Bioinformatic identification of cytochrome b5 homologues from the parasitic nematode Ascaris suum and the free-living nematode Caenorhabditis elegans highlights the crucial role of A. suum adult-specific secretory cytochrome b5 in parasitic adaptation |
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| Affiliation: | 1. Department of Molecular and Cellular Parasitology, Graduate School of Medicine, Juntendo University, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan;2. R & D Strategy Department, Yokohama Research Center, Mitsubishi Chemical Corporation, 1000 Kamoshida-cho, Aoba, Yokohama 227-8502, Japan;3. Department of Life Science, Faculty of Science and Engneering, Setsunan University, 17-8 Ikeda-naka-machi, Neyagawa, Osaka 572-8508, Japan;4. Department of Chemistry, Faculty of International Liberal Arts, Juntendo University, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan;5. Laboratory of Proteomics and Biomolecular Science, Biomedical Research Center, Graduate School of Medicine, Juntendo University, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113-8421, Japan;6. Department of Parasitology, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan;1. Institute of Parasitology, Department of Pathobiology, University of Veterinary Medicine Vienna, Vienna, Austria;4. Faculty of Veterinary and Agricultural Sciences, The University of Melbourne, Parkville, VIC, Australia;1. Jiangsu Institute of Parasitic Diseases, Key Laboratory of Parasitic Disease Control and Prevention (Ministry of Health), Jiangsu Provincial Key Laboratory of Parasite Molecular Biology, Wuxi, The People''s Republic of China;4. Public Health Research Center, Jiangnan University, Wuxi, The People''s Republic of China;5. National Institute of Parasitic Diseases, Chinese Center for Disease Control and Prevention, Shanghai, The People''s Republic of China;6. Key Laboratory of Parasite and Vector Biology of the Chinese Ministry of Health, Shanghai, The People''s Republic of China;7. Zhejiang Academy of Medical Sciences, Hangzhou, Zhejiang, The People''s Republic of China;1. Departamento de Microbiologia, Imunologia e Parasitologia, Faculdade de Ciências Médicas, Universidade do Estado do Rio de Janeiro, Av. Professor Manoel de Abreu, 444, 5° Andar, Vila Isabel, 20511-070 Rio de Janeiro, RJ, Brazil;2. Laboratório de Radiofarmácia Experimental, Departamento de Biofísica e Biometria, Instituto de Biologia Roberto Alcantara Gomes, Universidade do Estado do Rio de Janeiro, Av. 28 de Setembro, 87, 4° Andar fundos, Vila Isabel, 20551-030 Rio de Janeiro, RJ, Brazil |
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| Abstract: | We previously reported that adult Ascaris suum possesses NADH-metmyoglobin and NADH-methaemoglobin reductase systems that are located in the cells of the body wall and in the extracellular perienteric fluid, respectively, which helps them adapt to environmental hypoxia by recovering the differential functions of myoglobin and haemoglobin. A. suum cytochrome b5, an adult-specific secretory protein and an essential component of the NADH-metmyo (haemo) globin reductase system, has been extensively studied, and its unique nature has been determined. However, the relationship between A. suum cytochrome b5 and the canonical cytochrome b5 proteins, from the free-living nematode Caenorhabditis elegans is unclear. Here, we have characterised four cytochrome b5-like proteins from C. elegans (accession numbers: CAB01732, CCD68984, CAJ58492, and CAA98498) and three from A. suum (accession numbers: ADY48796, ADY46277, and ADY48338) and compared them with A. suum cytochrome b5 in silico. Bioinformatic and molecular analyses showed that CAA98498 from C. elegans is equivalent of A. suum cytochrome b5, which was not expressed as a mature mRNA. Further, the CAA98498 possessed no secretory signal peptide, which occurs in A. suum cytochrome b5 precursor. These results suggest that this free-living nematode does not need a haemoprotein such as the A. suum cytochrome b5 and highlight the crucial function of this A. suum adult-specific secretory cytochrome b5 in parasitic adaptation. |
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