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Search for additional influenza virus to cell interactions

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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.

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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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Authors and Affiliations

  1. Shemyakin & Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10, 117997, Moscow, Russia

    E. M. Rapoport, L. V. Mochalova & N. V. Bovin

  2. Institut für Physiologische Chemie, Tierärztliche Fakultät, Ludwig-Maximilians-Universität, Veterinärstr. 13, 80539, Munich, Germany

    H.-J. Gabius

  3. Institute of Applied Microbiology, University of Natural Resources and Applied Life Sciences, Muthgasse 18B, A-1190, Vienna, Austria

    J. Romanova

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  1. E. M. Rapoport
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  2. L. V. Mochalova
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  3. H.-J. Gabius
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  4. J. Romanova
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  5. N. V. Bovin
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Correspondence to N. V. Bovin.

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Rapoport, E.M., Mochalova, L.V., Gabius, HJ. et al. Search for additional influenza virus to cell interactions. Glycoconj J 23, 115–125 (2006). https://doi.org/10.1007/s10719-006-5444-x

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