Academic Journal
The hemoglobins of the trematodes Fasciola hepatica and Paramphistomum epiclitum: a molecular biological, physico-chemical, kinetic, and vaccination study
| العنوان: | The hemoglobins of the trematodes Fasciola hepatica and Paramphistomum epiclitum: a molecular biological, physico-chemical, kinetic, and vaccination study |
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| المؤلفون: | S. Dewilde, A. I. Ioanitescu, L. Kiger, K. Gilany, M.C. Marden, S. Van Doorslaer, J. Vercruysse, A. Pesce, L. Moens, M. Nardini, M. Bolognesi |
| المساهمون: | S. Dewilde, A.I. Ioanitescu, L. Kiger, K. Gilany, MC. Marden, S. Van Doorslaer, J. Vercruysse, A. Pesce, M. Nardini, M. Bolognesi, L. Moens |
| بيانات النشر: | Cold Spring Harbor Laboratory Press |
| سنة النشر: | 2008 |
| المجموعة: | The University of Milan: Archivio Istituzionale della Ricerca (AIR) |
| مصطلحات موضوعية: | 3D structure, Fluke, Hemoglobin, Ligand binding, Spectroscopy, Vaccination, Settore BIO/10 - Biochimica |
| الوصف: | The trematode Fasciola hepatica (Fa. he.) is a common parasite of human and livestock. The hemoglobin (Hb) of Fa. he., a potential immunogen, was chosen for characterization in the search for an effective vaccine. Characterization of trematode Hbs show that they are intracellular single-domain globins with the following remarkable features: (1) Fa. he. expresses two Hb isoforms that differ at two amino acid sites (F1: 119Y/123Q; F2: 119F/123L). Both isoforms are monoacetylated at their N-termini; (2) the genes coding for Fa. he. and Paramphistomum epiclitum (Pa. ep.) Hbs are interrupted by two introns at the conserved positions B12.2 and G7.0.; (3) UV/VIS and resonance Raman spectroscopy identify the recombinant Fa. he. HbF2 as a pentacoordinated high-spin ferrous Hb; (4) electron paramagnetic resonance spectroscopy of cyano-met Fa. he. HbF2 proves that the endogenously bound imidazole has no imidazolate character; (5) the major structural determinants of the globin fold are present, they contain a TyrB10/TyrE7 residue pair on the distal side. Although such distal-site pair is a signature for high oxygen affinity, as shown for Pa. ep. Hb, the oxygen-binding rate parameters for Fa. he. Hb are intermediate between those of myoglobin and those of other trematode Hbs; (6) the three-dimensional structure of recombinant Fa. he. HbF2 from this study closely resembles the three-dimensional structure of Pa. ep. determined earlier. The set of distal-site polar interactions observed in Pa. ep. Hb is matched with small but significant structural adjustments; (7) despite the potential immunogenic character of the fluke Hb, vaccination of calves with recombinant Fa. he. HbF2 failed to promote protection against parasitic infection. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/pmid/18621914; info:eu-repo/semantics/altIdentifier/wos/WOS:000259401900002; volume:17; issue:10; firstpage:1653; lastpage:1662; journal:PROTEIN SCIENCE; http://hdl.handle.net/2434/54871; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-52949146026 |
| DOI: | 10.1110/ps.036558.108 |
| الاتاحة: | http://hdl.handle.net/2434/54871 https://doi.org/10.1110/ps.036558.108 |
| رقم الانضمام: | edsbas.1635AA85 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1110/ps.036558.108 |
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