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

This Article Full Text 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 Johne, R. Articles by Müller, H. Search for Related Content PubMed PubMed Citation Articles by Johne, R. Articles by Müller, H. Agricola Articles by Johne, R. Articles by Müller, H.

Avian polyomavirus agnoprotein 1a is incorporated into the virus particle as a fourth structural protein, VP4

Institute of Virology, Faculty of Veterinary Medicine, University of Leipzig, An den Tierkliniken 29, D-04103 Leipzig, Germany¹

Author for correspondence: Hermann Müller. Fax +49 341 9738219. e-mail virology{at}vetmed.uni-leipzig.de

Agnoproteins, encoded by the 5'-region of the late bicistronic mRNA of some polyomaviruses, are small proteins with largely unknown functions. In avian polyomavirus (APV)-infected cells, mRNAs of seven putative agnoproteins have been observed. Recently, it has been shown that agnoprotein 1a and its truncated variant agnoprotein 1b, encoded by the predominant mRNA species, are essential for APV replication. Here, the presence of agnoprotein 1a is demonstrated in the nucleus of APV-infected cells and in purified APV particles. Interaction between agnoprotein 1a and the major structural protein, VP1, was demonstrated by co-immunoprecipitation experiments using lysates of recombinant baculovirus-infected insect cells. With proteins expressed in E. coli, binding to double-stranded DNA in a sequence-unspecific manner was shown for agnoprotein 1a, whereas agnoprotein 1b failed to bind. A leucine zipper-like motif present in agnoprotein 1a is considered to be involved in DNA binding. Due to the absence of any structural or functional homologies between APV agnoprotein 1a and the agnoproteins of mammalian polyomaviruses, it is suggested that this protein should be renamed VP4, indicating its function as a fourth structural protein of APV.

This article has been cited by other articles:

				R. Johne and H. Muller Polyomaviruses of Birds: Etiologic Agents of Inflammatory Diseases in a Tumor Virus Family J. Virol., November 1, 2007; 81(21): 11554 - 11559. [Full Text] [PDF]

				R. Johne, G. Paul, D. Enderlein, T. Stahl, C. Grund, and H. Muller Avian polyomavirus mutants with deletions in the VP4-encoding region show deficiencies in capsid assembly and virus release, and have reduced infectivity in chicken J. Gen. Virol., March 1, 2007; 88(3): 823 - 830. [Abstract] [Full Text] [PDF]

				R. Johne, W. Wittig, D. Fernandez-de-Luco, U. Hofle, and H. Muller Characterization of two novel polyomaviruses of birds by using multiply primed rolling-circle amplification of their genomes. J. Virol., April 1, 2006; 80(7): 3523 - 3531. [Abstract] [Full Text] [PDF]

				R. Johne and H. Muller Nuclear Localization of Avian Polyomavirus Structural Protein VP1 Is a Prerequisite for the Formation of Virus-Like Particles J. Virol., January 15, 2004; 78(2): 930 - 937. [Abstract] [Full Text] [PDF]