| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Animal: DNA Viruses |
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK1
Author for correspondence: Geoffrey L. Smith. Present address: The Wright–Fleming Institute, Imperial College School of Medicine, St Mary’s Campus, Norfolk Place, London W2 1PG, UK. Fax +44 207 594 3973. e-mail glsmith{at}ic.ac.uk
A mutational analysis of the vaccinia virus (VV) B5R protein is presented. This protein is related to the regulators of complement activation (RCA) superfamily, has four short consensus repeats (SCRs) that are typical of this superfamily and is present on extracellular enveloped virus (EEV) particles. Here we have constructed VV mutants in which the cytoplasmic tail (CT) of the B5R protein is progressively truncated, and domains of the B5R protein [the SCR (short consensus repeat) domains, the transmembrane anchor region or the CT] are substituted by corresponding domains from the VV haemagglutinin (HA), another EEV protein. Analysis of these mutant viruses showed that loss of the B5R CT did not affect the formation of intracellular enveloped virus (IEV), actin tails, EEV or virus plaque size. However, if the SCR domains of the B5R protein were replaced by the corresponding region of the HA, the virus plaque size was diminished, the formation of actin tails was decreased severely and the titre of infectious EEV released from cells was reduced approximately 25-fold compared to wild-type virus and 5-fold compared to a virus lacking the entire B5R gene. Thus the linkage of HA to the B5R transmembrane and CT is deleterious for the formation and release of EEV and for cell-to-cell virus spread. In contrast, deletion or substitution of the B5R CT did not affect virus replication, although the amount of cell surface B5R was reduced compared to control.
This article has been cited by other articles:
|
|
 |
|
  K. L. Roberts, A. Breiman, G. C. Carter, H. A. Ewles, M. Hollinshead, M. Law, and G. L. Smith Acidic residues in the membrane-proximal stalk region of vaccinia virus protein B5 are required for glycosaminoglycan-mediated disruption of the extracellular enveloped virus outer membrane J. Gen. Virol., July 1, 2009; 90(7): 1582 - 1591. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. H. Kirn, Y. Wang, W. Liang, C. H. Contag, and S. H. Thorne Enhancing Poxvirus Oncolytic Effects through Increased Spread and Immune Evasion Cancer Res., April 1, 2008; 68(7): 2071 - 2075. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. K. Earley, W. M. Chan, and B. M. Ward The Vaccinia Virus B5 Protein Requires A34 for Efficient Intracellular Trafficking from the Endoplasmic Reticulum to the Site of Wrapping and Incorporation into Progeny Virions J. Virol., March 1, 2008; 82(5): 2161 - 2169. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. Perdiguero, M. M. Lorenzo, and R. Blasco Vaccinia Virus A34 Glycoprotein Determines the Protein Composition of the Extracellular Virus Envelope J. Virol., March 1, 2008; 82(5): 2150 - 2160. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
B. Perdiguero and R. Blasco Interaction between Vaccinia Virus Extracellular Virus Envelope A33 and B5 Glycoproteins. J. Virol., September 1, 2006; 80(17): 8763 - 8777. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Aldaz-Carroll, J. C. Whitbeck, M. Ponce de Leon, H. Lou, L. Hirao, S. N. Isaacs, B. Moss, R. J. Eisenberg, and G. H. Cohen Epitope-Mapping Studies Define Two Major Neutralization Sites on the Vaccinia Virus Extracellular Enveloped Virus Glycoprotein B5R J. Virol., May 15, 2005; 79(10): 6260 - 6271. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Katz, B. M. Ward, A. S. Weisberg, and B. Moss Mutations in the Vaccinia Virus A33R and B5R Envelope Proteins That Enhance Release of Extracellular Virions and Eliminate Formation of Actin-Containing Microvilli without Preventing Tyrosine Phosphorylation of the A36R Protein J. Virol., November 15, 2003; 77(22): 12266 - 12275. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. L. Smith, A. Vanderplasschen, and M. Law The formation and function of extracellular enveloped vaccinia virus J. Gen. Virol., December 1, 2002; 83(12): 2915 - 2931. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Katz, E. Wolffe, and B. Moss Identification of Second-Site Mutations That Enhance Release and Spread of Vaccinia Virus J. Virol., October 11, 2002; 76(22): 11637 - 11644. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
O. Krauss, R. Hollinshead, M. Hollinshead, and G. L. Smith An investigation of incorporation of cellular antigens into vaccinia virus particles J. Gen. Virol., October 1, 2002; 83(10): 2347 - 2359. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Gubser and G. L. Smith The sequence of camelpox virus shows it is most closely related to variola virus, the cause of smallpox J. Gen. Virol., April 1, 2002; 83(4): 855 - 872. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Rodger and G. L. Smith Replacing the SCR domains of vaccinia virus protein B5R with EGFP causes a reduction in plaque size and actin tail formation but enveloped virions are still transported to the cell surface J. Gen. Virol., February 1, 2002; 83(2): 323 - 332. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. van Eijl, M. Hollinshead, G. Rodger, W.-H. Zhang, and G. L. Smith The vaccinia virus F12L protein is associated with intracellular enveloped virus particles and is required for their egress to the cell surface J. Gen. Virol., January 1, 2002; 83(1): 195 - 207. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Law, R. Hollinshead, and G. L. Smith Antibody-sensitive and antibody-resistant cell-to-cell spread by vaccinia virus: role of the A33R protein in antibody-resistant spread J. Gen. Virol., January 1, 2002; 83(1): 209 - 222. [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 | |
