Glycoconjugate Journal

, Volume 23, Issue 1, pp 115–125

Search for additional influenza virus to cell interactions

Authors

  • E. M. Rapoport
    • Shemyakin & Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
  • L. V. Mochalova
    • Shemyakin & Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
  • H.-J. Gabius
    • Institut für Physiologische Chemie, Tierärztliche FakultätLudwig-Maximilians-Universität
  • J. Romanova
    • Institute of Applied MicrobiologyUniversity of Natural Resources and Applied Life Sciences
    • Shemyakin & Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of Sciences
Article

DOI: 10.1007/s10719-006-5444-x

Cite this article as:
Rapoport, E.M., Mochalova, L.V., Gabius, H. et al. Glycoconj J (2006) 23: 115. doi:10.1007/s10719-006-5444-x

Abstract

Sialyl oligosaccharides have long been considered to be the sole receptors for influenza virus. However, according to [1] some viruses are able to grow in sialic-free MDCK cells. Here we attempted to reveal a possible second, non-sialic receptor, hypothesizing the involvement of additional carbohydrate lectin recognition in influenza virus reception process, first of all in situations when a lectin of the host cell could recognize the viral carbohydrate ligand. We tested the presence of galactose- and sialic acid-binding lectins, as well as mannoside- and sulfo-N-acetyllactosamine-recognizing properties of MDCK and Vero cells using polyacrylamide neoglycoconjugates and antibodies. MDCK cells bind galactoside probes stronger than Vero cells, whereas Vero cells bind preferentially sialoside, mannoside and various sulfo-oligosaccharide probes. The probing of viruses with the neoglycoconjugates revealed specific 6′-HSO 3 LacNAc (but not other sulfated oligosaccharides) binding property of A and B human strains. Affinity of 6′-HSO 3 LacNAc probe was comparable with affinity of 6′-SiaLac probe but the binding was not inhibited by the sialooligosaccharide.

Keywords

GalectinsGlycoconjugatesInfluenza virusHemagglutininSiglecs

Abbreviations

BHK

baby hamster kidney cells

biot

biotin residue

BSA

bovine serum albumin

FBS

fetal bovine serum

FITC

fluorescein isothiocyanate

fluo

fluorescein residue

HA

hemagglutinin

MBP

mannose-binding protein

MDBK

Madin-Darby bovine kidney cells

MDCK

Madin-Darby canine kidney cells

NA

neuraminidase

OS

oligosaccharide

PAA

polyacrylamide

PBS

phosphate buffered saline

PBA

PBS containing 0.2% BSA

RBS

receptor binding site

SP

surfactant protein

Sug

mono- or oligosaccharide residue

3′SL

3′-sialyllactose

LacNAc

N-acetyllactosamine

6′SLN

6′-sialyl-N-acetyllactosamine

3′SLN

3′-sialyl-N-acetyllactosamine

Neu5Ac

α-N-acetylneuraminic acid

asialoGM1

Galβ1-3GalNAcβ1-3Galβ1-4Glc

Fs

GalNAcα1-3GalNAcβ

Man 3

Manα1-6(Manα1-3)Man

A tri

GalNAcα1-3(Fucα1-2)Gal

A tetra

GalNAcα1-3(Fucα1-2)Galβ1-4GlcNAc

B tri

Galα1-3(Fucα1-2)Gal

SiaLe x

Neu5Acα2-3Galβ1-4(Fucα1-3)GlcNAc

7-OS

(GlcNAcβ1-2Manα1-) 2-3,6-Manβ1-4GlcNAcβ1-4GlcNAc

11-OS

(Neu5Acα2-6Galβ1-4GlcNAcβ1- 2Manα1-)2-3, 6-Manβ1-4GlcNAcβ1- 4GlcNAc

Tββ

Galβ1-3GalNAcβ

TF

Galβ1-3GalNAcα

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Copyright information

© Springer Science + Business Media, LLC 2006