spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    

This Article
Right arrow Summary Freely available
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Valenzuela, J. G.
Right arrow Articles by Ribeiro, J. M. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Valenzuela, J. G.
Right arrow Articles by Ribeiro, J. M. C.

Exploring the sialome of the tick Ixodes scapularis

Jesus G. Valenzuela1, Ivo M. B. Francischetti1, Van My Pham1, Mark K. Garfield2, Thomas N. Mather3 and José M. C. Ribeiro1,*

1 Medical Entomology Section, Laboratory of Parasitic Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda Maryland, 20892-0425, USA
2 Research Technologies Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA
3 Center for Vector-Borne Disease, University of Rhode Island, Kingston 02881-0804, USA



View larger version (104K):

[in a new window]
  		Fig. 1. (A) Alignment of related peptides, group 1 (Table 3) deduced from an Ixodes scapularis salivary gland cDNA library. Gray background, predicted signal secretory peptide as indicated by the SignalP program. Cysteine residues are shown white over a black background. Other conserved amino acid residues are shown in bold over a gray background. Asterisks, colons or stops below the sequences indicate identity, high conservation and conservation of the amino acids, respectively. (B) Unrooted cladogram indicating the three families HDC, ETC and HNC, named for their mature peptide amino-terminal sequence. The bar represents the degree of divergence among sequences.

 


View larger version (80K):

[in a new window]
  		Fig. 2. (A) Alignment of group 2 peptides (Table 3). See Fig. 1A legend for an explanation of the layout. (B) The alignment in A was used to build a hidden Markov model that retrieved the shown sequences when searched against the non-redundant NCBI protein database.

 


View larger version (48K):

[in a new window]
  		Fig. 3. (A) Alignment of group 3 peptides (Table 3). See Fig. 1A legend for an explanation of the layout. (B) The unrooted cladogram of all sequences. The bar represents the degree of divergence among sequences.

 


View larger version (54K):

[in a new window]
  		Fig. 4. (A) Alignment of group 4 peptides (Table 3). See Fig. 1A legend for an explanation of the layout. The SALP10 peptide from the NR protein database is added for comparison. (B) The unrooted cladogram of all sequences. The bar represents the degree of divergence among sequences.

 


View larger version (65K):

[in a new window]
  		Fig. 5. Alignment of group 5 peptides (Table 3). See Fig. 1A legend for an explanation of the layout.

 


View larger version (43K):

[in a new window]
  		Fig. 6. Alignment of group 6 peptides (Table 3). See Fig. 1A legend for an explanation of the layout.

 


View larger version (28K):

[in a new window]
  		Fig. 7. Alignment of group 7 peptides (Table 3). See Fig. 1A legend for an explanation of the layout. The Ixodes scapularis salivary peptide annotated as a thrombospodin from the NR protein database is added for comparison.

 


View larger version (60K):

[in a new window]
  		Fig. 8. Alignment of ISL1083_cluster9 with three other putative proteins from the salivary glands of Ixodes scapularis. See Fig. 1A legend for an explanation of the layout.

 


View larger version (32K):

[in a new window]
  		Fig. 9. Clustal alignment of ISTA397_cluster168 with Ixolaris, the TFPI of Ixodes scapularis. See Fig. 1A legend for an explanation of the layout.

 


View larger version (24K):

[in a new window]
  		Fig. 10. Lack of GPI anchor motif in ISL1194_5nuc: alignments of I. scapularis 5'-nucleotidase with rat, mouse (Mus), human (Homo), bovine (bos), and Boophilus tick 5'-nucleotidase. Identical residues in five or more sequences are bold with gray background. Similar polar or hydrophobic amino acids are shown with gray background. The arrow indicates the conserved serine residue involved in the GPI anchor of 5'-nucleotidases. The box shows the hydrophobic carboxyterminal region, which penetrates the cell membrane. Green background in the box indicates hydrophobic amino acid residues.

 


View larger version (42K):

[in a new window]
  		Fig. 11. Edman degradation of protein bands from Ixodes scapularis saliva and their corresponding gene products. Numbers at left indicate the position of the molecular mass markers (kDa).

 


View larger version (45K):

[in a new window]
  		Fig. 12. Edman degradation of protein bands from Ixodes scapularis salivary gland homogenates, and their corresponding gene products. Numbers at left indicate the position of the molecular mass markers (kDa).

 


View larger version (50K):

[in a new window]
  		Fig. 13. Clustal alignments of dendrotoxins and short peptides from Ixodes scapularis group 2 peptides deduced from a salivary gland cDNA library. Regions of positive charge (Pos) are shown by bars. Gly, glycine-rich region. Conserved cysteine residues are shown in black background; other conserved residues are in gray background.

 




© The Company of Biologists Ltd 2002