J Gen Virol Email Content Delivery
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Gen Virol 73 (1992), 1471-1479; DOI 10.1099/0022-1317-73-6-1471
© 1992 Society for General Microbiology

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 Carstens, E. B.
Right arrow Articles by Partington, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Carstens, E. B.
Right arrow Articles by Partington, S.
Agricola
Right arrow Articles by Carstens, E. B.
Right arrow Articles by Partington, S.

Analysis of polyhedra morphology mutants of Autographa californica nuclear polyhedrosis virus: molecular and ultrastructural features

Eric B. Carstens, Greg V. Williams, Peter Faulkner and Stephen Partington

Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada K7L 3N6

Two new mutants of Autographa californica multiple nuclear polyhedrosis virus affected in the morphogenesis of their polyhedra, designated M276 and M934, were investigated. Marker transfer experiments demonstrated that the observed phenotype was due exclusively to alterations in the polyhedrin gene. M276 contained a 229 base insertion near the carboxyl terminus coding region which resulted in synthesis of a truncated protein; M934 had a point mutation substituting phenylalanine for leucine at amino acid 183. Both mutations occurred in highly conserved regions of the protein and prevented the occlusion of virus particles, but did not affect targeting for the intranuclear ring zone. M276 was distinct in that it had prominent cytosolic condensations of polyhedrin, although these were probably due to decreased protein solubility. M934 polyhedrin condensations associated prematurely with calyx material such that it became incorporated into the condensation rather than at the surface. Results confirm that occlusion size and shape are features inherent to the polyhedrin protein, and suggest that polyhedrin conformation may help regulate the occlusion process.

Received 18 December 1991; accepted 4 February 1992.


This article has been cited by other articles:


Home page
J. Gen. Virol.Home page
Z Hu, T Luijckx, L. van Dinten, M. van Oers, J. Hajos, F. Bianchi, J. van Lent, D Zuidema, and J. Vlak
Specificity of polyhedrin in the generation of baculovirus occlusion bodies
J. Gen. Virol., April 1, 1999; 80(4): 1045 - 1053.
[Abstract]


Home page
J. Virol.Home page
J. E. Eason, R. H. Hice, J. J. Johnson, and B. A. Federici
Effects of Substituting Granulin or a Granulin-Polyhedrin Chimera for Polyhedrin on Virion Occlusion and Polyhedral Morphology in Autographa californica Multinucleocapsid Nuclear Polyhedrosis Virus
J. Virol., July 1, 1998; 72(7): 6237 - 6243.
[Abstract] [Full Text] [PDF]




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 © 1992 by the Society for General Microbiology.