
Horseflies are economically important blood-feeding arthropods and also a nuisance for humans and vectors for filariasis. They rely heavily on the pharmacological properties of their saliva to get a blood meal and suppress immune reactions of hosts. Little information is available on antihemostatic substances in horsefly salivary glands; especially no horsefly immune suppressants have been reported. By proteomics or peptidomics and coupling transcriptome analysis with pharmacological testing, several families of proteins or peptides, which act mainly on the hemostatic system or immune system of the host, were identified and characterized from 30,000 pairs salivary glands of the horsefly Tabanus yao (Diptera, Tabanidae). They are: (i) a novel family of inhibitors of platelet aggregation including two members, which possibly inhibit platelet aggregation by a novel mechanism and act on platelet membrane, (ii) a novel family of immunosuppressant peptides including 12 members, which can inhibit interferon-gamma production and increase interleukin-10 secretion, (iii) a serine protease inhibitor with 56 amino acid residues containing anticoagulant activity, (iv) a serine protease with anticoagulant activity, (v) a protease with fibrinogenolytic activity, (vi) three families of antimicrobial peptides including six members, (vii) a hyaluronidase, (viii) a vasodilator peptide, which is an isoform of vasotab identified from Hybomitra bimaculata, and interestingly (ix) two metallothioneins, which are the first metallothioneins reported from invertebrate salivary glands. The current work will facilitate the understanding of the molecular mechanisms of the ectoparasite-host relationship and help in identifying novel vaccine targets and novel leading pharmacological compounds.
Xu
Xueqing
X
Biotoxin Units of Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming 650223, Yunnan, China.
Yang
Hailong
H
Ma
Dongying
D
Wu
Jing
J
Wang
Yipeng
Y
Song
Yuzhu
Y
Wang
Xu
X
Lu
Yi
Y
Yang
Junxing
J
Lai
Ren
R
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism; D005591:Chemical Fractionation; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004175:Diptera / Q000737:chemistry* / Q000187:drug effects; D005247:Feeding Behavior / Q000187:drug effects; D006821:Hyaluronoglucosaminidase / Q000302:isolation & purification; D007166:Immunosuppressive Agents / Q000737:chemistry / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D008070:Lipopolysaccharides / Q000494:pharmacology; D008668:Metallothionein / Q000302:isolation & purification; D051379:Mice; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D010974:Platelet Aggregation / Q000187:drug effects; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry / Q000378:metabolism; D040901:Proteomics / Q000379:methods*; D012469:Salivary Glands / Q000737:chemistry* / Q000187:drug effects; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013154:Spleen / Q000166:cytology / Q000187:drug effects; D014020:Tissue Extracts
D023181:Antimicrobial Cationic Peptides; D018076:DNA, Complementary; D007166:Immunosuppressive Agents; D019476:Insect Proteins; D008070:Lipopolysaccharides; D010455:Peptides; D010975:Platelet Aggregation Inhibitors; D015842:Serine Proteinase Inhibitors; D014020:Tissue Extracts; D008668:Metallothionein; D006821:Hyaluronoglucosaminidase