This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dormitzer, P. R.
Right arrow Articles by Harrison, S. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dormitzer, P. R.
Right arrow Articles by Harrison, S. C.

 Previous Article  |  Next Article 

Journal of Virology, October 2002, p. 10512-10517, Vol. 76, No. 20
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.20.10512-10517.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Specificity and Affinity of Sialic Acid Binding by the Rhesus Rotavirus VP8* Core

Philip R. Dormitzer,1* Zhen-Yu J. Sun,2 Ola Blixt,3 James C. Paulson,3 Gerhard Wagner,2 and Stephen C. Harrison1,4

Laboratory of Molecular Medicine, Children's Hospital,1 Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115,2 Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037,3 Howard Hughes Medical Institute and Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 021384

Received 7 March 2002/ Accepted 2 July 2002

Nuclear magnetic resonance spectroscopy demonstrates that the rhesus rotavirus hemagglutinin specifically binds {alpha}-anomeric N-acetylneuraminic acid with a Kd of 1.2 mM. The hemagglutinin requires no additional carbohydrate moieties for binding, does not distinguish 3' from 6' sialyllactose, and has approximately tenfold lower affinity for N-glycolylneuraminic than for N-acetylneuraminic acid. The broad specificity and low affinity of sialic acid binding by the rotavirus hemagglutinin are consistent with this interaction mediating initial cell attachment prior to the interactions that determine host range and cell type specificity.

* Corresponding author. Mailing address: Laboratory of Molecular Medicine, Enders 673, Children's Hospital, 320 Longwood Ave., Boston, MA 02115. Phone: (617) 355-3026. Fax: (617) 738-0184. E-mail: dormitze{at}crystal.harvard.edu.

Journal of Virology, October 2002, p. 10512-10517, Vol. 76, No. 20
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.20.10512-10517.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Haselhorst, T., Blanchard, H., Frank, M., Kraschnefski, M. J., Kiefel, M. J., Szyczew, A. J., Dyason, J. C., Fleming, F., Holloway, G., Coulson, B. S., von Itzstein, M. (2007). STD NMR spectroscopy and molecular modeling investigation of the binding of N-acetylneuraminic acid derivatives to rhesus rotavirus VP8* core. Glycobiology 17: 68-81 [Abstract] [Full Text]  
  • Lopez, J. A., Maldonado, A. J., Gerder, M., Abanero, J., Murgich, J., Pujol, F. H., Liprandi, F., Ludert, J. E. (2005). Characterization of Neuraminidase-Resistant Mutants Derived from Rotavirus Porcine Strain OSU. J. Virol. 79: 10369-10375 [Abstract] [Full Text]  
  • Moustafa, I., Connaris, H., Taylor, M., Zaitsev, V., Wilson, J. C., Kiefel, M. J., von Itzstein, M., Taylor, G. (2004). Sialic Acid Recognition by Vibrio cholerae Neuraminidase. J. Biol. Chem. 279: 40819-40826 [Abstract] [Full Text]  
  • Burmeister, W. P., Guilligay, D., Cusack, S., Wadell, G., Arnberg, N. (2004). Crystal Structure of Species D Adenovirus Fiber Knobs and Their Sialic Acid Binding Sites. J. Virol. 78: 7727-7736 [Abstract] [Full Text]  
  • Haddad, A., Nokhbeh, M. R., Alexander, D. A., Dawe, S. J., Grise, C., Gulzar, N., Dimock, K. (2004). Binding to Decay-Accelerating Factor Is Not Required for Infection of Human Leukocyte Cell Lines by Enterovirus 70. J. Virol. 78: 2674-2681 [Abstract] [Full Text]  
  • Graham, K. L., Halasz, P., Tan, Y., Hewish, M. J., Takada, Y., Mackow, E. R., Robinson, M. K., Coulson, B. S. (2003). Integrin-Using Rotaviruses Bind {alpha}2{beta}1 Integrin {alpha}2 I Domain via VP4 DGE Sequence and Recognize {alpha}X{beta}2 and {alpha}V{beta}3 by Using VP7 during Cell Entry. J. Virol. 77: 9969-9978 [Abstract] [Full Text]  
  • Londrigan, S. L., Graham, K. L., Takada, Y., Halasz, P., Coulson, B. S. (2003). Monkey Rotavirus Binding to {alpha}2{beta}1 Integrin Requires the {alpha}2 I Domain and Is Facilitated by the Homologous {beta}1 Subunit. J. Virol. 77: 9486-9501 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»