Identification of putative proteins involved in granule biogenesis of tick salivary glands

Mans, Ben J.; Venter, Jacobus D.; Vrey, Pieter Jakobus; Louw, Abraham I.; Neitz, A.W.H.

doi:10.1002/1522-2683(200105)22:9<1739::aid-elps1739>3.0.co;2-7

Cited by 35 publications

(51 citation statements)

References 31 publications

(35 reference statements)

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“…It's closest known relatives (Fig. 3) are TSGP2 and TSGP3 of the soft tick O. savignyi (29) and collagen-dependent platelet aggregation inhibitor, moubatin (28). However, the four closely migrating HPLC peaks and N-terminal sequence of peak C (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Neither moubatin or the TSGP proteins have been proposed to inhibit C. TSGP2 and TSGP3 are abundant in SGE, have 95% amino acid identity (29), and unlike moubatin do not inhibit platelet aggregation (31). TSGP2 is toxic to mice but TSGP3 is not (34).…”

Section: Discussionmentioning

confidence: 99%

“…The primary sequence of OmCI has no detectable sequence similarity to any known C inhibitors in public databases. However, it does have a 58% amino acid identity to tick salivary gland proteins 2 and 3 (TSGP2 and TSGP3) of the soft tick Ornithodorus savignyi (29) and a 49% identity to moubatin from O. moubata (28). Multiple sequence alignment indicates that all six cysteine residues, and therefore presumably the disulfide-bridging pattern, is conserved in these four proteins (Fig.…”

Section: Primary Structure Of Omcimentioning

confidence: 99%

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Complement Inhibitor of C5 Activation from the Soft Tick Ornithodoros moubata

Nunn

Sharma

Paesen

et al. 2005

The Journal of Immunology

206

186

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Blood-feeding ticks must control C activation or be damaged by the host inflammatory response. We report the characterization and expression of a novel, relatively small, broad-acting C inhibitory protein (termed OmCI) from the soft tick Ornithodoros moubata. The native 17-kDa nonglycosylated protein inhibits both human and guinea pig classical and alternative C activation pathways. The IC50 values for each pathway were 12 and 27 nM, respectively, in hemolytic assays using human serum diluted 40-fold. The cDNA encodes a protein of 168 aa, including an 18-aa secretion signal sequence that is absent in the mature form. The inhibitor has 46% amino acid identity with moubatin, a platelet aggregation inhibitor also from O. moubata that is an outlying member of the lipocalin family. Native OmCI had no inhibitory effect on the addition of C8 and C9 to preformed C5b-C7 and C5b-C8 to form the membrane attack complex and no effect on the rate of C3a production by the C3 convertase enzymes C4bC2a, C3(H2O)Bb, or C3bBb. Both recombinant and native OmCI abolish production of C5a by human classical (C4bC3bC2a) and alternative (C3bC3bBb) C5 convertases. Addition of excess C5 but not C3 competes away the inhibitory activity of OmCI, indicating that OmCI targets C5 itself rather than inhibiting the C5 convertase C4bC3bC2a itself. Direct binding of OmCI to C5 was demonstrated by Western blotting and gel filtration chromatography using 125I-labeled proteins. OmCI is the first lipocalin family member shown to inhibit C and also the first natural inhibitor that specifically targets the C5 activation step.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Primary Structure Of Omcimentioning

confidence: 99%

See 1 more Smart Citation

Complement Inhibitor of C5 Activation from the Soft Tick Ornithodoros moubata

Nunn

Sharma

Paesen

et al. 2005

The Journal of Immunology

206

186

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“…1) contains the most abundantly expressed lipocalins in O. parkeri salivary glands and groups with TSGP1 a protein previously described for O. savignyi (Mans et al, 2003;Mans et al, 2001). These are good candidates for containing histamine/serotonin binding proteins because physiologically active concentrations of histamine and serotonin are near 1 μM concentrations, needing relatively large amounts of protein to sequester these biologically active amines.…”

Section: Putative Salivary Secreted Proteins Having Ubiquitous Domainmentioning

confidence: 99%

“…This salivary lipocalin may have been recruited to some granule biogenesis function specific to salivary gland function (Mans and Neitz, 2004c;Mans et al, 2001). …”

Section: Housekeeping Proteinsmentioning

confidence: 99%

An insight into the sialome of the soft tick, Ornithodorus parkeri

Francischetti¹,

Mans²,

Meng

et al. 2008

Insect Biochemistry and Molecular Biology

Self Cite

103

104

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While hard ticks (Ixodidae) take several days to feed on their hosts, soft ticks (Argasidae) feed faster, usually taking less than one hour per meal. Saliva assists in the feeding process by providing a cocktail of anti-hemostatic, anti-inflammatory and immunomodullatory compounds. Saliva of hard ticks has been shown to contain several families of genes each having multiple members, while those of soft ticks are relatively unexplored.Analysis of the salivary transcriptome of the soft tick Ornithodorus parkeri, the vector of the relapsing fever agent Borrelia parkeri, indicates that gene duplication events have led to a large expansion of the lipocalin family, as well as of several genes containing Kunitz domains indicative of serine protease inhibitors, and several other gene families also found in hard ticks. Novel protein families with sequence homology to insulin growth factor-binding protein (prostacyclin-stimulating factor), adrenomedulin, serum amyloid A protein precursor and similar to HIV envelope protein were also characterized for the first time in the salivary gland of a blood-sucking arthropod.The sialotranscriptome of O. parkeri confirms that gene duplication events are an important driving force in the creation of salivary cocktails of blood-feeding arthropods, as was observed with hard ticks and mosquitoes. Most of the genes coding for expanded families are homologous to those found in hard ticks, indicating a strong common evolutionary path between the two families. As happens to all genera of blood-sucking arthropods, several new proteins were also found, indicating the process of adaptation to blood feeding still continues to recent times.

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Savicalin, a lipocalin from hemocytes of the soft tick, Ornithodoros savignyi

et al. 2010

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Savicalin, is a lipocalin found in the hemocytes of the soft tick, Ornithodoros savignyi. It could be assigned to the tick lipocalin family based on BLAST analysis. Savicalin is the first non-salivary gland lipocalin described in ticks. The mature sequence is composed of 188 amino acids with a molecular mass of 21481.9 Da. A homolog for savicalin was found in a whole body EST-library from a related soft tick O. porcinus, while other tick salivary gland derived lipocalins retrieved from the non-redundant sequence database are more distantly related. Homology modeling supports the inclusion of savicalin into the lipocalin family. The model as well as multiple alignments suggests the presence of five disulphide bonds. Two conserved disulphide bonds are found in hard and soft tick lipocalins. A third disulphide bond is shared with the TSGP4-clade of leukotriene C4 binding soft tick lipocalins and a fourth is shared with a lipocalin from the hard tick Ixodes scapularis. The fifth disulphide bond is unique and links  strands D-E. Phylogenetic analysis showed that savicalin is a distant relative of salivary gland derived lipocalins, but groups within a clade that is possibly non-salivary gland derived. It lacks the biogenic amine-binding motif associated with tick histamine and serotonin binding proteins. Expression profiles indicate that savicalin is found in hemocytes, midgut and ovaries, but not in the salivary glands. Up-regulation occurs in hemocytes after bacterial challenge and in midguts and ovaries after feeding. Given its tissue distribution and upregulation of expression, it is possible that this lipocalin functions in tick development after feeding or in an anti-microbial capacity.

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Identification of putative proteins involved in granule biogenesis of tick salivary glands

Cited by 35 publications

References 31 publications

Complement Inhibitor of C5 Activation from the Soft Tick Ornithodoros moubata

Complement Inhibitor of C5 Activation from the Soft Tick Ornithodoros moubata

An insight into the sialome of the soft tick, Ornithodorus parkeri

Savicalin, a lipocalin from hemocytes of the soft tick, Ornithodoros savignyi

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