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Influenza virus receptors

Matrosovich M, Klenk H-D (2003) Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding. Rev Med Virol 13 85-97 Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk H-D (2004) Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol 78 12665-12667... [Pg.150]

Shinya K, Ebina M, Yamada S, Ono M, Kasai N, Kawaoka Y. Avian flu influenza virus receptors in the human airway. Nature 2006 440 435-436. [Pg.403]

Baum LG, Paulson JC (1990) Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity. Acta Histochem Suppl 40 35-38... [Pg.19]

Gambaryan A, Webster R, Matrosovich M (2002) Differences between influenza virus receptors on target cells of duck and chicken. Arch Virol 147 1197-1208... [Pg.19]

Kuchipudi SV, Nelli R, White GA, Bain M, Chang KC, Dunham S (2009) Differences in influenza virus receptors in chickens and ducks implications for interspecies transmission. J Mol Genet Med 3 143-151... [Pg.19]

Pillai SP, Lee CW (2010) Species and age related differences in the type and distribution of influenza virus receptors in different tissues of chickens, ducks and turkeys. Virol J 7 5... [Pg.19]

Fazekas de St. Groth S. (1948) Destruction of Influenza Virus Receptors in Mouse Lung by an Enzyme from V. Cholera. Aust. J. Exp. Biol. 26, 29 36. [Pg.1942]

McCrea, J. F., 1954, Studies on influenza virus receptor substance and receptor-substance analogues. II. Isolation and purification of a mucoprotein receptor substance from human erythrocyte stroma treated with pentane, Yale J. Biol. Med. 26 191. [Pg.233]

Springer, G. F., and Rapaport, M. J., 1957, Specific release of heterogenetic mononucleosis receptor by influenza viruses, receptor destroying enzyme and plant proteases, Proc. Soc. Exp. Biol. Med. 96 103-107. [Pg.356]

Watowich, S.I., et al. Crystal structures of influenza virus haemagglutinin in complex with high affinity receptor analogs. Structure 2 719-731, 1994. [Pg.87]

Fig. 1 A view of the influenza virus haemagglutinin (HA) monomer with the receptor fragment a-2,3-sialyUactose [a-Neu5Ac-(2,3)- 3-Gal-(1,4)-P-Glc] bound... Fig. 1 A view of the influenza virus haemagglutinin (HA) monomer with the receptor fragment a-2,3-sialyUactose [a-Neu5Ac-(2,3)- 3-Gal-(1,4)-P-Glc] bound...
Varghese IN, Colman PM (1991) Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution. 1 Mol Biol 221 473 86 Varghese IN, Laver WG, Colman PM (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303 35 0 Varghese IN, McKimm-Breschkin IL, Caldwell IB, Kortt AA, Colman PM (1992) The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 14 327-332... [Pg.153]

Glycophorin A appears to serve a variety of functions on the red-cell membrane, and has been implicated in several red-cell disorders. Because it extends from the external environment of the cell into the cell cytoplasm, it is considered to constitute a receptor for malarial parasites,"" influenza viruses, lectins, and Portuguese man-of-war toxin. Many of these receptor functions are attributable to the carbohydrate composition of these... [Pg.170]

Specific proteins on the surface of virus particles, e.g. the haemagglutinins of influenza viruses (Fig. 3.8), mediate their adherence to glycoprotein receptors in the plasma membrane of host cells. Viruses make use of a variety of membrane glycoproteins as... [Pg.68]

In general, virus receptors carry out normal functions in the cell. For example, in bacteria some phage receptors are pili or flagella, others are cell-envelope components, and others are transport binding proteins. The receptor for influenza vims is a glycoprotein found on red blood cells and on cells of the mucous membrane of susceptible animals, whereas the receptor site of poliovirus is a lipoprotein. However, many animal and plant viruses do not have specific attachment sites at all and the vims enters passively as a result of phagocytosis or some other endocytotic process. [Pg.124]

Several reports are available on the biological activities of thioamide derivatives. The thioamide derivatives have shown significant activities, such as antituberculosis drug, anti-influenza virus activity, antitumor activity, anthelmintic activity, opioid receptor binding property, etc.94 101... [Pg.160]

Lawrence, B.P. and Vorderstrasse, B.A., Activation of the aryl hydrocarbon receptor diminishes the memory response to homotypic influenza virus infection but does not impair host resistance, Toxicol. Sci., 79, 304, 2004. [Pg.120]

Mitchell, K. and Lawrence, B.P., T cell receptor transgenic mice provide novel insights into understanding cellular targets of TCDD Suppression of antibody production, but not the response of CD8+ T cells, during infection with influenza virus, Toxicol. Appl. Pharmacol., 192, 275, 2003. [Pg.254]

Fig. 4—A comparison of the H-D antigenic component and the receptor for influenza virus hemagglutinin, which are a-NeuGc-(2 — 3)-/ -Gal and a-NeuAc-(2 — 3)-/ -Gal, respectively, on the backbones / -D-Gal-( 1 — 4)-jS-d-G1cNAc-( 1 -> 3)-jS-D-Gal-(l - 4)-d-G1cNAc (sialyl i), yS-D-Gal-(l — 4)-yJ-D-GlcNAc-(l - 6)-D-Gal (sialyl I). The CH3 of the acetamido group of Ar-acetylneuraminic acid, which is a CH2OH group in iV-glycolyl-neuraminic acid, is shown. Fig. 4—A comparison of the H-D antigenic component and the receptor for influenza virus hemagglutinin, which are a-NeuGc-(2 — 3)-/ -Gal and a-NeuAc-(2 — 3)-/ -Gal, respectively, on the backbones / -D-Gal-( 1 — 4)-jS-d-G1cNAc-( 1 -> 3)-jS-D-Gal-(l - 4)-d-G1cNAc (sialyl i), yS-D-Gal-(l — 4)-yJ-D-GlcNAc-(l - 6)-D-Gal (sialyl I). The CH3 of the acetamido group of Ar-acetylneuraminic acid, which is a CH2OH group in iV-glycolyl-neuraminic acid, is shown.
The initial step in the sequence of events leading to influenza virus infections in mammalian hosts is mediated by the multiple attachment of virus particles to host sialoside receptors in the nasopharynx [41]. These receptors consist largely of cell surface sialylated glycoproteins and gangliosides. The subsequent steps involve receptor-mediated endocytosis with ensuing release of the viral nucleo-plasmid. The first event responsible for the receptor-virus interaction is therefore an attractive target for both antiviral and related microbial intervention. [Pg.363]

Influenza virus particles are spheroidal and approximately 100 nm in diameter. The outer-membrane envelope contains 500 copies of hemagglutinin (HA) trimers and 100 copies of neuraminidase tetramers. The hemagglutinin constitutes the receptor sites for a-sialoside ligands. X-ray analyses show that the three sialic acid binding pockets reside 46 A apart, each trimer being separated on the virion surface by about 65-110 A [42],... [Pg.364]

Fig. 8 (top) Liposome with polydiacetylene linked monolayer mixed with ligand for receptor detection. (bottom) Colorimetric detection of influenza virus using polymerized liposomes to which have been added increasing amounts of influenza virus from left to right. [18]... [Pg.399]


See other pages where Influenza virus receptors is mentioned: [Pg.296]    [Pg.277]    [Pg.677]    [Pg.296]    [Pg.277]    [Pg.677]    [Pg.1050]    [Pg.80]    [Pg.86]    [Pg.223]    [Pg.1050]    [Pg.272]    [Pg.147]    [Pg.148]    [Pg.255]    [Pg.99]    [Pg.6]    [Pg.6]    [Pg.112]    [Pg.248]    [Pg.89]    [Pg.358]    [Pg.339]    [Pg.398]    [Pg.186]    [Pg.186]   
See also in sourсe #XX -- [ Pg.295 , Pg.296 ]




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