Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the full-length transcripts (cDNA) and proteins.
The venom gland of the snake Bitis gabonica (Gaboon viper) was used for the first time to construct a unidirectional cDNA phage library followed by high-throughput sequencing and bioinformatic analysis. Hundreds of cDNAs were obtained and clustered into contigs. We found mostly novel full-length cDNA coding for metalloproteases (P-II and P-III classes), Lys49-phospholipase A2, serine proteases with essential mutations in the active site, Kunitz protease inhibitors, several C-type lectins, bradykinin-potentiating peptide, vascular endothelial growth factor, nucleotidases and nucleases, nerve growth factor, and L-amino acid oxidases. Two new members of the recently described short coding region family of disintegrin, displaying RGD and MLD motifs are reported. In addition, we have identified for the first time a cytokine-like molecule and a multi-Kunitz protease inhibitor in snake venoms. The CLUSTAL alignment and the unrooted cladograms for selected families of B. gabonica venom proteins are also presented. A significant number of sequences were devoid of database matches, suggesting that their biologic function remains to be identified. This paper also reports the N-terminus of the 15 most abundant venom proteins and the sequences matching their corresponding transcripts. The electronic version of this manuscript, available on request, contains spreadsheets with hyperlinks to FASTA-formatted files for each contig and the best match to the GenBank and Conserved Domain Databases, in addition to CLUSTAL alignments of each contig. We have thus generated a comprehensive catalog of the B. gabonica venom gland, containing for each secreted protein: (i) the predicted molecular weight, (ii) the predicted isoelectric point, (iii) the accession number, and (iv) the putative function. The role of these molecules is discussed in the context of the envenomation caused by the Gaboon viper.
Medical Entomology Section, Laboratory of Malaria and Vector Research, National Institutes of Allergy and Infectious Diseases, National Institutes of Health, Rockville, MD 20852, USA. ifrancischetti@niaid.nih.gov
Ivo M B
IM
Francischetti
Van
V
My-Pham
Jim
J
Harrison
Mark K
MK
Garfield
José M C
JM
Ribeiro
D000594:Amino Acid Oxidoreductases / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D007611:Aprotinin / Q000235:genetics; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D003851:Deoxyribonucleases / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D015723:Gene Library; D006133:Growth Substances / Q000235:genetics; D050830:L-Amino Acid Oxidase; D037181:Lectins, C-Type / Q000235:genetics; D045726:Metalloproteases / Q000235:genetics; D008969:Molecular Sequence Data; D009708:Nucleotidases / Q000235:genetics; D010741:Phospholipases A / Q000235:genetics; D010802:Phylogeny; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics; D012910:Snake Venoms / Q000235:genetics* / Q000378:metabolism; D017819:Viperidae / Q000235:genetics* / Q000378:metabolism
D018076:DNA, Complementary; D006133:Growth Substances; D037181:Lectins, C-Type; D011506:Proteins; D012910:Snake Venoms; D007611:Aprotinin; D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase; D003851:Deoxyribonucleases; D010741:Phospholipases A; D009708:Nucleotidases; D045726:Metalloproteases; D012697:Serine Endopeptidases