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Journal of Virology, May 2009, p. 4757-4765, Vol. 83, No. 10
0022-538X/09/$08.00+0     doi:10.1128/JVI.01927-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Isolation and Preliminary Characterization of Herpes Simplex Virus 1 Primary Enveloped Virions from the Perinuclear Space{triangledown}

Maryn E. Padula, Mariam L. Sydnor, and Duncan W. Wilson*

Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461

Received 12 September 2008/ Accepted 26 February 2009

Herpes simplex virus 1 (HSV-1) nucleocapsids exit the nucleus by budding into the inner nuclear membrane, where they exist briefly as primary enveloped virions. These virus particles subsequently fuse their envelopes with the outer nuclear membrane, permitting nucleocapsids to then enter the cytoplasm and complete assembly. We have developed a method to isolate primary enveloped virions from HSV-1-infected cells and subjected the primary enveloped virion preparation to MALDI-MS/MS (matrix-assisted laser desorption ionization-tandem mass spectrometry) analyses. We identified most capsid proteins, a tegument protein (VP22), a glycoprotein (gD), and a cellular protein (annexin A2) in the primary enveloped virion preparation. We determined that annexin A2 does not play an essential role in infection under our experimental conditions. Elucidating the structure and biochemical properties of this unique virus assembly intermediate will provide new insights into HSV-1 biology.

* Corresponding author. Mailing address: Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461. Phone: (718) 430-2305. Fax: (718) 430-8567. E-mail: wilson{at}aecom.yu.edu

{triangledown} Published ahead of print on 11 March 2009.

Journal of Virology, May 2009, p. 4757-4765, Vol. 83, No. 10
0022-538X/09/$08.00+0     doi:10.1128/JVI.01927-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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