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Toward a catalog for the transcripts and proteins (sialome) from the salivary gland of the malaria vector Anopheles gambiae

Ivo M. B. Francischetti¹, Jesus G. Valenzuela¹, Van My Pham¹, Mark K. Garfield² and José M. C. Ribeiro^1,*

¹ Medical Entomology Section, Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD20892-0425, USA
² Research Technology Branch, Twinbrook II, USA

View larger version (48K): [in a new window]   Fig. 1. SDS-PAGE of A. gambiae salivary proteins, under denaturing non-reducing conditions. Molecular mass markers are shown on the left. The match found is shown on the right. *Sequence was obtained using salivary protein separated by a 12 % NU-PAGE gel, Mops buffer, under denaturing non-reducing conditions.

View larger version (22K): [in a new window]   Fig. 2. Comprehensive bio-informatic analysis of 5' EST from A. gambiae cDNA library and data generation. A. gambiae cDNA libraries enriched for full coding clones were constructed. 5' EST sequences were systematically generated from the clones and analyzed for hits in nonredundant databases. Signal peptides were predicted by submission of the cluster sequences to the SignalP server, allowing the identification of putative secretory (S), housekeeping (H) or unknown (U) cDNAs. Putative functions were annotated according to database hits, when available.

View larger version (29K): [in a new window]   Fig. 3. A. gambiae salivary gland EST. The 691 individual sequences were assigned as secretory (S), housekeeping (H) or unknown (U) function cDNAs and the % representation is shown in (A). The 251 clusters were assigned as having no matches to the database, or having hits to sequences obtained from D. melanogaster (or other organisms), or from A. gambiae, and the % representation is shown in (B).

View larger version (78K): [in a new window]   Fig. 4. CLUSTAL alignment of novel A. gambiae calreticulin (An gambiae Calr, gi 18389888), Amblyomma americanum calreticulin (Am america Calr, gi 3924593), and D. melanogaster calreticulin (Dr melanog Calr, gi 7299219). Similar amino acid residues are marked with a gray background, identical amino acids with a black background.

View larger version (20K): [in a new window]   Fig. 5. CLUSTAL alignment of novel A. gambiae selenoprotein (An gambiae seleno; gi 18389880) and D. melanogaster (Dr melanog seleno, gi 7293955). Similar amino acid residues are marked with a gray background, identical amino acids with a black background.

View larger version (97K): [in a new window]   Fig. 6. CLUSTAL alignment of novel A. gambiae antigen 5-related proteins (An gambiae A5 rel 1, gi 18389882; An gambiae A5 rel 2, gi 18389884; and An gambiae A5 rel 3, gi 18389886) and G. morsitans antigen 5 (Gl morsita A5, gi 8927462), D. melanogaster antigen 5 (Dr melanog A5, gi 7292977), and L. longipalpis antigen 5 (Lu longipa A5, gi 4887102). Similar amino acid residues are marked with a gray background, identical amino acids with a black background.

View larger version (31K): [in a new window]   Fig. 7. CLUSTAL alignment of novel A. gambiae 30 kDa protein (An gambiae 30 kDa; gi 18389878) and A. aegypti (Ae aegypti 30 kDa, gi 2114497). Similar amino acid residues are marked with a gray background, identical amino acids with a black background.

View larger version (15K): [in a new window]   Fig. 8. CLUSTAL alignment of novel A. gambiae long D7 protein (An gambiae D7 rela 1; gi 18389890) and A. aegypti long D7 (Ae aegypti D7 rela2, gi 159559). Similar amino acid residues are marked with a gray background, identical amino acids with a black background.