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First published online September 15, 2004
Journal of Experimental Biology 207, 3717-3729 (2004)
Published by The Company of Biologists 2004
doi: 10.1242/jeb.01185

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Identification of the most abundant secreted proteins from the salivary glands of the sand fly Lutzomyia longipalpis, vector of Leishmania chagasi

Jesus G. Valenzuela^1,*, Mark Garfield², Edgar D. Rowton³ and Van M. Pham¹

¹ Vector Molecular Biology Unit, Laboratory of Malaria and Vector Research, NIAID, National Institutes of Health, 12735 Twinbrook Parkway, Room 2E-22C, Rockville, MD 20852, USA,
² Structural Biology Unit, NIAID, Rockville, MD 20852, USA
³ Department of Entomology, Walter Reed Army Institute of Research, Washington, DC 20307, USA

View larger version (58K): [in a new window]   Fig. 1. Proteome analysis of Lutzomyia longipalpis salivary proteins. Salivary proteins were separated by SDS-PAGE and transferred to PVDF membrane as described in the Materials and methods section. N-terminal sequences are annotated on the left, and their corresponding cDNAs are annotated on the right.

View larger version (57K): [in a new window]   Fig. 2. (A) ClustalW analysis of yellow-related proteins from different Diptera, including Phlebotomus papatasi salivary proteins, Aedes aegypti dopachrome converting enzyme, Anopheles gambiae and the three yellow-related proteins found in the salivary gland cDNA library of Lutzomyia longipalpis. Reverse-shaded amino acids represent identical amino acids among all these proteins; gray-shaded amino acids represent identical amino acids among phlebotomine yellow-related proteins. (B) Dendrogram of the yellow-related proteins indicating the distribution of three distinct clades. Bootstrap values are indicated in their respective nodes.

View larger version (58K): [in a new window]   Fig. 3. Small proteins and peptides of novel sequences present in the salivary glands of the sand fly Lutzomyia longipalpis. Protein sequences represent the translation of their corresponding cDNAs. The signal secretory peptide is underlined. Amino acids of mature peptides are in bold. N-terminus peptides observed in proteomics analysis that differ from predicted SignalP programs are highlighted in gray.

View larger version (44K): [in a new window]   Fig. 4. (A) ClustalW analysis of the six C-type lectin proteins found expressed in the salivary glands of Lutzomyia longipalpis. (B) ClustalW analysis of C-type lectin-related proteins from various organisms, including insects and a mammal. Reverse-shaded amino acids indicate identical amino acids among all these proteins; gray-shaded amino acids represent highly conserved amino acids. (C) Dendrogram of the C-type lectin-related proteins from Lu. longipalpis and other organisms. Bootstrap values are indicated in their respective nodes.

View larger version (30K): [in a new window]   Fig. 5. Predicted protein sequence from the cDNA of cluster 20 (LJL04). Reverse-shaded amino acids and gray-shaded amino acids represent the repeats found in this protein. Bolded amino acids represent a putative signal secretory peptide.

View larger version (84K): [in a new window]   Fig. 6. ClustalW alignment of angiotensin converting enzyme-related proteins from different organisms, including Lutzomyia longipalpis, Anopheles gambiae, Drosophila melanogaster, chicken and human. Reverse-shaded amino acids represent identical amino acids among all these proteins.

View larger version (93K): [in a new window]   Fig. 7. ClustalW alignment of serpin-related proteins from different organisms, including Lutzomyia longipalpis, Manduca sexta, Anopheles gambiae, Drosophila melanogaster, cat flea, mouse and human. Reverse-shaded amino acids represent identical amino acids among all these proteins. Gray-shaded amino acids represent highly conserved amino acids.

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