J Gen Virol Try Microbiology Online
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
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 Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bupp, K.
Right arrow Articles by Gonzalez-Scarano, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bupp, K.
Right arrow Articles by Gonzalez-Scarano, F.
Agricola
Right arrow Articles by Bupp, K.
Right arrow Articles by Gonzalez-Scarano, F.

Journal of General Virology, Vol 79, 667-671, Copyright © 1998 by Society for General Microbiology


ARTICLES

Pseudotype formation with La Crosse virus glycoproteins

K Bupp and F Gonzalez-Scarano
Department of Microbiology, University of Pennsylvania Medical Center, Philadelphia 19104-6146, USA.

Pseudotype formation is a powerful tool for analysing mechanisms of virus neutralization and entry, since it allows for analysis of glycoprotein properties without the necessity for preparing recombinant genomes. Using recombinant vaccinia viruses, we prepared pseudotypes of La Crosse virus with recombinant glycoproteins cloned from the monoclonal antibody (MAb)-resistant variant V31. The resulting pseudotypes became partially resistant to MAb 807-31. Furthermore, when the V31 glycoproteins were incorporated into a second MAb-resistant variant (V33), the pseudotyped virus became sensitive to neutralization by the MAb (807-33) originally used in its selection. These results suggest a simple technique for the incorporation of glycoprotein mutations into bunyaviruses, allowing analysis of mechanisms of neutralization and other virus entry functions.


This article has been cited by other articles:


Home page
J. Gen. Virol.Home page
T. Briese, A. Rambaut, and W. I. Lipkin
Analysis of the medium (M) segment sequence of Guaroa virus and its comparison to other orthobunyaviruses
J. Gen. Virol., October 1, 2004; 85(10): 3071 - 3077.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
O. Vapalahti, A. Lundkvist, V. Fedorov, C. J. Conroy, S. Hirvonen, A. Plyusnina, K. Nemirov, K. Fredga, J. A. Cook, J. Niemimaa, et al.
Isolation and Characterization of a Hantavirus from Lemmus sibiricus: Evidence for Host Switch during Hantavirus Evolution
J. Virol., July 1, 1999; 73(7): 5586 - 5592.
[Abstract] [Full Text]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1998 by the Society for General Microbiology.