Browse by author
Lookup NU author(s): Professor Debra Bevitt, Emeritus Professor Geoffrey Toms
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
The fusion glycoprotein, F, of human respiratory syncytial virus is a principal target of neutralising antibodies and an important protective immunogen. Among sub-group A strains of the virus the F gene is highly conserved. A comparison of F gene sequences of two sub-group B strains, 8/60 and 18537, indicates that the gene also is conserved within this sub-group. However, both limited sequence variability and antigenic variation occurs between F genes from different virus sub-groups. Such variability may be important in the failure of natural- and vaccine-induced immunity and it is thus important to identify the variable epitopes. Three anti-F MAbs exhibiting sub-group specific neutralisation and binding to recombinant F glycoprotein were studied. Comparison of A2 and 8/60 F gene sequences revealed 64 predicted varient amino acids. In order to map the variant amino acids responsible for sub-group specific binding, three sets of chimaeric genes, in which different domains of A2 and 8/60 F were exchanged, were created and expressed. Sub-group specificity mapped to the N-terminal region of F1 for two MAbs (RS2B8 and RS348) and to the C-terminal region for the third. By using site-directed mutagenesis, sub-group specific binding of MAbs RS2B8 and RS348 was attributed to a predicted loop region between residues 200 and 216. This loop carried four residues variant between the sub-groups. Change of at least two was necessary to abrogate MAb binding. © 2001 Wiley-Liss, Inc.
Author(s): Connor AL, Bevitt DJ, Toms GL
Publication type: Article
Publication status: Published
Journal: Journal of Medical Virology
Year: 2001
Volume: 63
Issue: 2
Pages: 168-177
ISSN (print): 0146-6615
ISSN (electronic): 1096-9071
Publisher: John Wiley & Sons, Inc.
URL: http://dx.doi.org/10.1002/1096-9071(20000201)63:2<168::AID-JMV1012>3.0.CO;2-U
DOI: 10.1002/1096-9071(20000201)63:2<168::AID-JMV1012>3.0.CO;2-U
PubMed id: 11170054
Altmetrics provided by Altmetric