Molecular characterization and comparative study of 6 salivary gland metalloproteases from the hard tick, Haemaphysalis longicornis

Harnnoi, Thasaneeya; Sakaguchi, Takeshi; Nishikawa, Yoshifumi; Xuan, Xuenan; Fujisaki, Kozo

doi:10.1016/j.cbpb.2006.12.008

Cited by 39 publications

(34 citation statements)

References 29 publications

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“…These metalloproteases are also a common finding in snake venoms (Takeya et al, 1993). Recently, 6 such enzymes were characterized from the tick Haemaphysalis longicornis (Harnnoi et al, 2007). Supplemental file S2 presents evidence for the presence of such salivary enzyme in O. parkeri in the form of OP-new-266, a 249 AA fragment of such enzyme containing the HEXXH zinc-binding motif of the enzyme active site, in addition to high similarity to proteins in the NR database annotated as metalloproteases from both soft and hard ticks.…”

Section: Enzymesmentioning

confidence: 99%

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

Francischetti¹,

Mans²,

Meng

et al. 2008

Insect Biochemistry and Molecular Biology

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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Section: Enzymesmentioning

confidence: 99%

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

Francischetti¹,

Mans²,

Meng

et al. 2008

Insect Biochemistry and Molecular Biology

103

104

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“…Disintegrins bind to integrins and interfere with ligand binding, probably through competitive inhibition; the cysteine-rich domain of ADAM/ADAMTS serves to target the molecule to the substrates and facilitates enzymatic functions (53). Disintegrins in tick saliva inhibit platelet aggregation and are important for successful tick feeding (8,11,16). ISL 929 and ISL 1373 belong to the ixostatin family and have been proposed to be involved in angiogenesis and repair inhibition (44).…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Neutrophil Function by Two Tick Salivary Proteins

Guo¹,

Booth

Paley³

et al. 2009

Infect Immun

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“…HlSC-1 was identified from expressed sequence tags constructed from salivary glands cDNA libraries of H. longicornis as described previously (Harnnoi et al 2007). The plasmids containing HlSC-1 gene-encoding inserts were extracted using the Qiagen DNA purification kit (QIAGEN Sciences, Germantown, MA, USA).…”

Section: Methodsmentioning

confidence: 99%

“…Recently, with the examination of the H. longicornis salivary gland cDNA library (Harnnoi et al 2007), we have identified a novel cystatin-like homologue, named HlSC-1. The cDNA encoding the gene product was amplified from H. longicornis RNA by RT-PCR, subcloned, and sequenced.…”

Section: Hlsc-1 Encodes a Cystatin-like Homologue In H Longicornismentioning

confidence: 99%

A salivary cystatin, HlSC-1, from the ixodid tick Haemaphysalis longicornis play roles in the blood-feeding processes

et al. 2009

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Ticks feed exclusively on blood to obtain their nutrients, but the gene products that mediate blood-sucking processes in ticks are still unknown. We report here the molecular characterization and possible biological function of a cysteine protease inhibitor (HlSC-1) identified in the salivary gland of the ixodid tick Haemaphysalis longicornis. The HlSC-1 cDNA contains 423 bp that code for 140 amino acids with a predictable molecular weight of 12 kDa. The recombinant HlSC-1 expressed in Escherichia coli was shown to inhibit the activity of papain and cathepsin L, while cathepsin B activity was unaffected. Immunolocalization studies detected the endogenous enzyme in the salivary gland type II acini of an adult tick. Furthermore, quantitative RT-PCR analysis showed that the expression of HlSC-1 transcripts was associated with blood-feeding processes and was highly up-regulated in the early phase of feeding. Our results strongly suggest that HlSC-1 may play pivotal roles in the blood-feeding processes.

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Molecular characterization and comparative study of 6 salivary gland metalloproteases from the hard tick, Haemaphysalis longicornis

Cited by 39 publications

References 29 publications

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

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

Inhibition of Neutrophil Function by Two Tick Salivary Proteins

A salivary cystatin, HlSC-1, from the ixodid tick Haemaphysalis longicornis play roles in the blood-feeding processes

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