TY - JOUR
T1 - A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua
T2 - Identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome
AU - Veiga, Ana B.G.
AU - Ribeiro, José M.C.
AU - Guimarães, Jorge A.
AU - Francischetti, Ivo M.B.
N1 - Funding Information:
We thank Drs. Thomas E. Wellems, Robert W. Gwadz, and Thomas J. Kindt (NIAID/NIH) for encouragement and support and the Brazilian agency CAPES (Ministry of Science and Technology Department) for the fellowship to A.B.G. Veiga. We thank Van My Phan (LMVR/NIAID) for technical assistance and Dr. Mark K. Garfield (Research Technologies Branch/NIAID) for protein sequencing. We acknowledge Brenda Rae Marshall (NIAID) for editorial assistance. We express special thanks to the Health Department of the city of Videira (Santa Catarina, Brazil) for providing L. obliqua caterpillars. The authors are grateful to both reviewers for their time, comments and valuable suggestions in the manuscript.
PY - 2005/8/1
Y1 - 2005/8/1
N2 - Accidents with the caterpillar Lonomia obliqua are often associated with a coagulation disorder and hemorrhagic syndrome in humans. In the present study, we have constructed cDNA libraries from two venomous structures of the caterpillar, namely the tegument and the bristle. High-throughput sequencing and bioinformatics analyses were performed in parallel. Over one thousand cDNAs were obtained and clustered to produce a database of 538 contigs and singletons (clusters) for the tegument library and 368 for the bristle library. We have thus identified dozens of full-length cDNAs coding for proteins with sequence homology to snake venom prothrombin activator, trypsin-like enzymes, blood coagulation factors and prophenoloxidase cascade activators. We also report cDNA coding for cysteine proteases, Group III phospholipase A2, C-type lectins, lipocalins, in addition to protease inhibitors including serpins, Kazal-type inhibitors, cystatins and trypsin inhibitor-like molecules. Antibacterial proteins and housekeeping genes are also described. A significant number of sequences were devoid of database matches, suggesting that their biologic function remains to be defined. We also report the N-terminus of the most abundant proteins present in the bristle, tegument, hemolymph, and "cryosecretion". Thus, we have created a catalog that contains the predicted molecular weight, isoelectric point, accession number, and putative function for each selected molecule from the venomous structures of L. obliqua. The role of these molecules in the coagulation disorder and hemorrhagic syndrome caused by envenomation with this caterpillar is discussed. All sequence information and the Supplemental Data, including figures and tables with hyperlinks to FASTA-formatted files for each contig and the best match to the databases, are available at http://www.ncbi.nih.gov/projects/omes.
AB - Accidents with the caterpillar Lonomia obliqua are often associated with a coagulation disorder and hemorrhagic syndrome in humans. In the present study, we have constructed cDNA libraries from two venomous structures of the caterpillar, namely the tegument and the bristle. High-throughput sequencing and bioinformatics analyses were performed in parallel. Over one thousand cDNAs were obtained and clustered to produce a database of 538 contigs and singletons (clusters) for the tegument library and 368 for the bristle library. We have thus identified dozens of full-length cDNAs coding for proteins with sequence homology to snake venom prothrombin activator, trypsin-like enzymes, blood coagulation factors and prophenoloxidase cascade activators. We also report cDNA coding for cysteine proteases, Group III phospholipase A2, C-type lectins, lipocalins, in addition to protease inhibitors including serpins, Kazal-type inhibitors, cystatins and trypsin inhibitor-like molecules. Antibacterial proteins and housekeeping genes are also described. A significant number of sequences were devoid of database matches, suggesting that their biologic function remains to be defined. We also report the N-terminus of the most abundant proteins present in the bristle, tegument, hemolymph, and "cryosecretion". Thus, we have created a catalog that contains the predicted molecular weight, isoelectric point, accession number, and putative function for each selected molecule from the venomous structures of L. obliqua. The role of these molecules in the coagulation disorder and hemorrhagic syndrome caused by envenomation with this caterpillar is discussed. All sequence information and the Supplemental Data, including figures and tables with hyperlinks to FASTA-formatted files for each contig and the best match to the databases, are available at http://www.ncbi.nih.gov/projects/omes.
KW - Caterpillar venom
KW - Coagulation
KW - Fibrinolysis
KW - Hemorrhage
KW - Toxins
UR - https://www.scopus.com/pages/publications/23644459517
UR - https://www.scopus.com/pages/publications/23644459517#tab=citedBy
U2 - 10.1016/j.gene.2005.05.002
DO - 10.1016/j.gene.2005.05.002
M3 - Article
C2 - 16023793
AN - SCOPUS:23644459517
SN - 0378-1119
VL - 355
SP - 11
EP - 27
JO - Gene
JF - Gene
IS - 1-2
ER -