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


     

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
Right arrow Citation Map
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 Galindo, I.
Right arrow Articles by Carrascosa, A. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Galindo, I.
Right arrow Articles by Carrascosa, A. L.
Agricola
Right arrow Articles by Galindo, I.
Right arrow Articles by Carrascosa, A. L.
Journal of General Virology (2000), 81, 59-65.
© 2000 Society for General Microbiology

Animal: DNA Viruses

Characterization of the African swine fever virus protein p49: a new late structural polypeptide

Inmaculada Galindo1, Eladio Viñuelab,1 and Angel L. Carrascosa1

Centro de Biología Molecular ‘Severo Ochoa’ (CSIC–UAM), Universidad Autónoma de Madrid, 28049 Madrid, Spain1

Author for correspondence: Angel Carrascosa. Fax +34 91 397 47 99. e-mail acarrascosa{at}cbm.uam.es

The open reading frame B438L, located within the EcoRI B fragment of the African swine fever virus genome, is predicted to encode a protein of 438 amino acids with a molecular mass of 49·3 kDa. It presents a cell attachment RGD (Arg–Gly–Asp) motif but no other significant similarity to protein sequences in databases. Northern blot and primer extension analysis showed that B438L is transcribed only at late times during virus infection. The B438L gene product has been expressed in Escherichia coli, purified and used as an antigen for antibody production. The rabbit antiserum specific for pB438L recognized a protein of about 49 kDa in virus-infected cell extracts. This protein was synthesized late in infection by all the virus strains tested, was located in cytoplasmic virus factories and appeared as a structural component of purified virus particles.




This article has been cited by other articles:


Home page
 J. Virol.Home page
C. Epifano, J. Krijnse-Locker, M. L. Salas, J. Salas, and J. M. Rodriguez
Generation of Filamentous Instead of Icosahedral Particles by Repression of African Swine Fever Virus Structural Protein pB438L
J. Virol., December 1, 2006; 80(23): 11456 - 11466.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
A. Leitão, C. Cartaxeiro, R. Coelho, B. Cruz, R. M. E. Parkhouse, F. C. Portugal, J. D. Vigário, and C. L. V. Martins
The non-haemadsorbing African swine fever virus isolate ASFV/NH/P68 provides a model for defining the protective anti-virus immune response
J. Gen. Virol., March 1, 2001; 82(3): 513 - 523.
[Abstract] [Full Text]

Home page
 J. Virol.Home page
R. García-Escudero and E. Viñuela
Structure of African Swine Fever Virus Late Promoters: Requirement of a TATA Sequence at the Initiation Region
J. Virol., September 1, 2000; 74(17): 8176 - 8182.
[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 © 2000 by the Society for General Microbiology.