Both antiviral activity and intracellular localization of chicken Mx protein depend on a polymorphism at amino acid position 631 |
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| Authors: | Keisuke Sasaki Akihiro Yoneda Akinori Ninomiya Manabu Kawahara Tomomasa Watanabe |
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| Institution: | 1. Department of Chemistry and Biochemistry, University of Arizona, 1306 East University Boulevard, Tucson, AZ 85721, USA;2. Department of Pharmacology, University of Arizona, 1501 North Campbell Avenue, Tucson, AZ 85724, USA;1. Clinical Research Center, National Center for Child Health and Development, Faculty of Veterinary Medicine, Tokyo University of Agriculture and Technology;2. Department of Veterinary Surgery, Faculty of Veterinary Medicine, Tokyo University of Agriculture and Technology;1. Department of Laboratory Sciences, Gunma University School of Health Science, 3-39-15 Showa, Maebashi, Gunma 371-8514, Japan;2. Research Institute, Kagome Co. Ltd., 17 Nishitomiyama, Nasushiobara, Tochigi 329-2762, Japan;1. Department of Neurosurgery, National Hospital Organization Nagoya Medical Center, Nagoya, Japan;2. Department of Neurosurgery, Japanese Red Cross Nagoya Daiichi Hospital, Nagoya, Japan;3. Department of Neurosurgery, Fujita Health University School of Medicine, Toyoake, Japan;4. Department of Respiratory Medicine, National Hospital Organization Nagoya Medical Center, Nagoya, Japan;5. Department of Neurosurgery, Nagoya University Graduate School of Medicine, Nagoya, Japan;1. Hara Pediatric Clinic, Kaita-cho, Aki-gun, Hiroshima 736-0035, Japan;2. Center for Public Health and Environment, Hiroshima Prefectural Technology Research Institute, Hiroshima, Japan;1. Laboratory of Animal Breeding and Reproduction, Graduate School of Agriculture, Hokkaido University, Japan;2. Division of Molecular Therapeutics, Center for Food & Medical Innovation, Hokkaido University, Japan |
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| Abstract: | The Mx protein is known to inhibit the multiplication of several RNA viruses. In chickens, a polymorphism at amino acid position 631 (631 aa) of Mx protein has been suggested to be involved in the antiviral ability against vesicular stomatitis virus (VSV) and influenza virus, indicating that a Ser-to-Asn substitution at 631 aa is the source of this antiviral ability. However, how the substitution at 631 aa contributes to the antiviral activity remains to be clarified. In this study, we investigated differences in antiviral activity against VSV and intracellular localization between Ser and Asn types at 631 aa of the chicken Mx protein. The results showed that chicken Mx protein with an Asn at 631 aa inhibited VSV multiplication and Mx distribution in a granular-like pattern in the cytoplasm. However, Mx carrying the Ser type did not inhibit viral growth and homogenous spread throughout the cytoplasm. Furthermore, we found that replacing Ser with Asn at 631 aa provided Mx with antiviral activity against VSV, with Mx showing granular-like distribution in the cytoplasm. These results demonstrated that a single amino acid polymorphism at 631 aa of the chicken Mx protein altered both the antiviral activity and intracellular localization. |
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