Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities

James Stevens; Ola Blixt; Laurel Glaser; Jeffery K Taubenberger; Peter Palese; James C Paulson; Ian A Wilson

doi:10.1016/j.jmb.2005.11.002

Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities

James Stevens, Ola Blixt, Laurel Glaser, Jeffery K Taubenberger, Peter Palese, James C Paulson, Ian A Wilson

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

577 Citationer (Scopus)

Abstract

Udgivelsesdato: 2006-Feb-3

Originalsprog	Engelsk
Tidsskrift	Journal of Molecular Biology
Vol/bind	355
Udgave nummer	5
Sider (fra-til)	1143-55
Antal sider	12
ISSN	0022-2836
DOI	https://doi.org/10.1016/j.jmb.2005.11.002
Status	Udgivet - 2005
Udgivet eksternt	Ja

Bibliografisk note

Keywords: Amino Acid Sequence; Animals; Carbohydrate Conformation; Carbohydrate Sequence; Hemagglutinin Glycoproteins, Influenza Virus; Humans; Influenza A virus; Microarray Analysis; Models, Molecular; Molecular Sequence Data; Receptors, Virus; Sequence Alignment; Sialic Acids

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10.1016/j.jmb.2005.11.002

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Citationsformater

@article{73911fc008bf11de8478000ea68e967b,

title = "Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities",

abstract = "Influenza A virus specificity for the host is mediated by the viral surface glycoprotein hemagglutinin (HA), which binds to receptors containing glycans with terminal sialic acids. Avian viruses preferentially bind to alpha2-3-linked sialic acids on receptors of intestinal epithelial cells, whereas human viruses are specific for the alpha2-6 linkage on epithelial cells of the lungs and upper respiratory tract. To define the receptor preferences of a number of human and avian H1 and H3 viruses, including the 1918 H1N1 pandemic strains, their hemagglutinins were analyzed using a recently described glycan array. The array, which contains 200 carbohydrates and glycoproteins, not only revealed clear differentiation of receptor preferences for alpha2-3 and/or alpha2-6 sialic acid linkage, but could also detect fine differences in HA specificity, such as preferences for fucosylation, sulfation and sialylation at positions 2 (Gal) and 3 (GlcNAc, GalNAc) of the terminal trisaccharide. For the two 1918 HA variants, the South Carolina (SC) HA (with Asp190, Asp225) bound exclusively alpha2-6 receptors, while the New York (NY) variant, which differed only by one residue (Gly225), had mixed alpha2-6/alpha2-3 specificity, especially for sulfated oligosaccharides. Only one mutation of the NY variant (Asp190Glu) was sufficient to revert the HA receptor preference to that of classical avian strains. Thus, the species barrier, as defined by the receptor specificity preferences of 1918 human viruses compared to likely avian virus progenitors, can be circumvented by changes at only two positions in the HA receptor binding site. The glycan array thus provides highly detailed profiles of influenza receptor specificity that can be used to map the evolution of new human pathogenic strains, such as the H5N1 avian influenza.",

author = "James Stevens and Ola Blixt and Laurel Glaser and Taubenberger, {Jeffery K} and Peter Palese and Paulson, {James C} and Wilson, {Ian A}",

note = "Keywords: Amino Acid Sequence; Animals; Carbohydrate Conformation; Carbohydrate Sequence; Hemagglutinin Glycoproteins, Influenza Virus; Humans; Influenza A virus; Microarray Analysis; Models, Molecular; Molecular Sequence Data; Receptors, Virus; Sequence Alignment; Sialic Acids",

year = "2005",

doi = "10.1016/j.jmb.2005.11.002",

language = "English",

volume = "355",

pages = "1143--55",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

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TY - JOUR

T1 - Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities

AU - Stevens, James

AU - Blixt, Ola

AU - Glaser, Laurel

AU - Taubenberger, Jeffery K

AU - Palese, Peter

AU - Paulson, James C

AU - Wilson, Ian A

N1 - Keywords: Amino Acid Sequence; Animals; Carbohydrate Conformation; Carbohydrate Sequence; Hemagglutinin Glycoproteins, Influenza Virus; Humans; Influenza A virus; Microarray Analysis; Models, Molecular; Molecular Sequence Data; Receptors, Virus; Sequence Alignment; Sialic Acids

PY - 2005

Y1 - 2005

N2 - Influenza A virus specificity for the host is mediated by the viral surface glycoprotein hemagglutinin (HA), which binds to receptors containing glycans with terminal sialic acids. Avian viruses preferentially bind to alpha2-3-linked sialic acids on receptors of intestinal epithelial cells, whereas human viruses are specific for the alpha2-6 linkage on epithelial cells of the lungs and upper respiratory tract. To define the receptor preferences of a number of human and avian H1 and H3 viruses, including the 1918 H1N1 pandemic strains, their hemagglutinins were analyzed using a recently described glycan array. The array, which contains 200 carbohydrates and glycoproteins, not only revealed clear differentiation of receptor preferences for alpha2-3 and/or alpha2-6 sialic acid linkage, but could also detect fine differences in HA specificity, such as preferences for fucosylation, sulfation and sialylation at positions 2 (Gal) and 3 (GlcNAc, GalNAc) of the terminal trisaccharide. For the two 1918 HA variants, the South Carolina (SC) HA (with Asp190, Asp225) bound exclusively alpha2-6 receptors, while the New York (NY) variant, which differed only by one residue (Gly225), had mixed alpha2-6/alpha2-3 specificity, especially for sulfated oligosaccharides. Only one mutation of the NY variant (Asp190Glu) was sufficient to revert the HA receptor preference to that of classical avian strains. Thus, the species barrier, as defined by the receptor specificity preferences of 1918 human viruses compared to likely avian virus progenitors, can be circumvented by changes at only two positions in the HA receptor binding site. The glycan array thus provides highly detailed profiles of influenza receptor specificity that can be used to map the evolution of new human pathogenic strains, such as the H5N1 avian influenza.

AB - Influenza A virus specificity for the host is mediated by the viral surface glycoprotein hemagglutinin (HA), which binds to receptors containing glycans with terminal sialic acids. Avian viruses preferentially bind to alpha2-3-linked sialic acids on receptors of intestinal epithelial cells, whereas human viruses are specific for the alpha2-6 linkage on epithelial cells of the lungs and upper respiratory tract. To define the receptor preferences of a number of human and avian H1 and H3 viruses, including the 1918 H1N1 pandemic strains, their hemagglutinins were analyzed using a recently described glycan array. The array, which contains 200 carbohydrates and glycoproteins, not only revealed clear differentiation of receptor preferences for alpha2-3 and/or alpha2-6 sialic acid linkage, but could also detect fine differences in HA specificity, such as preferences for fucosylation, sulfation and sialylation at positions 2 (Gal) and 3 (GlcNAc, GalNAc) of the terminal trisaccharide. For the two 1918 HA variants, the South Carolina (SC) HA (with Asp190, Asp225) bound exclusively alpha2-6 receptors, while the New York (NY) variant, which differed only by one residue (Gly225), had mixed alpha2-6/alpha2-3 specificity, especially for sulfated oligosaccharides. Only one mutation of the NY variant (Asp190Glu) was sufficient to revert the HA receptor preference to that of classical avian strains. Thus, the species barrier, as defined by the receptor specificity preferences of 1918 human viruses compared to likely avian virus progenitors, can be circumvented by changes at only two positions in the HA receptor binding site. The glycan array thus provides highly detailed profiles of influenza receptor specificity that can be used to map the evolution of new human pathogenic strains, such as the H5N1 avian influenza.

U2 - 10.1016/j.jmb.2005.11.002

DO - 10.1016/j.jmb.2005.11.002

M3 - Journal article

C2 - 16343533

SN - 0022-2836

VL - 355

SP - 1143

EP - 1155

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 5

ER -