title: Glycomic analysis of human respiratory tract tissues and correlation with influenza virus infection.
abstract: The first step in influenza infection of the human respiratory tract is binding of the virus to sialic (Sia) acid terminated receptors. The binding of different strains of virus for the receptor is determined by the α linkage of the sialic acid to galactose and the adjacent glycan structure. In this study the N- and O-glycan composition of the human lung, bronchus and nasopharynx was characterized by mass spectrometry. Analysis showed that there was a wide spectrum of both Sia α2-3 and α2-6 glycans in the lung and bronchus. This glycan structural data was then utilized in combination with binding data from 4 of the published glycan arrays to assess whether these current glycan arrays were able to predict replication of human, avian and swine viruses in human ex vivo respiratory tract tissues. The most comprehensive array from the Consortium for Functional Glycomics contained the greatest diversity of sialylated glycans, but was not predictive of productive replication in the bronchus and lung. Our findings indicate that more comprehensive but focused arrays need to be developed to investigate influenza virus binding in an assessment of newly emerging influenza viruses.
authors.affiliation: Department of Pathology, The University of Hong Kong, Queen Mary Hospital, Pokfulam, Hong Kong, China.
authors.forename: Trevenan
authors.initials: T
authors.lastname: Walther
authors.forename: Rositsa
authors.initials: R
authors.lastname: Karamanska
authors.forename: Renee W Y
authors.initials: RW
authors.lastname: Chan
authors.forename: Michael C W
authors.initials: MC
authors.lastname: Chan
authors.forename: Nan
authors.initials: N
authors.lastname: Jia
authors.forename: Gillian
authors.initials: G
authors.lastname: Air
authors.forename: Clark
authors.initials: C
authors.lastname: Hopton
authors.forename: Maria P
authors.initials: MP
authors.lastname: Wong
authors.forename: Anne
authors.initials: A
authors.lastname: Dell
authors.forename: J S
authors.initials: JS
authors.lastname: Malik Peiris
authors.forename: Stuart M
authors.initials: SM
authors.lastname: Haslam
authors.forename: John M
authors.initials: JM
authors.lastname: Nicholls
mesh_terms: D000328:Adult; D000818:Animals; D001717:Birds; D001980:Bronchi / Q000737:chemistry / Q000821:virology; D002460:Cell Line; D004285:Dogs; D005690:Galactose / Q000378:metabolism; D054794:Glycomics; D006801:Humans; D009980:Influenza A virus / Q000502:physiology*; D007251:Influenza, Human / Q000378:metabolism* / Q000821:virology; D008168:Lung / Q000737:chemistry / Q000821:virology; D046228:Microarray Analysis; D019158:N-Acetylneuraminic Acid / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry / Q000302:isolation & purification*; D011956:Receptors, Cell Surface / Q000378:metabolism; D012137:Respiratory System / Q000737:chemistry* / Q000821:virology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013552:Swine; D056189:Viral Tropism; D053585:Virus Attachment; D014779:Virus Replication
chemical_list: D011134:Polysaccharides; D011956:Receptors, Cell Surface; C092488:sialic acid receptor; D019158:N-Acetylneuraminic Acid; D005690:Galactose