Purification and properties of the hemoglobins of the platyhelminth Isoparorchis hypselobagri (trematoda: Isoparorchidae) and its host Wallagu attu (catfish)

Rashid, K.A.; Haque, Mohammad Imdadul; Siddiqi, Ather H.; Stern, Mary S.; Sharma, Pawan K.; Vinogradov, S.N.; Walz, Daniel A.

doi:10.1016/0305-0491(93)90063-b

Cited by 6 publications

(8 citation statements)

References 19 publications

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“…The invariance of the n ‐value with pH (Fig. 2) indicate the absence of aggregation phenomena, and accords with earlier studies showing the monomeric nature of the trematode Hbs [5,7,14], although time‐bound aggregation has been observed in stored Hbs of Pe [9], Isoparorchis hypselobagri ( Ih ) [7,9] and Gc (unpublished results).…”

Section: Discussionsupporting

confidence: 91%

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Functional differentiation in trematode hemoglobin isoforms

Rashid

Weber

1999

European Journal of Biochemistry

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The Hbs and the major electrophoretic Hb components (isoHbs) were isolated from three species of the trematodes, Explanatum explanatum (Ee), Gastrothylax crumenifer (Gc) and Paramphistomum epiclitum (Pe), that parasitise the common Indian water buffalo Bubalus bubalis.The Hbs are monomeric and resemble the so-called nonfunctional mutant hemoglobins that have Tyr at B10 or E7 positions (replacing Leu and the His residues, respectively). However, they are capable of binding with O 2 and CO.O 2 equilibrium studies of trematode Hb isoforms reveal extremely high O 2 affinities, with half-saturation O 2 tension (P 50 ) values up to 800 times lower than those of human hemoglobins. This correlates with Tyr residues at B10 and at the distal position (E7) that decrease the O 2 dissociation rate by contributing hydrogen bonds (H-bonds) to the bound O 2 . These substitutions also increase the O 2 association rates either due to orientation of E7-Tyr towards the solvent and/or by sterically hindering the entry of water molecules into the heme pocket. The latter may account for the low rate of autoxidation of trematode Hbs.The Hbs and their isoforms from different species exhibited pronounced variation in O 2 affinity, which may relate to subtle differences in the structure of the heme pocket. The O 2 affinities of the composite (unfractionated) Hbs were intermediate to those of the individual Hb isoform.The P [9,13,14]. Other O 2 avid Hb molecules achieve high affinity either by decreasing the O 2 dissociation rates through additional stabilization of the heme-O 2 complex as in the nematode Ascaris [15±17] or by increasing the O 2 association rates, which in the Hb from root nodules of leguminous plants (legHb) correlates with a large heme pocket [18].The high O 2 affinity of trematode, Ascaris and plants Hbs might not provide for efficient release of O 2 , whereby the function of these pigments remains speculative.Trematode Hbs seem to achieve high O 2 affinity by a novel mechanism of combining slow O 2 dissociation, probably by a mechanism similar to the Ascaris, with fast O 2 association [9]. The molecular basis for the fast O 2 association in trematode Hbs is still unknown.Recent research has focused on the effects of specific amino acid exchanges in the environment of the heme pocket of naturally occurring or engineered mutants on their functional characteristics. Several amino acids in the heme pocket of Hb Correspondance to Roy E. Weber, Danish Center for Respiratory Adaptation, Department of Zoophysiology, Institute of Biological Sciences, University of Aarhus, DK-8000, Aarhus C, Denmark. Fax: + 45 86194186. Tel: + 45 89422599. E-mail: Roy.Weber@biology.aau.dk Abbreviations: Dd, Dicrocoelium dendriticum; Ih, Isoparorchis hypselobagri; Ee, Explanatum explanatum; Gc, Gastrothylax crumenifer; Pe, Paramphistomum epiclitum; H-bond, hydrogen bond; isoHbs, isoforms of hemoglobins; legHb, hemoglobin from root nodules of leguminous plants; M-value, partition coefficient (ratio of binding constant of the heme pigment for CO an...

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Section: Discussionsupporting

confidence: 91%

“…Because trematodes lead a parasitic mode of life and feed upon the tissues and blood of their vertebrate hosts [2,3] their Hb was originally thought to derive from the host [4]. Biochemical studies [5–9] however, have shown that trematodes are capable of synthesizing Hb.…”

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confidence: 99%

Functional differentiation in trematode hemoglobin isoforms

Rashid

Weber

1999

European Journal of Biochemistry

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“…Trematodes possess a cytoplasmic oxygen-binding hemoprotein distributed throughout the body (Rashid et al 1993(Rashid et al , 1997. The immunolocalization of recombinant C. sinensis myoglobin in adult worms, in this study, shows that myoglobin is well distributed in C. sinensis.…”

Section: Discussionmentioning

confidence: 99%

Cloning and characterization of Clonorchis sinensis myoglobin using immune sera against excretory?secretory antigens

Sim

Park

Yong

2003

Parasitology Research

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Clonorchis sinensis excretory-secretory (ES) antigens were separated by gradient SDS-PAGE and the antigenic protein isolated at 21 kDa was injected into rats. A C. sinensis cDNA library was then immunoscreened with sera from the 21-kDa antigenic protein-immunized rats. The selected genes, which were named C. sinensis myoglobin, contained a single open reading frame of 450 base pairs encoding 150 amino acids. A single hybridized band of 0.57 kb and two to four hybridized bands were detected by Northern and Southern blotting. Purified recombinant C. sinensis myoglobin was recognized by clonorchiasic rabbit sera (50%) and clonorchiasic human sera (25%). An indirect immunofluorescence assay showed that C. sinensis myoglobin is distributed over the whole body of the adult worm. It is believed that the abundance of C. sinensis myoglobin plays an important role as an oxygen reservoir under anaerobic conditions.

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“…After Wharton's discovery in 1938 of Hb in Cercorchis robustus that parasitizes turtles (656), Hb has been recorded in a large number of trematodes from a diverse range of vertebrate and invertebrate hosts (e.g., Isoparorchis hypselobagri from the swim bladder of the catfish Wallago attu, Explanatum explanatum, Paramphistomum epiclitum, and Gastrothylax crumenifer from the rumen and bile ducts of Indian buffalo Bubalus bubalis, Gastrodiscoides hominis from pig caeca, Notocotylus triserialis from duck digestive caeca, Dicrocoelium dendriticum from sheep liver, and Paravortex scrobiculariae and Proctoeces subtenuis from the intestine and kidney, respectively, of the estuarine bivalve Scrobicularia plana) (218,349,432). The major forms of platyhelminth Hbs appear always to be monomeric (73,444,500), and disulfide-bonded dimer formation may be time dependent, as observed with Isoparorchis hypselobagri Hb (444).…”

Section: Platyhelminthsmentioning

confidence: 99%

Nonvertebrate Hemoglobins: Functions and Molecular Adaptations

Weber

Vinogradov

2001

Physiological Reviews

452

404

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Hemoglobin (Hb) occurs in all the kingdoms of living organisms. Its distribution is episodic among the nonvertebrate groups in contrast to vertebrates. Nonvertebrate Hbs range from single-chain globins found in bacteria, algae, protozoa, and plants to large, multisubunit, multidomain Hbs found in nematodes, molluscs and crustaceans, and the giant annelid and vestimentiferan Hbs comprised of globin and nonglobin subunits. Chimeric hemoglobins have been found recently in bacteria and fungi. Hb occurs intracellularly in specific tissues and in circulating red blood cells (RBCs) and freely dissolved in various body fluids. In addition to transporting and storing O(2) and facilitating its diffusion, several novel Hb functions have emerged, including control of nitric oxide (NO) levels in microorganisms, use of NO to control the level of O(2) in nematodes, binding and transport of sulfide in endosymbiont-harboring species and protection against sulfide, scavenging of O(2 )in symbiotic leguminous plants, O(2 )sensing in bacteria and archaebacteria, and dehaloperoxidase activity useful in detoxification of chlorinated materials. This review focuses on the extensive variation in the functional properties of nonvertebrate Hbs, their O(2 )binding affinities, their homotropic interactions (cooperativity), and the sensitivities of these parameters to temperature and heterotropic effectors such as protons and cations. Whenever possible, it attempts to relate the ligand binding properties to the known molecular structures. The divergent and convergent evolutionary trends evident in the structures and functions of nonvertebrate Hbs appear to be adaptive in extending the inhabitable environment available to Hb-containing organisms.

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Purification and properties of the hemoglobins of the platyhelminth Isoparorchis hypselobagri (trematoda: Isoparorchidae) and its host Wallagu attu (catfish)

Cited by 6 publications

References 19 publications

Functional differentiation in trematode hemoglobin isoforms

Functional differentiation in trematode hemoglobin isoforms

Cloning and characterization of Clonorchis sinensis myoglobin using immune sera against excretory?secretory antigens

Nonvertebrate Hemoglobins: Functions and Molecular Adaptations

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