Glycosylation is not necessary for recognition of the fusion glycoprotein domain of the Human respiratory syncytial virus by a polyclonal antibody

2010 ◽  
Vol 54 (3) ◽  
pp. 181-187 ◽  
Author(s):  
S. HE. Lim ◽  
F. Jahanshiri ◽  
F. A. Jalilian ◽  
R. A. Rahim ◽  
Z. Sekawi ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Polyclonal Antibody ◽  
Human Respiratory Syncytial Virus ◽  
Fusion Glycoprotein ◽  
Syncytial Virus

scholarly journals Fatty Acid Acylation of the Fusion Glycoprotein of Human Respiratory Syncytial Virus

1989 ◽  
Vol 264 (18) ◽  
pp. 10339-10342
Author(s):  
R G Arumugham ◽  
R C Seid ◽  
S Doyle ◽  
S W Hildreth ◽  
P R Paradiso
Keyword(s):  
Fatty Acid ◽  
Respiratory Syncytial Virus ◽  
Human Respiratory Syncytial Virus ◽  
Fusion Glycoprotein ◽  
Syncytial Virus

scholarly journals Trivalency of a Nanobody Specific for the Human Respiratory Syncytial Virus Fusion Glycoprotein Drastically Enhances Virus Neutralization and Impacts Escape Mutant Selection

2016 ◽  
Vol 60 (11) ◽  
pp. 6498-6509 ◽  
Author(s):  
Concepción Palomo ◽  
Vicente Mas ◽  
Laurent Detalle ◽  
Erik Depla ◽  
Olga Cano ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Antigenic Site ◽  
Serial Passage ◽  
Human Respiratory Syncytial Virus ◽  
Escape Mutant ◽  
Comprehensive Description ◽  
Mutant Selection ◽  
Fusion Glycoprotein ◽  
Escape Mutants ◽  
Syncytial Virus

ABSTRACTALX-0171 is a trivalent Nanobody derived from monovalent Nb017 that binds to antigenic site II of the human respiratory syncytial virus (hRSV) fusion (F) glycoprotein. ALX-0171 is about 6,000 to 10,000 times more potent than Nb017 in neutralization tests with strains of hRSV antigenic groups A and B. To explore the effect of this enhanced neutralization on escape mutant selection, viruses resistant to either ALX-0171 or Nb017 were isolated after serial passage of the hRSV Long strain in the presence of suboptimal concentrations of the respective Nanobodies. Resistant viruses emerged notably faster with Nb017 than with ALX-0171 and in both cases contained amino acid changes in antigenic site II of hRSV F. Detailed binding and neutralization analyses of these escape mutants as well as previously described mutants resistant to certain monoclonal antibodies (MAbs) offered a comprehensive description of site II mutations which are relevant for neutralization by MAbs and Nanobodies. Notably, ALX-0171 showed a sizeable neutralization potency with most escape mutants, even with some of those selected with the Nanobody, and these findings make ALX-0171 an attractive antiviral for treatment of hRSV infections.

scholarly journals The Fusion Glycoprotein of Human Respiratory Syncytial Virus Facilitates Virus Attachment and Infectivity via an Interaction with Cellular Heparan Sulfate

2000 ◽  
Vol 74 (14) ◽  
pp. 6442-6447 ◽  
Author(s):  
Steven A. Feldman ◽  
Susette Audet ◽  
Judy A. Beeler
Keyword(s):  
Respiratory Syncytial Virus ◽  
Heparan Sulfate ◽  
Specific Activity ◽  
Recombinant Vaccinia Virus ◽  
Enzymatic Digestion ◽  
Human Respiratory Syncytial Virus ◽  
Virus Binding ◽  
Virus Attachment ◽  
Fusion Glycoprotein ◽  
Syncytial Virus

ABSTRACT Human respiratory syncytial virus (RSV) F glycoprotein (RSV-F) can independently interact with immobilized heparin and facilitate both attachment to and infection of cells via an interaction with cellular heparan sulfate. RSV-glycosaminoglycan (GAG) interactions were evaluated using heparin-agarose affinity chromatography. RSV-F from A2- and B1/cp-52 (cp-52)-infected cell lysates, RSV-F derived from a recombinant vaccinia virus, and affinity-purified F protein all bound to and were specifically eluted from heparin columns. In infectivity inhibition studies, soluble GAGs decreased the infectivity of RSV A2 and cp-52, with bovine lung heparin exhibiting the highest specific activity against both A2 (50% effective dose [ED50] = 0.28 ± 0.11 μg/ml) andcp-52 (ED50 = 0.55 ± 0.14 μg/ml). Furthermore, enzymatic digestion of cell surface GAGs by heparin lyase I and heparin lyase III but not chondroitinase ABC resulted in a significant reduction in cp-52 infectivity. Moreover, bovine lung heparin inhibited radiolabeled A2 and cp-52 virus binding up to 90%. Taken together, these data suggest that RSV-F independently interacts with heparin/heparan sulfate and this type of interaction facilitates virus attachment and infectivity.

scholarly journals Identification of Linear Heparin-Binding Peptides Derived from Human Respiratory Syncytial Virus Fusion Glycoprotein That Inhibit Infectivity

2006 ◽  
Vol 81 (1) ◽  
pp. 261-271 ◽  
Author(s):  
Roberta L. Crim ◽  
Susette A. Audet ◽  
Steven A. Feldman ◽  
Howard S. Mostowski ◽  
Judy A. Beeler
Keyword(s):  
Respiratory Syncytial Virus ◽  
Cell Surface ◽  
A549 Cells ◽  
Vero Cells ◽  
Human Respiratory Syncytial Virus ◽  
Virus Infectivity ◽  
Heparin Binding ◽  
The Third ◽  
Fusion Glycoprotein ◽  
Syncytial Virus

ABSTRACT It has been shown previously that the fusion glycoprotein of human respiratory syncytial virus (RSV-F) interacts with cellular heparan sulfate. Synthetic overlapping peptides derived from the F-protein sequence of RSV subtype A (strain A2) were tested for their ability to bind heparin using heparin-agarose affinity chromatography (HAAC). This evaluation identified 15 peptides representing eight linear heparin-binding domains (HBDs) located within F1 and F2 and spanning the protease cleavage activation site. All peptides bound to Vero and A549 cells, and binding was inhibited by soluble heparins and diminished by either enzymatic treatment to remove cell surface glycosaminoglycans or by treatment with sodium chlorate to decrease cellular sulfation. RSV-F HBD peptides were less likely to bind to glycosaminoglycan-deficient CHO-745 cells than parental CHO-K1 cells that express these molecules. Three RSV-F HBD peptides (F16, F26, and F55) inhibited virus infectivity; two of these peptides (F16 and F55) inhibited binding of virus to Vero cells, while the third (F26) did not. These studies provided evidence that two of the linear HBDs mapped by peptides F16 and F55 may mediate one of the first steps in the attachment of virus to cells while the third, F26, inhibited infectivity at a postattachment step, suggesting that interactions with cell surface glycosaminoglycans may play a role in infectivity of some RSV strains.

scholarly journals Antigenic Structure of Human Respiratory Syncytial Virus Fusion Glycoprotein

1998 ◽  
Vol 72 (8) ◽  
pp. 6922-6928 ◽  
Author(s):  
Juan A. López ◽  
Regla Bustos ◽  
Claes Örvell ◽  
Mabel Berois ◽  
Juan Arbiza ◽  
...  
Keyword(s):  
Respiratory Syncytial Virus ◽  
Protein Sequence ◽  
Neutralizing Antibodies ◽  
Human Respiratory Syncytial Virus ◽  
Antigenic Structure ◽  
Antigenic Sites ◽  
Fusion Glycoprotein ◽  
Escape Mutants ◽  
Syncytial Virus ◽  
Prediction Of Secondary Structure

ABSTRACT New series of escape mutants of human respiratory syncytial virus were prepared with monoclonal antibodies specific for the fusion (F) protein. Sequence changes selected in the escape mutants identified two new antigenic sites (V and VI) recognized by neutralizing antibodies and a group-specific site (I) in the F1 chain of the F molecule. The new epitopes, and previously identified antigenic sites, were incorporated into a refined prediction of secondary-structure motifs to generate a detailed antigenic map of the F glycoprotein.

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