N -Glycolylneuraminic Acid on Human Epithelial Cells Prevents Entry of Influenza A Viruses That Possess N -Glycolylneuraminic Acid Binding Ability

التفاصيل البيبلوغرافية
العنوان: N -Glycolylneuraminic Acid on Human Epithelial Cells Prevents Entry of Influenza A Viruses That Possess N -Glycolylneuraminic Acid Binding Ability
المؤلفون: Sawako Kawagishi, Midori Masuda, Kiyoshi Ikeda, Tadamune Otsubo, Takashi Suzuki, Maiko Takano, Masahiro Takaguchi, Akira Minami, Takashi Yamanaka, Tadanobu Takahashi, Yuuki Kurebayashi
المصدر: Journal of Virology. 88:8445-8456
بيانات النشر: American Society for Microbiology, 2014.
سنة النشر: 2014
مصطلحات موضوعية: Immunology, Biology, medicine.disease_cause, Microbiology, Virus, Cell Line, chemistry.chemical_compound, N-Glycolylneuraminic acid, Virology, Influenza A virus, medicine, Animals, Humans, Receptor, Infectivity, Virus receptor, Cell Membrane, Epithelial Cells, Haplorhini, Transfection, Virus Internalization, Molecular biology, Virus-Cell Interactions, chemistry, Cell culture, Insect Science, Receptors, Virus, Neuraminic Acids
الوصف: Some animal influenza A viruses (IAVs) bind not only to N -acetylneuraminic acid (Neu5Ac) but also to N -glycolylneuraminic acid (Neu5Gc), which has been discussed as a virus receptor. Human cells cannot synthesize Neu5Gc due to dysfunction of the CMP-Neu5Ac hydroxylase (CMAH) gene, which converts CMP-Neu5Ac to CMP-Neu5Gc. However, exogenous Neu5Gc from Neu5Gc-rich dietary sources is able to be metabolically incorporated into surfaces of tissue cells and may be related to enhancement of the infectivity and severity of IAV. Here, we investigated the receptor function of Neu5Gc on IAV infection in Neu5Gc-expressing cells by transfection of the monkey CMAH gene into human cells or by incubation with human cells in the presence of N -glycolylmannosamine. Expression of Neu5Gc on human cells clearly suppressed infectivity of IAVs that possess Neu5Gc binding ability. Furthermore, there was no difference in infectivity of a transfectant virus that included the wild-type HA gene from A/Memphis/1/1971 (H3N2), which shows no Neu5Gc binding, between parent MCF7 cells and cells stably expressing the monkey CMAH gene (CMAH-MCF7 cells). On the other hand, cell entry of the transfectant virus that included the Neu5Gc-binding HA gene with a single mutation to Tyr at position Thr155 was arrested at the stage of internalization from the plasma membrane of the CMAH-MCF7 cells. These results indicate that expression of Neu5Gc on the surface of human epithelial cells suppresses infection of IAVs that possess Neu5Gc binding ability. Neu5Gc is suggested to work as a decoy receptor of Neu5Gc-binding IAVs but not a functional receptor for IAV infection. IMPORTANCE Influenza A viruses (IAVs) bind to the host cell surfaces through sialic acids at the terminal of glycoconjugates. For IAV binding to sialic acids, some IAVs bind not only to N -acetylneuraminic acid (Neu5Ac) as a receptor but also to N -glycolylneuraminic acid (Neu5Gc). Neu5Gc has been discussed as a receptor of human and animal IAVs. Our results showed that Neu5Gc expression on human epithelial cells suppresses infection of IAVs that possess Neu5Gc binding ability. Neu5Gc is suggested to be a “decoy receptor” of Neu5Gc-binding IAVs but not a functional receptor for IAV infection. Human cells cannot synthesize Neu5Gc because of dysfunction of the CMP- N -acetylneuraminic acid hydroxylase gene but can exogenously and metabolically incorporate Neu5Gc from dietary sources. The expression of Neu5Gc on human epithelial cells by taking in exogenous Neu5Gc from Neu5Gc-rich dietary sources may be related to restriction of the infection of IAVs that have acquired Neu5Gc binding ability.
تدمد: 1098-5514
0022-538X
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebc867f8ba08892ed72dcbb8af551106Test
https://doi.org/10.1128/jvi.00716-14Test
حقوق: OPEN
رقم الانضمام: edsair.doi.dedup.....ebc867f8ba08892ed72dcbb8af551106
قاعدة البيانات: OpenAIRE