HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Rees, P. J. Articles by Dimmock, N. J. Search for Related Content PubMed PubMed Citation Articles by Rees, P. J. Articles by Dimmock, N. J. Agricola Articles by Rees, P. J. Articles by Dimmock, N. J.

Kinetics of Synthesis of Influenza Virus Ribonucleoprotein Structures

Department of Biological Sciences University of Warwick, Coventry, CV4 7AL, U.K.

The synthesis of influenza virus ribonucleoprotein structures (RNPs) in infected chick embryo cells was analysed by polyacrylamide gel electrophoresis (PAGE) in the presence of sodium deoxycholate which resolves the RNPs into five size classes. A relatively small proportion of total RNPs accumulated in the nucleus but free NP protein was found there in large amounts over the period 1.5 to 4 h post-infection. In contrast, by 4 h post-infection, all cytoplasmic NP was complexed into RNP structures. At early times, during a 15 min pulse of [³⁵S]methionine, nearly all the newly synthesized NP was incorporated into RNPs but by 4 h the majority of pulse-labelled NP was present as free protein. However, the proportion of free NP:NP in RNPs remained constant over the 1.5 to 4 h post-infection period, indicating that there was a delay before the NP synthesized later in infection was assembled into RNP structures. Individual RNP size classes were predominantly cytoplasmic and accumulated at similar rates but were not produced in equimolar amounts. The rates of synthesis of individual RNPs were in general agreement with their rates of accumulation with the remarkable exception of RNP d (containing RNA 7, the matrix protein gene). This was synthesized nearly 10-fold faster but accumulated at the same rate as the other RNPs. Possibly RNP d is more rapidly degraded than the other RNPs.

Keywords: influenza virus, ribonucleoprotein synthesis, nucleus & cytoplasm, electrophoresis of RNPs

Received 3 September 1981; accepted 17 November 1981.

This article has been cited by other articles:

				E. K.-W. Hui, D. F. Smee, M.-H. Wong, and D. P. Nayak Mutations in Influenza Virus M1 CCHH, the Putative Zinc Finger Motif, Cause Attenuation in Mice and Protect Mice against Lethal Influenza Virus Infection. J. Virol., June 1, 2006; 80(12): 5697 - 5707. [Abstract] [Full Text] [PDF]

				T. Liu and Z. Ye Introduction of a Temperature-Sensitive Phenotype into Influenza A/WSN/33 Virus by Altering the Basic Amino Acid Domain of Influenza Virus Matrix Protein J. Virol., September 15, 2004; 78(18): 9585 - 9591. [Abstract] [Full Text] [PDF]

				E. K.-W. Hui, S. Barman, T. Y. Yang, and D. P. Nayak Basic Residues of the Helix Six Domain of Influenza Virus M1 Involved in Nuclear Translocation of M1 Can Be Replaced by PTAP and YPDL Late Assembly Domain Motifs J. Virol., June 15, 2003; 77(12): 7078 - 7092. [Abstract] [Full Text] [PDF]

				T. Liu and Z. Ye Restriction of Viral Replication by Mutation of the Influenza Virus Matrix Protein J. Virol., November 13, 2002; 76(24): 13055 - 13061. [Abstract] [Full Text] [PDF]

				Z. Ye, T. Liu, D. P. Offringa, J. McInnis, and R. A. Levandowski Association of Influenza Virus Matrix Protein with Ribonucleoproteins J. Virol., September 1, 1999; 73(9): 7467 - 7473. [Abstract] [Full Text]