The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: The primary structure

Babin, Donald R.; Peanasky, Robert J.; Goos, Susan M.

doi:10.1016/0003-9861(84)90530-7

Cited by 51 publications

(42 citation statements)

References 17 publications

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“…The site of cleavage of the signal peptide was predicted using the SignalP computer software program (13). An initial BLAST search confirmed amino acid sequence homology to other members of the Ascaris family of serine protease inhibitors (7,8), including the AcAP5 and AcAPc2 anticoagulants from A. caninum (6,17) (Fig. 2).…”

Section: Resultsmentioning

confidence: 92%

“…The 40 -44% amino acid sequence identity (52-55% similarity) to the two AcAP sequences, in addition to the conservation and alignment of the 10 cysteine residues, which are known to play a critical role in defining the tertiary molecular structure of the Ascaris type inhibitors (9,33,34), suggests that AceAP1 is, in fact, a member of this family of nematode proteins. In addition to those from Ancylostoma hookworms, Ascaris-type inhibitors have also been identified other nematode species, including A. suum (7,8), Anisakis simplex (35), and Trichuris muris (36). In contrast to the hookworm anticoagulants, the Ascaris inhibitors from these non-bloodfeeding nematodes have been found to inhibit primarily intestinal serine proteases.…”

Section: Discussionmentioning

confidence: 99%

“…One of these, A. caninum anticoagulant peptide 5 (AcAP5), 1 is a potent and specific inhibitor of coagulation factor Xa, whereas the second, AcAPc2, blocks the activity of factor VIIa in complex with membrane-bound tissue factor (5,6). Both of these hookworm proteins are members of a family of related serine protease inhibitors first identified in the non-bloodfeeding intestinal nematode Ascaris suum (7)(8)(9).…”

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confidence: 99%

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Molecular Characterization of Ancylostoma Inhibitors of Coagulation Factor Xa

Harrison

Nerlinger

Bungiro

et al. 2002

Journal of Biological Chemistry

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Bloodfeeding hookworms, which currently infect over a billion people in the developing world, are a leading cause of gastrointestinal hemorrhage and iron deficiency anemia. The major anticoagulant inhibitor of coagulation factor Xa has been identified from the hookworm parasite Ancylostoma ceylanicum using reverse transcription PCR and 3-rapid amplification of cDNA ends. This is the first anticoagulant cloned from a hookworm species for which humans are recognized permissive hosts. Despite ϳ50% amino acid similarity, A. ceylanicum anticoagulant peptide 1 (AceAP1) is both immunologically and mechanistically distinct from AcAP5, its homologue isolated from the dog hookworm Ancylostoma caninum. Studies using plasma clotting times and single stage chromogenic assays of factor Xa activity have demonstrated that the recombinant AceAP1 protein is substantially less potent than AcAP5 and that soluble whole worm protein extracts of adult A. ceylanicum possess less anticoagulant activity than extracts of A. caninum. These values correlate with previously reported differences in bloodfeeding capabilities between these two species of hookworm, suggesting that factor Xa inhibitory activity is predictive of hookworm bloodfeeding capabilities in vivo. These fundamental differences in the mechanism of action and immunoreactivity of the major anticoagulant virulence factors from related Ancylostoma hookworm species may have significant implications for human vaccine development.

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Section: Resultsmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Molecular Characterization of Ancylostoma Inhibitors of Coagulation Factor Xa

Harrison

Nerlinger

Bungiro

et al. 2002

Journal of Biological Chemistry

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“…Although an original 3' oligonucleotide primer was designed in order to amplify nematode serine protease inhibitors [17,21], the translated amino acid sequence of a partial cDNA was found to have homology to the CTL family of proteins, including members from both the free living nematode C. elegans and other parasitic species [4,30,34]. Using standard techniques, the full length cDNA corresponding to Ancylostoma ceylanicum C-type lectin 1 (AceCTL-1) was successfully amplified from adult hookworm RNA.…”

Section: Resultsmentioning

confidence: 99%

“…Total RNA was utilized as template in a reverse transcription reaction using previously described methods [16][17][18]. The first strand cDNA mixture was combined with PCR primers corresponding to the nematode spliced leader [19,20] and a conserved amino acid sequence previously identified in a family of nematode serine protease inhibitors [17,21]. Following amplification, resulting PCR products were ligated into the pCR 2.1 (Invitrogen) plasmid vector and One Shot E. coli INVαF' cells (Invitrogen) were transformed with the ligation product.…”

Section: Cloning Of the Acectl-1 Cdnamentioning

confidence: 99%

Molecular cloning and characterization of a C-type lectin from Ancylostoma ceylanicum: Evidence for a role in hookworm reproductive physiology

Brown

Harrison

Kapulkin

et al. 2007

Molecular and Biochemical Parasitology

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Lectins comprise a family of related proteins that mediate essential cell functions through binding to carbohydrates. Within this protein family, C-type lectins are defined by the requirement of calcium for optimal biologic activity. Using reverse transcription PCR, a cDNA corresponding to a putative C-type lectin has been amplified from the hookworm parasite Ancylostoma ceylanicum. The 550 nucleotide open reading frame of the Ancylostoma ceylanicum C-type Lectin-1 (AceCTL-1) cDNA corresponds to a 167 amino acid mature protein (18706 Da) preceded by a 17 amino acid secretory signal sequence. The recombinant protein (rAceCTL-1) was expressed in Drosophila S2 cells and purified using a combination of affinity chromatography and reverse phase HPLC. Using in vitro carbohydrate binding studies, it was determined that rAceCTL-1 binds N-acetyl-D-glucosamine, a common component of eukaryotic egg cell membranes. Using a polyclonal IgG raised against the recombinant protein, the native AceCTL-1 was identified in sperm and soluble protein extracts of adult male A. ceylanicum by immunoblot. Probing of adult hookworm sections with the polyclonal IgG demonstrated localization to the testes in males, as well as the spermatheca and developing embryos in females, consistent with its role as a sperm protein. Together, these data strongly suggest that AceCTL-1 is a male gender-specific C-type lectin with a function in hookworm reproductive physiology.

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Novel gene containing multiple epidermal growth factor-like motifs transiently expressed in the papillae of the ascidian tadpole larvae

et al. 1997

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We have investigated molecular mechanisms of the embryonic development of an ascidian, a primitive chordate which shares features of both invertebrates and vertebrates, with a view to identifying genes involved in development and metamorphosis. We isolated 12 partial cDNA sequences which were expressed in a stage‐specific manner using differential display. We report here the isolation of a full‐length cDNA sequence for one of these genes which was specifically expressed during the tailbud and larval stages of ascidian development. This cDNA, 1213 bp in length, is predicted to encode a protein of 337 amino acids containing four epidermal growth factor (EGF)–like repeats and three novel cysteine‐rich repeats. Characterization of its spatial expression pattern by in situ hybridisation in late tailbud and larval embryos demonstrated strong expression localised throughout the papillae and anteriormost trunk and weaker expression in the epidermis of the remainder of the embryo. As recent evidence indicates that the signal for metamorphosis originates in the anterior trunk region, these results suggest that this gene may have a role in signalling the initiation of metamorphosis. Dev. Dyn. 1997;210:264–273. © 1997 Wiley‐Liss, Inc.

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The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: The primary structure

Cited by 51 publications

References 17 publications

Molecular Characterization of Ancylostoma Inhibitors of Coagulation Factor Xa

Molecular Characterization of Ancylostoma Inhibitors of Coagulation Factor Xa

Molecular cloning and characterization of a C-type lectin from Ancylostoma ceylanicum: Evidence for a role in hookworm reproductive physiology

Novel gene containing multiple epidermal growth factor-like motifs transiently expressed in the papillae of the ascidian tadpole larvae

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