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 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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ye, Z P
Right arrow Articles by Wagner, R R
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ye, Z P
Right arrow Articles by Wagner, R R

Next Article 

J Virol. 1987 February; 61(2): 239-246

Functional and antigenic domains of the matrix (M1) protein of influenza A virus.

Z P Ye, R Pal, J W Fox and R R Wagner

ABSTRACT

The membrane- and ribonucleocapsid (RNP)-binding domains of the matrix (M1) protein of influenza A virus (WSN strain) were partially mapped and characterized by reactivity with monoclonal antibodies (MAb) as well as by proteolytic cleavages and amino acid sequencing of the resulting peptides. Of two peptides formed by formic acid hydrolysis, a 9-kilodalton fragment at the amino-terminal third of the M1 protein was recognized by MAb M2-1C6 (to epitope 1), and a 15-kilodalton fragment at the carboxy-terminal two-thirds was recognized by MAb 289/4 (to epitope 2). Partial cleavage by staphylococcal V8 protease gave rise to a 16-kilodalton peptide, mapping to amino acid 8, which was recognized by MAbs to all three epitopes but rather weakly by MAb 904/6 to epitope 3. These studies suggest that epitope 1 of the M1 protein resides between amino acids 8 and 89, whereas epitopes 2 and possibly 3 are located between amino acids 89 and 141 or somewhat more carboxy distal. The intact M1 protein and its N-terminal 9- and 10-kilodalton peptides generated by formic acid or V8 protease cleavage, respectively, reconstituted with dipalmitoylphosphatidylcholine vesicles, but these N-terminal peptides had little effect on in vitro transcription of the RNP core. In sharp contrast, both intact M1 protein and the C-terminal 15-kilodalton formic acid fragment were able to inhibit viral transcription markedly. Moreover, MAb 289/4 (to epitope 2) reversed this inhibited transcription significantly. These studies suggest that the lipid-binding domain of the M1 protein is located within the amino-terminal third, whereas the site involved in the interaction of the M1 protein with RNP cores is located within the carboxy-terminal two-thirds.

J Virol. 1987 February; 61(2): 239-246




This article has been cited by other articles:

  • Robb, N. C., Smith, M., Vreede, F. T., Fodor, E. (2009). NS2/NEP protein regulates transcription and replication of the influenza virus RNA genome. J. Gen. Virol. 90: 1398-1407 [Abstract] [Full Text]  
  • Noton, S. L., Medcalf, E., Fisher, D., Mullin, A. E., Elton, D., Digard, P. (2007). Identification of the domains of the influenza A virus M1 matrix protein required for NP binding, oligomerization and incorporation into virions. J. Gen. Virol. 88: 2280-2290 [Abstract] [Full Text]  
  • Liu, T., Ye, Z. (2005). Attenuating Mutations of the Matrix Gene of Influenza A/WSN/33 Virus. J. Virol. 79: 1918-1923 [Abstract] [Full Text]  
  • Burleigh, L. M., Calder, L. J., Skehel, J. J., Steinhauer, D. A. (2005). Influenza A Viruses with Mutations in the M1 Helix Six Domain Display a Wide Variety of Morphological Phenotypes. J. Virol. 79: 1262-1270 [Abstract] [Full Text]  
  • Hagmaier, K., Gelderblom, H. R., Kochs, G. (2004). Functional comparison of the two gene products of Thogoto virus segment 6. J. Gen. Virol. 85: 3699-3708 [Abstract] [Full Text]  
  • Liu, T., Ye, Z. (2004). 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. 78: 9585-9591 [Abstract] [Full Text]  
  • Rodriguez, L., Cuesta, I., Asenjo, A., Villanueva, N. (2004). Human respiratory syncytial virus matrix protein is an RNA-binding protein: binding properties, location and identity of the RNA contact residues. J. Gen. Virol. 85: 709-719 [Abstract] [Full Text]  
  • Rubin, S. A., Amexis, G., Pletnikov, M., Vanderzanden, J., Mauldin, J., Sauder, C., Malik, T., Chumakov, K., Carbone, K. M. (2003). Changes in Mumps Virus Gene Sequence Associated with Variability in Neurovirulent Phenotype. J. Virol. 77: 11616-11624 [Abstract] [Full Text]  
  • Hui, E. K.-W., Barman, S., Yang, T. Y., Nayak, D. P. (2003). 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. 77: 7078-7092 [Abstract] [Full Text]  
  • Bourmakina, S. V., Garcia-Sastre, A. (2003). Reverse genetics studies on the filamentous morphology of influenza A virus. J. Gen. Virol. 84: 517-527 [Abstract] [Full Text]  
  • Liu, T., Ye, Z. (2002). Restriction of Viral Replication by Mutation of the Influenza Virus Matrix Protein. J. Virol. 76: 13055-13061 [Abstract] [Full Text]  
  • Ye, Z., Liu, T., Offringa, D. P., McInnis, J., Levandowski, R. A. (1999). Association of Influenza Virus Matrix Protein with Ribonucleoproteins. J. Virol. 73: 7467-7473 [Abstract] [Full Text]  
  • Garoff, H., Hewson, R., Opstelten, D.-J. E. (1998). Virus Maturation by Budding. Microbiol. Mol. Biol. Rev. 62: 1171-1190 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»