Specificity of Baculovirus P6.9 Basic DNA-Binding Proteins and Critical Role of the C Terminus in Virion Formation

Author:

Wang Manli12,Tuladhar Era1,Shen Shu2,Wang Hualin2,van Oers Monique M.1,Vlak Just M.1,Westenberg Marcel13

Affiliation:

1. Laboratory of Virology, Wageningen University, Droevendaalsesteeg 1, 6708 PB Wageningen, Netherlands

2. State Key Laboratory of Virology, Key Laboratory of Molecular Virology and Joint Laboratory of Invertebrate Virology, Wuhan Institute of Virology,Chinese Academy of Sciences, Wuhan 430071, People's Republic of China

3. Pharmaceutical Science Research Division, King's College London, Franklin-Wilkins Building, 150 Stamford Street, London SE1 9NH, United Kingdom

Abstract

ABSTRACT The majority of double-stranded DNA (dsDNA) viruses infecting eukaryotic organisms use host- or virus-expressed histones or protamine-like proteins to condense their genomes. In contrast, members of the Baculoviridae family use a protamine-like protein named P6.9. The dephosphorylated form of P6.9 binds to DNA in a non-sequence-specific manner. By using a p6.9 -null mutant of Autographa californica multiple nucleopolyhedrovirus ( Ac MNPV), we demonstrate that P6.9 is not required for viral DNA replication but is essential for the production of infectious virus. Virion production was rescued by P6.9 homologs from a number of Alpha baculovirus species and one Gammabaculovirus species but not from the genus Betabaculovirus , comprising the granuloviruses, or by the P6.9 homolog VP15 from the unrelated white spot syndrome virus of shrimp. Mutational analyses demonstrated that Ac MNPV P6.9 with a conserved 11-residue deletion of the C terminus was not capable of rescuing p6.9 -null Ac MNPV, while a chimeric Betabaculovirus P6.9 containing the P6.9 C-terminal region of an Alphabaculovirus strain was able to do so. This implies that the C terminus of baculovirus P6.9 contains sequence elements essential for virion formation. Such elements may possibly interact with species- or genus-specific domains of other nucleocapsid proteins during virus assembly.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference58 articles.

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