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Influenza C virus

O-Acetyl-N-acetylmannosamine 6, prepared from Af-acetylmannosamine either by chemical acetylation [28] or by transesterification catalyzed by subtilisin [31], led to 9-0-acetyl Neu5Ac 7 [29], a receptor of influenza C virus occurring on human erythrocytes. Several other 9-O-substituted Neu5Ac derivatives could also be prepared [29-32]. [Pg.472]

Acetylation of mucin-bound and membrane-bound sialic acids makes them more resistant towards sialidase action [8,33,245,853,854]. This may be one of the reasons why intestinal mucins, especially of the colon, are often O-acetylated (ref. [245], and section 8.4.2). The high level of 0-acetylation of sialic acids observed in the endothelia of blood vessels, e.g, in liver, detected by histochemical methods using influenza C virus hemagglutinin, is assumed to have a similar function [234,235,730]. [Pg.343]

Rogers, G. N. Herrler, G. Paulson, J. C. Klenk, H. D., Influenza C virus uses 9-0-acetyl-N-acetylneuraminic acid as a. high affinity receptor determinant for attachment to cells. JR/o/C/tem 1986,261, (13), 5947-51. Brossmer, R. Gross, H. J., Fluorescent and photoactivatable sialic acids. Methods Enzymol 1994,247,177-93. [Pg.13]

Influenzavirus C (influenza C virus). Enveloped, helical, negative-sense, and... [Pg.1215]

H. (2006) Clinical features of influenza C virus infection in children. The Journal of Infectious Diseases, 193, 1229-1235. [Pg.677]

Isolation of influenza C virus recombinants. Journal of Virology, 32, 1006-1014. [Pg.677]

Structure of the haemagglutinin-esterase-fiision glycoprotein of influenza C virus. [Pg.677]

Fig. 1 Sialic acid binding sites of the hemagglutinin (a) and the neuraminidase (b) of influenza A virus and the hemagglutinin-esterase-fusion protein of influenza C virus (c). Molecular surfaces of HA and HEF trimers and the NA tetramer are shown. Receptor-binding sites of HA, HEF and the hemadsorption site of NA are colored ye/tow. The catalytic sites of NA and HEF are colored green. Sialic acid moieties in the binding sites of HA and NA are shown as stick models. The figtffe is based on crystal structures IMQM, 1W20, and IFLC from Protein Data Bank... Fig. 1 Sialic acid binding sites of the hemagglutinin (a) and the neuraminidase (b) of influenza A virus and the hemagglutinin-esterase-fusion protein of influenza C virus (c). Molecular surfaces of HA and HEF trimers and the NA tetramer are shown. Receptor-binding sites of HA, HEF and the hemadsorption site of NA are colored ye/tow. The catalytic sites of NA and HEF are colored green. Sialic acid moieties in the binding sites of HA and NA are shown as stick models. The figtffe is based on crystal structures IMQM, 1W20, and IFLC from Protein Data Bank...
Herrler G, Rott R, Klenk HD, Muller HP, Shukla AK, Schauer R (1985) The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase. EMBO J... [Pg.21]

HerrlCT G, Multhaup G, BeyreutherK, KlenkHD(1988) Serine 71 of the glycoprotein HEF is located at the active site of the acetylesterase of influenza C virus. Arch Virol 102 269-274... [Pg.22]

Pleschka S, Klenk HD, Herder G (1995) The catalytic triad of the influenza C virus glycoprotein HEF esterase characterization by site-directed mutagenesis and functional analysis. J Gen Virol 76 2529-2537... [Pg.22]

Vlasak R, Muster T, Lauro AM, Powers JC, Palese P (1989) Influenza C virus esterase analysis of catalytic site, inhibition, and possible function. J Virol 63 2056-2062... [Pg.22]

Hofling K, Klenk HD, Herrler G (1997) Inactivation of inhibitors by the receptor-destroying enzyme of influenza C virus. J Gtm Virol 78 567-570... [Pg.22]

Herrlta G, Gross HJ, Brossmer R (1995) A synthetic sialic acid analog that is resistant to the receptOT-destroying enzyme can be used by influenza C virus as a receptor determinant for infectitm of cells. Biochem Biophys Res Commun 216 821-827... [Pg.22]

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See also in sourсe #XX -- [ Pg.1694 ]



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