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Journal of Virology, June 2005, p. 7918-7921, Vol. 79, No. 12
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.12.7918-7921.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Determination of the Minimal Distance between the Matrix and Transmembrane Domains of the Large Hepatitis B Virus Envelope Protein

Britta Kluge,{dagger} Michaela Schläger, Alexander Pairan, and Volker Bruss*

Department of Virology, University of Göttingen, D-37075 Göttingen, Germany

Received 17 December 2004/ Accepted 7 February 2005

The cytosolic matrix domain (MD) located between amino acids (aa) 103 and 124 of the large hepatitis B virus envelope protein L is essential for virion formation. We reduced the distance between MD and the transmembrane domain (TD; aa 254 to 272) by deletions starting at aa 132. Six mutants with deletions of up to aa 234 were wild type, and four mutants with slightly larger deletions were blocked with respect to virion morphogenesis. Thus, the minimal distance between MD and TD was around 26 aa. This spacer might be required by MD to reach contact sites on the capsid.

* Corresponding author. Mailing address: University of Göttingen, Department of Virology, Kreuzbergring 57, D-37075 Göttingen, Germany. Phone: 49-551-395759. Fax: 49-552-394471. E-mail: vbruss{at}gwdg.de.

{dagger} Present address: Robert Koch-Institut, Nordufer 20, 13353 Berlin, Germany.

Journal of Virology, June 2005, p. 7918-7921, Vol. 79, No. 12
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.12.7918-7921.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Pairan, A., Bruss, V. (2009). Functional Surfaces of the Hepatitis B Virus Capsid. J. Virol. 83: 11616-11623 [Abstract] [Full Text]  
  • Blanchet, M., Sureau, C. (2006). Analysis of the Cytosolic Domains of the Hepatitis B Virus Envelope Proteins for Their Function in Viral Particle Assembly and Infectivity. J. Virol. 80: 11935-11945 [Abstract] [Full Text]  


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