scholarly journals The Amino-terminal Immunoglobulin-like Domain of Sialoadhesin Contains the Sialic Acid Binding Site

1995 ◽  
Vol 270 (44) ◽  
pp. 26184-26191 ◽  
Author(s):  
Deepa Nath ◽  
P. Anton van der Merwe ◽  
Sørge Kelm ◽  
Paul Bradfield ◽  
Paul R. Crocker
Keyword(s):  
Sialic Acid ◽  
Binding Site ◽  
Amino Terminal ◽  
Sialic Acid Binding

scholarly journals Neutrophils do not bind to or phagocytize human immune complexes formed with influenza virus

Blood ◽  
1993 ◽  
Vol 82 (5) ◽  
pp. 1639-1646 ◽  
Author(s):  
DR Ratcliffe ◽  
J Michl ◽  
EB Cramer
Keyword(s):  
Influenza Virus ◽  
Sialic Acid ◽  
Epithelial Cells ◽  
Binding Site ◽  
Immune Complexes ◽  
Human Neutrophils ◽  
Sialic Acid Binding ◽  
Infected Cells ◽  
Neutrophil Adherence ◽  
Human Immune

Abstract Neutrophils appear to form the first line of defense against influenza virus, yet it is unclear how these leukocytes recognize influenza- infected cells. While demonstrating that neutrophils adhere specifically to the sialic acid-binding site on the hemagglutinin molecule (HA) on the surface of influenza-infected (WSN[H1N1]) epithelial cells and not to other viral or epithelial cell antigens, it was observed that human neutrophils do not recognize immune complexes formed with influenza virus. Intact antibodies (mouse monoclonal antibodies [MoAbs] IgG1 and IgG2b, human immune heat-inactivated serum [predominantly IgG1], and IgG purified from human immune serum) that block the sialic acid-binding site on HA significantly reduced (> 80%) neutrophil adherence to influenza-infected epithelial cells. Binding and phagocytosis of free influenza virions and neutrophil agglutination by influenza virus were completely prevented by these antibodies. Intact and F(ab')2 fragments of mouse MoAbs to other viral epitopes caused increased neutrophil adherence to infected cells. This binding was eliminated by F(ab'2) fragments of MoAbs against the sialic acid- binding site on HA, but not by saturating amounts of MoAbs, which block the neutrophil Fc receptors. Thus, it appears that human neutrophils show little ability to bind via their Fc receptors to the immune complexes formed with antibody and either influenza-infected epithelial cells or the free virion. These findings are in contrast to the general dogma, and are the first example of antibody opsonization reducing, rather than enhancing, neutrophil binding and phagocytosis of a pathogen.

A Secondary Sialic Acid Binding Site on Influenza Virus Neuraminidase: Fact or Fiction?

2012 ◽  
Vol 51 (9) ◽  
pp. 2221-2224 ◽  
Author(s):  
Jimmy C. C. Lai ◽  
Jean-Michel Garcia ◽  
Jeffrey C. Dyason ◽  
Raphael Böhm ◽  
Paul D. Madge ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Sialic Acid ◽  
Binding Site ◽  
Sialic Acid Binding ◽  
Influenza Virus Neuraminidase

scholarly journals Characterization of the Sialic Acid-binding Site in Sialoadhesin by Site-directed Mutagenesis

1996 ◽  
Vol 271 (16) ◽  
pp. 9267-9272 ◽  
Author(s):  
Mary Vinson ◽  
P. Anton van der Merwe ◽  
Sørge Kelm ◽  
Andy May ◽  
E. Yvonne Jones ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Binding Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Sialic Acid Binding

scholarly journals Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases

1997 ◽  
Vol 94 (22) ◽  
pp. 11808-11812 ◽  
Author(s):  
J. N. Varghese ◽  
P. M. Colman ◽  
A. van Donkelaar ◽  
T. J. Blick ◽  
A. Sahasrabudhe ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Sialic Acid ◽  
Avian Influenza ◽  
Avian Influenza Virus ◽  
Binding Site ◽  
Sialic Acid Binding

scholarly journals Localization of the Putative Sialic Acid-binding Site on the Immunoglobulin Superfamily Cell-surface Molecule CD22

1996 ◽  
Vol 271 (16) ◽  
pp. 9273-9280 ◽  
Author(s):  
P. Anton van der Merwe ◽  
Paul R. Crocker ◽  
Mary Vinson ◽  
A. Neil Barclay ◽  
Roland Schauer ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Cell Surface ◽  
Binding Site ◽  
Immunoglobulin Superfamily ◽  
Surface Molecule ◽  
Cell Surface Molecule ◽  
Sialic Acid Binding

scholarly journals Structures of Merkel Cell Polyomavirus VP1 Complexes Define a Sialic Acid Binding Site Required for Infection

2012 ◽  
Vol 8 (7) ◽  
pp. e1002738 ◽  
Author(s):  
Ursula Neu ◽  
Holger Hengel ◽  
Bärbel S. Blaum ◽  
Rachel M. Schowalter ◽  
Dennis Macejak ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Binding Site ◽  
Merkel Cell Polyomavirus ◽  
Merkel Cell ◽  
Sialic Acid Binding

scholarly journals Siglec-7 Undergoes a Major Conformational Change When Complexed with the α(2,8)-Disialylganglioside GT1b

2006 ◽  
Vol 281 (43) ◽  
pp. 32774-32783 ◽  
Author(s):  
Helen Attrill ◽  
Akihiro Imamura ◽  
Ritu S. Sharma ◽  
Makoto Kiso ◽  
Paul R. Crocker ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Immune System ◽  
Sialic Acid ◽  
Binding Site ◽  
Structural Data ◽  
Site Structure ◽  
Sialic Acid Binding ◽  
Structural Template ◽  
Polar Interactions ◽  
Ganglioside Gt1b

The siglecs are a group of mammalian sialic acid binding receptors expressed predominantly in the immune system. The CD33-related siglecs show complex recognition patterns for sialylated glycans. Siglec-7 shows a preference for α(2,8)-disialylated ligands and provides a structural template for studying the key interactions that drive this selectivity. We have co-crystallized Siglec-7 with a synthetic oligosaccharide corresponding to the α(2,8)-disialylated ganglioside GT1b. The crystal structure of the complex offers a first glimpse into how this important family of lectins binds the structurally diverse gangliosides. The structure reveals that the C-C′ loop, a region implicated in previous studies as driving siglec specificity, undergoes a dramatic conformational shift, allowing it to interact with the underlying neutral glycan core of the ganglioside. The structural data in combination with mutagenesis studies show that binding of the ganglioside is driven by extensive hydrophobic contacts together with key polar interactions and that the binding site structure is complementary to preferred solution conformations of GT1b.

scholarly journals Second Sialic Acid Binding Site in Newcastle Disease Virus Hemagglutinin-Neuraminidase: Implications for Fusion

2004 ◽  
Vol 78 (7) ◽  
pp. 3733-3741 ◽  
Author(s):  
Viatcheslav Zaitsev ◽  
Mark von Itzstein ◽  
Darrin Groves ◽  
Milton Kiefel ◽  
Toru Takimoto ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Newcastle Disease Virus ◽  
Binding Site ◽  
Disease Virus ◽  
Newcastle Disease ◽  
Surface Glycoprotein ◽  
Crystal Forms ◽  
Sialic Acid Receptors ◽  
Sialic Acid Binding ◽  
Infected Cells

ABSTRACT Paramyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein, the hemagglutinin-neuraminidase (HN), that is involved in attachment to sialic acid receptors, promotion of fusion, and removal of sialic acid from infected cells and progeny virions. Previously we showed that Newcastle disease virus (NDV) HN contained a pliable sialic acid recognition site that could take two states, a binding state and a catalytic state. Here we present evidence for a second sialic acid binding site at the dimer interface of HN and present a model for its involvement in cell fusion. Three different crystal forms of NDV HN now reveal identical tetrameric arrangements of HN monomers, perhaps indicative of the tetramer association found on the viral surface.

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