Complete primary structure of a galactose-specific lectin from the venom of the rattlesnake Crotalus atrox. Homologies with Ca2(+)-dependent-type lectins

Hirabayashi, Jun; Kusunoki, Takahiro; Kasai, Ken‐ichi

doi:10.1016/s0021-9258(18)52246-8

Cited by 88 publications

(16 citation statements)

References 42 publications

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“…High-affinity interaction of the human hepatic lectin with galactose was shown to require a Trp residue close to the Ca 2+ /carbohydrate-binding site (23). Human proteoglycan core protein and rattlesnake C-type lectin contain Phe and Tyr, respectively, in similar positions (23,26). The human hepatic lectin also contains a Gly-rich loop that holds the Trp in position for packing with galactose and also excludes mannose from the binding site (27), and this loop is missing in the herring AFP (Figure 5).…”

Section: Discussionmentioning

confidence: 99%

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The Ice-Binding Site of Atlantic Herring Antifreeze Protein Corresponds to the Carbohydrate-Binding Site of C-Type Lectins

Ewart

Yang

et al. 1998

Biochemistry

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The type II antifreeze proteins (AFPs) of smelt and Atlantic herring are homologous to the carbohydrate-recognition domains (CRDs) of Ca2+-dependent (C-type) animal lectins and, like these lectins, acquire a stable and active structure upon binding Ca2+ ions. In the C-type lectin CRD, the carbohydrate-binding site is located at a Ca2+-binding site. Site-directed mutagenesis was used to test the hypothesis that the ice-binding site of the type II AFP corresponds to the carbohydrate-binding site of the lectins. To disrupt this site in the herring AFP without perturbing the Ca2+-dependent protein fold, a double mutant was constructed that changed the Ca2+- and carbohydrate-binding motif from the galactose-type of wild-type AFP containing the sequence Gln-Pro-Asp to a mannose-type that has the sequence Glu-Pro-Asn and is also known to bind Ca2+. The mutant AFP exhibited proper Ca2+ binding, folding, and stability as demonstrated by ruthenium red staining, proteolysis protection assays, and CD spectroscopy. However, it showed no antifreeze activity (thermal hysteresis) and did not alter ice crystal morphology to form bipyramidal crystals as does the active wild-type AFP. These results demonstrate that the ice-binding site of the herring type II AFP corresponds to the carbohydrate-binding site of the C-type lectin CRDs and further suggest that this ice-binding function evolved from the carbohydrate-binding site of a preexisting C-type lectin.

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Section: Discussionmentioning

confidence: 99%

“…The positions of aromatic residues that may stack with galactose are indicated by asterisks, and the Gly residues of the Gly-rich loop of the hepatic lectins are indicated by circumflexes. Sequences are hafpl, herring AFP (11); rsl, rattlesnake lectin (26); cpgcp, cartilage proteoglycan core protein (29); and rhep1, rat hepatic lectin (30).…”

Section: Discussionmentioning

confidence: 99%

The Ice-Binding Site of Atlantic Herring Antifreeze Protein Corresponds to the Carbohydrate-Binding Site of C-Type Lectins

Ewart

Yang

et al. 1998

Biochemistry

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“…While snake venom is known to contain C-type lectins such as Crotalus atrox lectin (7) and Lachesis muta stenophyrs lectin (8), homodimers of a Ca 2+ -dependent carbohydrate recognition domain, many C-type lectin-like heterodimers with various functions have been isolated from Crotalinae and Viperinae snake venom. For example, botrocetin (9), bothrojaracin (10), jararaca GPIb-bp (11), and jararaca IX/X-bp (12) were obtained from the venom of Bothrops jararaca.…”

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confidence: 99%

Coagulation Factor X-Binding Protein from Deinagkistrodon acutus Venom Is a Gla Domain-Binding Protein

et al. 1998

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Factor IX/factor X-binding protein (IX/X-bp) is an anticoagulant isolated from the venom of Trimeresurus flavoviridis (habu snake) and binds predominantly to factor IX. In this study, we isolated IX/X-bp-like proteins from the venom of Deinagkistrodon acutus (hundred pace snake) with binding characteristics different from those of IX/X-bp. The complete amino acid sequence and binding characteristics of the main anticoagulant protein, named X-bp, were investigated. The concentrations of X-bp at half-maximal binding to solid-phase factors X and IX were 0.4 and 3 nM, respectively. The binding of X-bp to solid-phase factor X was inhibited by 50% by 6- and 9-fold excess concentrations of factor X and Gla domain (GD) peptide 1-44, respectively, but was not influenced by GD peptide 1-41 and Gla domainless factor X. X-bp bound two Ca2+ ions per molecule with Kd values of 16 +/- 0.7 (mean +/- SE, n = 6) and 103 +/- 10 microM. X-bp was a heterodimer of C-type lectin-like subunits. The 16 kDa chain (A chain) consisted of 129 amino acid residues and was 68% identical to the sequence of the A chain of IX/X-bp. The 15 kDa chain (B chain) consisted of 123 amino acid residues and was 87% identical to IX/X-bp. Three-dimensional model construction from the known fold of IX/X-bp showed that amino acid residues different from those of IX/X-bp are mostly on the molecular surface. Some of these are concentrated on a part of the concave surface which is considered to be the coagulation factor-binding site, presumably acting as a discriminator for ligand binding. These results indicated that X-bp isolated from D. acutus venom was a GD-binding protein, and the C-terminal region of GD peptide was critical for folding of the peptide.

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“…Toxins in snake venoms that affect the coagulation system exhibit considerable heterogeneity in terms of function as well as molecular structure (Tu, 1977; Pirkle & Markland, 1987). Recently, there have been several reports of a novel class of toxins that include the structure of the carbohydraterecognition domain of C-type lectins; these toxins include botrocetin (Usami et al, 1993), Crotalus atrox lectin (Hirabayashi et al, 1991), and RVV-X (Takeyaetal., 1992), and habu IX/X-bp also belongs to this group (Atoda et al, 1991). Botrocetin is a well-known toxin, found in the venom of B. jararaca, that has been used to study interactions between vWF and platelets (Read et al, 1978(Read et al, ,1989Fujimura et al, 1987;Andrews et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Isolation and characterization of an anticoagulant protein homologous to botrocetin from the venom of Bothrops jararaca

Sekiya

Atoda²,

Morita³

1993

Biochemistry

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We previously isolated a unique anticoagulant protein named IX/X-bp (factor IX/factor X-binding protein) from the venom of the habu snake Trimeresurus flavoviridis. We recently determined its primary structure and found that this protein had a structure homologous to the carbohydrate-recognition domains of C-type lectins. Most interestingly, a high homology was found between this protein and botrocetin, an inducer of platelet agglutination found in the venom of the jararaca snake Bothrops jararaca. To examine the possible identity of these proteins, we searched for IX/X-bp-like protein(s) in the venom of B. jararaca. When the venom was subjected to DEAE anion-exchange chromatography, such an activity was eluted separately from that of botrocetin. This activity was purified to homogeneity and designated jararaca IX/X-bp. Jararaca IX/X-bp was a disulfide-linked heterodimer consisting of 16- and 15-kDa subunits, being structurally similar to botrocetin. The respective NH2-terminal amino acid sequences were also very similar. Jararaca IX/X-bp had no botrocetin-like activity. However, this protein did have an activity to bind to factors IX and X and protein S in a Ca(2+)-dependent fashion, that resulted in interference with coagulation, while botrocetin did not. The binding to coagulation factors appeared not to be mediated by the lectin-like activity of jararaca IX/X-bp, because a derivative of factor X free of carbohydrates retained the ability to bind. It is concluded, therefore, that the two proteins isolated from the same venom have different biological activities despite the high degree of structural similarity between them.

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Complete primary structure of a galactose-specific lectin from the venom of the rattlesnake Crotalus atrox. Homologies with Ca2(+)-dependent-type lectins

Cited by 88 publications

References 42 publications

The Ice-Binding Site of Atlantic Herring Antifreeze Protein Corresponds to the Carbohydrate-Binding Site of C-Type Lectins

The Ice-Binding Site of Atlantic Herring Antifreeze Protein Corresponds to the Carbohydrate-Binding Site of C-Type Lectins

Coagulation Factor X-Binding Protein from Deinagkistrodon acutus Venom Is a Gla Domain-Binding Protein

Isolation and characterization of an anticoagulant protein homologous to botrocetin from the venom of Bothrops jararaca

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