The quail and chicken intestine have sialyl-galactose sugar chains responsible for the binding of influenza A viruses to human type receptors

Guo, Chao; Takahashi, Noriko; Yagi, Hirokazu; Kato, Koichi; Takahashi, Toshifumi; Yi, Shuang-Qin; Chen, Yong; Ito, Toshihiro; Otsuki, Koichi; Kida, Hiroshi; Kawaoka, Yoshihiro; Hidari, Kazuya I.P.J.; Miyamoto, Daisei; Suzuki, Takashi; Suzuki, Yasuo

doi:10.1093/glycob/cwm038

Cited by 86 publications

(70 citation statements)

References 52 publications

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“…Erythrocytes from various animal species that differ in oligosaccharide composition were used. Agglutination of erythrocytes from cows, horses, and pigs requires NeuAc␣2,3Gal or NeuGc␣2,3Gal recognition, while agglutination of those from chickens, ducks, guinea pigs, and humans (type O) requires NeuAc␣2,3Gal and NeuAc␣2,6Gal recognition (7,10,12). To explore the receptor specificity of H9N2 viruses, hemagglutination assays were conducted with 50 l 0.5% host red blood cells from each of the following: chicken, duck, goose, pigeon, quail, buffalo, donkey, goat, pig, dog, guinea pig, and human (type O) in phosphate buffer solution (pH 7.4) at 4°C for 45 min, as described previously (12).…”

Section: Methodsmentioning

confidence: 99%

“…For example, agglutination of erythrocytes from cows, horses, and pigs requires NeuAc␣2, 3Gal or NeuGc␣2,3Gal recognition, while agglutination of those from chickens, ducks, guinea pigs, and humans (type O) requires NeuAc␣2,3Gal and NeuAc␣2,6Gal recognition (7,10,12). Therefore, receptor specificity of influenza A viruses correlates with the agglutination of erythrocytes from different animal species (7,10,12). In order to explore the receptor specificity of the H9N2 viruses, the agglutination patterns of these H9N2 variants were systematically analyzed with erythrocytes from different animal species (Table 3).…”

Section: Introductionmentioning

confidence: 99%

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A Novel Genotype H9N2 Influenza Virus Possessing Human H5N1 Internal Genomes Has Been Circulating in Poultry in Eastern China since 1998

Zhang

Tang

Liu

et al. 2009

J Virol

100

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Many novel reassortant influenza viruses of the H9N2 genotype have emerged in aquatic birds in southern China since their initial isolation in this region in 1994. However, the genesis and evolution of H9N2 viruses in poultry in eastern China have not been investigated systematically. In the current study, H9N2 influenza viruses isolated from poultry in eastern China during the past 10 years were characterized genetically and antigenically. Phylogenetic analysis revealed that these H9N2 viruses have undergone extensive reassortment to generate multiple novel genotypes, including four genotypes (J, F, K, and L) that have never been recognized before. The major H9N2 influenza viruses represented by A/Chicken/Beijing/1/1994 (Ck/BJ/1/94)-like viruses circulating in poultry in eastern China before 1998 have been gradually replaced by A/Chicken/Shanghai/F/1998 (Ck/SH/F/98)-like viruses, which have a genotype different from that of viruses isolated in southern China. The similarity of the internal genes of these H9N2 viruses to those of the H5N1 influenza viruses isolated from 2001 onwards suggests that the Ck/SH/F/98-like virus may have been the donor of internal genes of human and poultry H5N1 influenza viruses circulating in Eurasia. Experimental studies showed that some of these H9N2 viruses could be efficiently transmitted by the respiratory tract in chicken flocks. Our study provides new insight into the genesis and evolution of H9N2 influenza viruses and supports the notion that some of these viruses may have been the donors of internal genes found in H5N1 viruses.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A Novel Genotype H9N2 Influenza Virus Possessing Human H5N1 Internal Genomes Has Been Circulating in Poultry in Eastern China since 1998

Zhang

Tang

Liu

et al. 2009

J Virol

100

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“…By using a multi-dimensional high-performance liquid chromatography (HPLC) mapping technique [26][27][28], we have been able to carry out N-glycosylation profiling in a quantitative manner at molecular, cellular, and organ levels. This prompts us to characterize the N-glycans expressed on CAM and AM cells of 10-day-old chicken embryonated eggs.…”

Section: Introductionmentioning

confidence: 99%

Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses

et al. 2008

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The initial step essential in influenza virus infection is specific binding of viral hemagglutinin to host cell-surface glycan receptors. Influenza A virus specificity for the host is mediated by viral envelope hemagglutinin, that binds to receptors containing glycans with terminal sialic acids. Human viruses preferentially bind to α2→6 linked sialic acids on receptors of host cells, whereas avian viruses are specific for the α2→3 linkage on the target cells. Human influenza virus isolates more efficiently infect amniotic membrane (AM) cells than chorioallantoic membrane (CAM) cells. N-glycans were isolated from AM and CAM cells of 10-day-old chicken embryonated eggs and their structures were analyzed by multi-dimensional HPLC mapping and MALDI-TOF-MS techniques. Terminal Nacetylneuraminic acid contents in the two cell types were similar. However, molar percents of α2→3 linkage prefer- Glycoconj J (2009) 26:433-443

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“…Chickens and quails, however, represent exceptions. In their intestinal epithelium are present both SA(α-2,3) as well as SA(α-2,6) receptors (Wan and Perez, 2006;Guo et al, 2007). Similarly, in the epithelium of swine respiratory tract are also present both SA(α-2,3) and SA(α-2,6) receptors (Sriwilaijaroen and Suzuki, 2012).…”

Section: Receptor Binding Activity and Iav Host Tropismmentioning

confidence: 99%

The role of fusion activity of influenza A viruses in their biological properties

Jakubcová¹,

Hollý²,

Varečková³

2016

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Summary. -Infl uenza A viruses (IAVs) cause acute respiratory infections of humans, which are repeated yearly. Human IAV infections are associated with signifi cant morbidity and mortality and therefore they represent a serious health problem. All human IAV strains are originally derived from avian IAVs, which, aft er their adaptation to humans, can spread in the human population and cause pandemics with more or less severe course of the disease. Presently, however, the potential of avian IAV to infect humans and to cause the disease cannot be predicted. Many studies are therefore focused on factors infl uencing the virulence and pathogenicity of IAV viruses in a given host. Th e virus-host interaction starts by virus attachment via the envelope glycoprotein hemagglutinin (HA) to the receptors on the cell surface. In addition to receptor binding, HA mediates also the fusion of viral and endosomal membranes, which follows the virus endocytosis. Th e fusion potential of HA trimer, primed by proteolytic cleavage, is activated by low pH in endosomes, resulting in HA refolding into the fusion-active form. Th e HA conformation change is predetermined by its 3-D structure, is pH-dependent, irreversible and strain-specifi c. Th e process of fusion activation of IAV hemagglutinin is crucial for virus entry into the cell and for the ability of the virus to replicate in the host. Here we discuss the known data about the characteristics of fusion activation of HA in relation to IAV virulence and pathogenicity.Keywords: infl uenza A viruses; pH optimum of fusion; IAV virulence and pathogenicity; HA conformation change; IAV interspecies transmission; adaptation changes * Corresponding author. E-mail: viruevar@savba.sk; phone: 421-2-59302427. Abbreviations: HA = hemagglutinin; HA0 = HA precursor; HA1 = heavy chain of HA; HA2 = light chain of HA; HPAI = highly pathogenic avian infl uenza; IAV(s) = infl uenza A virus(es); LPAI = low pathogenic avian infl uenza; M1 protein = matrix protein; mRNA = messenger RNA; NA = neuraminidase; NEP protein = nuclear export protein; NS1 protein = nonstructural protein 1; PA = polymerase acidic protein; PB1 = polymerase basic protein 1; PB2 = polymerase basic protein 2; RBS = receptor binding site; RNA = ribonucleic acid; RNP = ribonucleoprotein; SA = sialic acid; vRNA = viral RNA Content: 1. Introduction 2. Structure and function of hemagglutinin 2.1 Receptor binding activity and IAV host tropism 2.2 Fusion activity and structural rearrangements of HA during the membrane fusion 3. Th e HA cleavability by host proteases and HA fusion activation pH as factors of IAV virulence and pathogenicity 3.1 Cleavage activation of HA as a determinant of IAV pathogenicity 3.2 Fusion activation pH as a determinant of IAV virulence 4. Th e role of fusion activation pH and stability of HA in the adaptation of IAV to the new host 5. Other viral proteins infl uencing the IAV virulence 6. Conclusion

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The quail and chicken intestine have sialyl-galactose sugar chains responsible for the binding of influenza A viruses to human type receptors

Cited by 86 publications

References 52 publications

A Novel Genotype H9N2 Influenza Virus Possessing Human H5N1 Internal Genomes Has Been Circulating in Poultry in Eastern China since 1998

A Novel Genotype H9N2 Influenza Virus Possessing Human H5N1 Internal Genomes Has Been Circulating in Poultry in Eastern China since 1998

Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses

The role of fusion activity of influenza A viruses in their biological properties

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