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Red blood with blue-blood ancestry: intriguing structure of a snail hemoglobin.

ABSTRACT: The phylogenetic enigma of snail hemoglobin, its isolated occurrence in a single gastropod family, the Planorbidae, and the lack of sequence data, stimulated the present study. We present here the complete cDNA and predicted amino acid sequence of two hemoglobin polypeptides from the planorbid Biomphalaria glabrata (intermediate host snail for the human parasite Schistosoma mansoni). Both isoforms contain 13 different, cysteine-free globin domains, plus a small N-terminal nonglobin "plug" domain with three cysteines for subunit dimerization (total M(r) approximately 238 kDa). We also identified the native hemoglobin molecule and present here a preliminary 3D reconstruction from electron microscopical images (3 nm resolution); it suggests a 3 x 2-mer quaternary structure (M(r) approximately 1.43 MDa). Moreover, we identified a previously undescribed rosette-like hemolymph protein that has been mistaken for hemoglobin. We also detected expression of an incomplete hemocyanin as trace component. The combined data show that B. glabrata hemoglobin evolved from pulmonate myoglobin, possibly to replace a less-efficient hemocyanin, and reveals a surprisingly simple evolutionary mechanism to create a high molecular mass respiratory protein from 78 similar globin domains.

SUBMITTER: Lieb B

PROVIDER: S-EPMC1567689 | biostudies-literature | 2006 Aug

REPOSITORIES: biostudies-literature

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Red blood with blue-blood ancestry: intriguing structure of a snail hemoglobin.

Lieb Bernhard B Dimitrova Konstantina K Kang Hio-Sun HS Braun Sabrina S Gebauer Wolfgang W Martin Andreas A Hanelt Ben B Saenz Steven A SA Adema Coen M CM Markl Jürgen J

Proceedings of the National Academy of Sciences of the United States of America 20060728 32

The phylogenetic enigma of snail hemoglobin, its isolated occurrence in a single gastropod family, the Planorbidae, and the lack of sequence data, stimulated the present study. We present here the complete cDNA and predicted amino acid sequence of two hemoglobin polypeptides from the planorbid Biomphalaria glabrata (intermediate host snail for the human parasite Schistosoma mansoni). Both isoforms contain 13 different, cysteine-free globin domains, plus a small N-terminal nonglobin "plug" domain ...[more]

PMID: 16877545

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Project description:Abnormally shaped red blood cells (RBCs), called poikilocytes, can cause anemia. At present, the biochemical abnormalities in poikilocytes are not well understood. Normal RBCs and poikilocytes were analyzed using whole-blood and single-cell methods. Poikilocytes were induced in rat blood by intragastrically administering titanium dioxide (TiO2) nanoparticles. Complete blood count and inductively coupled plasma mass spectrometry analyses were performed on whole-blood to measure average RBC morphology, blood hemoglobin (HGB), iron content, and other blood parameters. Follow-up confocal Raman spectroscopy was performed on single RBCs to analyze cell-type-specific HGB content. Two types of poikilocytes, acanthocytes and echinocytes, were observed in TiO2 blood samples, along with normal RBCs. Acanthocytes (diameter 7.7??±??0.5???m) and echinocytes (7.6??±??0.6???m) were microscopically larger (p??<??0.05) than normal RBCs (6.6??±??0.4???m) found in control blood samples (no TiO2 administration). Similarly, mean corpuscular volume was higher (p??<??0.05) in TiO2 whole-blood (70.70??±??1.97??fl) than in control whole-blood (67.42??±??2.03??fl). Poikilocytes also had higher HGB content. Mean corpuscular hemoglobin was higher (p??<??0.05) in TiO2 whole-blood (21.84??±??0.75??pg) than in control whole-blood (20.8??±??0.32??pg). Iron content was higher (p??<??0.001) in TiO2 whole-blood (697.0??±??24.5??mg??/??l) than in control whole-blood (503.4??±??38.5??mg??/??l), which supports elevated HGB as iron is found in HGB. HGB-associated Raman bands at 1637, 1585, and 1372??cm??-??1 had higher (p??<??0.001) amplitudes in acanthocytes and echinocytes than in RBCs from control blood and normal RBCs from TiO2 blood. Further, the 1585-cm??-??1 band had a lower (p??< ?0.05) amplitude in normal RBCs from TiO2 versus control RBCs. This represents biochemical abnormalities in normal appearing RBCs. Overall, poikilocytes, especially acanthocytes, have elevated HGB.

Dataset Information

Red blood with blue-blood ancestry: intriguing structure of a snail hemoglobin.

Publications

Red blood with blue-blood ancestry: intriguing structure of a snail hemoglobin.

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