Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (17)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Smith, B. J.
Right arrow Articles by Colman, P. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smith, B. J.
Right arrow Articles by Colman, P. M.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 15, No. 5, 365-371, May 2002
© 2002 Oxford University Press

Modelling the structure of the fusion protein from human respiratory syncytial virus

Brian J. Smith,1,2, Michael C. Lawrence,3 and Peter M. Colman,1

Biomolecular Research Institute, 343 Royal Parade, Parkville, Victoria 3052, Australia

The fusion protein of respiratory syncytial virus (RSV-F) is responsible for fusion of virion with host cells and infection of neighbouring cells through the formation of syncytia. A three-dimensional model structure of RSV-F was derived by homology modelling from the structure of the equivalent protein in Newcastle disease virus (NDV). Despite very low sequence homology between the two structures, most features of the model appear to have high credibility, although a few small regions in RSV-F whose secondary structure is predicted to be different to that in NDV are likely to be poorly modelled. The organization of individual residues identified in escape mutants against monoclonal antibodies correlates well with known antigenic sites. The location of residues involved in point mutations in several drug-resistant variants is also examined.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Gen. Virol.Home page
N. D. Ulbrandt, H. Ji, N. K. Patel, A. S. Barnes, S. Wilson, P. A. Kiener, J. Suzich, and M. P. McCarthy
Identification of antibody neutralization epitopes on the fusion protein of human metapneumovirus
J. Gen. Virol., December 1, 2008; 89(12): 3113 - 3118.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. K. Lee, A. Prussia, T. Paal, L. K. White, J. P. Snyder, and R. K. Plemper
Functional Interaction between Paramyxovirus Fusion and Attachment Proteins
J. Biol. Chem., June 13, 2008; 283(24): 16561 - 16572.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
C. Deffrasnes, M.-E. Hamelin, G. A. Prince, and G. Boivin
Identification and Evaluation of a Highly Effective Fusion Inhibitor for Human Metapneumovirus
Antimicrob. Agents Chemother., January 1, 2008; 52(1): 279 - 287.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
S. A. Miller, S. Tollefson, J. E. Crowe Jr., J. V. Williams, and D. W. Wright
Examination of a Fusogenic Hexameric Core from Human Metapneumovirus and Identification of a Potent Synthetic Peptide Inhibitor from the Heptad Repeat 1 Region
J. Virol., January 1, 2007; 81(1): 141 - 149.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
S. Biacchesi, Q. N. Pham, M. H. Skiadopoulos, B. R. Murphy, P. L. Collins, and U. J. Buchholz
Modification of the Trypsin-Dependent Cleavage Activation Site of the Human Metapneumovirus Fusion Protein To Be Trypsin Independent Does Not Increase Replication or Spread in Rodents or Nonhuman Primates.
J. Virol., June 1, 2006; 80(12): 5798 - 5806.
[Abstract] [Full Text] [PDF]


Home page
J. Gen. Virol.Home page
P. J. Branigan, N. D. Day, C. Liu, L. L. Gutshall, J. A. Melero, R. T. Sarisky, and A. M. D. Vecchio
The cytoplasmic domain of the F protein of Human respiratory syncytial virus is not required for cell fusion
J. Gen. Virol., February 1, 2006; 87(2): 395 - 398.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
J. L. Douglas, M. L. Panis, E. Ho, K.-Y. Lin, S. H. Krawczyk, D. M. Grant, R. Cai, S. Swaminathan, X. Chen, and T. Cihlar
Small Molecules VP-14637 and JNJ-2408068 Inhibit Respiratory Syncytial Virus Fusion by Similar Mechanisms
Antimicrob. Agents Chemother., June 1, 2005; 49(6): 2460 - 2466.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
C. Cianci, D. R. Langley, D. D. Dischino, Y. Sun, K.-L. Yu, A. Stanley, J. Roach, Z. Li, R. Dalterio, R. Colonno, et al.
Targeting a binding pocket within the trimer-of-hairpins: Small-molecule inhibition of viral fusion
PNAS, October 19, 2004; 101(42): 15046 - 15051.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
C. Cianci, K.-L. Yu, K. Combrink, N. Sin, B. Pearce, A. Wang, R. Civiello, S. Voss, G. Luo, K. Kadow, et al.
Orally Active Fusion Inhibitor of Respiratory Syncytial Virus
Antimicrob. Agents Chemother., February 1, 2004; 48(2): 413 - 422.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
J. L. Douglas, M. L. Panis, E. Ho, K.-Y. Lin, S. H. Krawczyk, D. M. Grant, R. Cai, S. Swaminathan, and T. Cihlar
Inhibition of Respiratory Syncytial Virus Fusion by the Small Molecule VP-14637 via Specific Interactions with F Protein
J. Virol., May 1, 2003; 77(9): 5054 - 5064.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
A. Yamaguchi, M. Iwadate, E.-i. Suzuki, K. Yura, S. Kawakita, H. Umeyama, and M. Go
Enlarged FAMSBASE: protein 3D structure models of genome sequences for 41 species
Nucleic Acids Res., January 1, 2003; 31(1): 463 - 468.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.