title: The quail and chicken intestine have sialyl-galactose sugar chains responsible for the binding of influenza A viruses to human type receptors.
abstract: The receptor specificity of influenza viruses is one factor that allows avian influenza viruses to cross the species barrier. The recent transmissions of avian H5N1 and H9N2 influenza viruses from chickens and/or quails to humans indicate that avian influenza viruses can directly infect humans without an intermediate host, such as pigs. In this study, we used two strains of influenza A virus (A/PR/8/34, which preferentially binds to an avian-type receptor, and A/Memphis/1/71, which preferentially binds to a human-type receptor) to probe the receptor specificities in host cells. Epithelial cells of both quail and chicken intestines (colons) could bind both avian- and human-type viruses. Infected cultured quail colon cells expressed viral protein and allowed replication of the virus strain A/PR/8/34 or A/Memphis/1/71. To understand the molecular basis of these phenomena, we further investigated the abundance of sialic acid (Sia) linked to galactose (Gal) by the alpha2-3 linkage (Siaalpha2-3Gal) and Siaalpha2-6Gal in host cells. In glycoprotein and glycolipid fractions from quail and chicken colon epithelial cells, there were some bound components of Sia-Gal linkage-specific lectins, Maackia amurensis agglutinin (specific for Siaalpha2-3 Gal) and Sambucus nigra agglutinin (specific for Siaalpha2-6Gal), indicating that both Siaalpha2-3Gal and Siaalpha2-6Gal exist in quail and chicken colon cells. Furthermore, we demonstrated by fluorescence high-performance liquid chromatography (HPLC) analysis that 5-N-acetylneuraminic acid was the main molecular species of Sia, and we demonstrated by multi-dimensional HPLC mapping and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analysis that bi-antennary complex-type glycans alpha2-6 sialylated at the terminal Gal residue(s) are major (more than 79%) sialyl N-glycans expressed by intestinal epithelial tissues in both the chicken and quail. Taken together, these results indicate that quails and chickens have molecular characterization as potential intermediate hosts for avian influenza virus transmission to humans and could generate new influenza viruses with pandemic potential.
authors: Institute of Bioengineering, Zhejiang Academy of Medical Sciences, 182 Tianmushan Road, Hangzhou 310016, China.
authors: Chao-Tan
authors: CT
authors: Guo
authors: Noriko
authors: N
authors: Takahashi
authors: Hirokazu
authors: H
authors: Yagi
authors: Koichi
authors: K
authors: Kato
authors: Tadanobu
authors: T
authors: Takahashi
authors: Shuang-Qin
authors: SQ
authors: Yi
authors: Yong
authors: Y
authors: Chen
authors: Toshihiro
authors: T
authors: Ito
authors: Koichi
authors: K
authors: Otsuki
authors: Hiroshi
authors: H
authors: Kida
authors: Yoshihiro
authors: Y
authors: Kawaoka
authors: Kazuya I-P Jwa
authors: KI
authors: Hidari
authors: Daisei
authors: D
authors: Miyamoto
authors: Takashi
authors: T
authors: Suzuki
authors: Yasuo
authors: Y
authors: Suzuki
mesh_terms: D000818:Animals; D002241:Carbohydrates / Q000737:chemistry*; D002645:Chickens; D004847:Epithelial Cells / Q000821:virology; D005690:Galactose / Q000737:chemistry*; D006017:Glycolipids / Q000737:chemistry; D006031:Glycosylation; D006801:Humans; D053124:Influenza A Virus, H5N1 Subtype / Q000378:metabolism*; D053127:Influenza A Virus, H9N2 Subtype / Q000378:metabolism*; D009980:Influenza A virus / Q000378:metabolism*; D007413:Intestinal Mucosa / Q000378:metabolism*; D019158:N-Acetylneuraminic Acid / Q000737:chemistry*; D011485:Protein Binding; D011784:Quail
chemical_list: D002241:Carbohydrates; D006017:Glycolipids; D019158:N-Acetylneuraminic Acid; D005690:Galactose