کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10758732 | 1050412 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Influenza virus utilizes N-linked sialoglycans as receptors in A549 cells
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کلمات کلیدی
IFVSSATLCNeu5GcMAHSIANeu5AcMAMMonoclonal antibody - آنتی بادی مونوکلونالN-acetylneuraminic acid - اسید N-استیلون اورامینیکN-glycolylneuraminic acid - اسید N-گلیکولیل نورامنیکSPR - تشدید پلاسمون سطحیSurface plasmon resonance - تشدید پلاسمون سطحیSialic acid - سیالیک اسیدhemagglutinin - هماگلوتینینInfluenza virus - ویروس آنفولانزاthin-layer chromatography - کروماتوگرافی نازک لایهReceptor - گیرنده
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Influenza virus utilizes N-linked sialoglycans as receptors in A549 cells Influenza virus utilizes N-linked sialoglycans as receptors in A549 cells](/preview/png/10758732.png)
چکیده انگلیسی
Influenza viruses (IFVs) recognize sialoglycans expressed on the host cell surface. To understand the mechanisms underlying tissue and host tropisms of IFV, it is essential to elucidate the molecular interaction of the virus with the host sialoglycan receptor. We established and applied a new monoclonal antibody, clone HYB4, which specifically recognizes the Neu5Acα2-3 determinant at the non-reducing terminal Gal residue of both glycoproteins and gangliosides to investigate the biochemical properties of IFV receptors in A549 cells. HYB4 significantly blocked virus binding to A549 cells in a dose-dependent manner. Virus overlay assay indicated that several glycoproteins with molecular masses of 80-120 kDa of A549 cells were commonly recognized by different subtypes of IFV, such as H1N1 and H3N2. H1N1 virus binding to the glycoproteins was diminished by pretreatment with either sialidase or PNGase F. On TLC-immunostaining experiments with HYB4, GM3 ganglioside was only detected in A549 cells. Interestingly, this antibody bound to GM3 gangliosides on TLC and plastic surfaces, but not on lipid bilayers. In comparison with the recognition of Maackia amurensis lectins, HYB4 exclusively recognized Neu5Acα2-3Galβ1-4GlcNAc residues expressed on glycoproteins. These results strongly suggest that N-linked sialoglycans with the Neu5Acα2-3 determinant on several glycoproteins are receptors for influenza virus in A549 cells.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 436, Issue 3, 5 July 2013, Pages 394-399
Journal: Biochemical and Biophysical Research Communications - Volume 436, Issue 3, 5 July 2013, Pages 394-399
نویسندگان
Kazuya I.P.J. Hidari, Maho Yamaguchi, Fumihiko Ueno, Tomoko Abe, Kazuhiro Yoshida, Takashi Suzuki,