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Journal of Virology, November 2001, p. 11239-11243, Vol. 75, No. 22
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.22.11239-11243.2001

N-Terminal Cleavage Fragment of Glycosylated Gag Is Incorporated into Murine Oncornavirus Particles

Ryuichi Fujisawa,1 Frank J. McAtee,1 Cynthia Favara,1 Stanley F. Hayes,2 and John L. Portis1,*

Laboratory of Persistent Viral Diseases1 and Microscopy Branch,2 National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories, Hamilton, Montana 59840

Received 4 December 2000/Accepted 18 August 2001

Glycosylated Gag (Glycogag) is a transmembrane protein encoded by murine and feline oncornaviruses. While the protein is dispensible for virus replication, Glycogag-null mutants of a neurovirulent murine oncornavirus are slow to spread in vivo and exhibit a loss of pathogenicity. The function of this protein in the virus life cycle, however, is not understood. Glycogag is expressed at the plasma membrane of infected cells but has not been detected in virions. In the present study we have reexamined this issue and have found an N-terminal cleavage fragment of Glycogag which was pelleted by high-speed centrifugation and sedimented in sucrose density gradients at the same bouyant density as virus particles. Its association with virions was confirmed by velocity sedimentation through iodixanol, which effectively separated membrane microvesicles from virus particles. Furthermore, the apparent molecular weight of the virion-associated protein was different from that of the protein extracted from the plasma membrane, suggesting some level of specificity or selectivity of incorporation.

* Corresponding author. Mailing address: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, 903 S. 4th St., Hamilton, MT 59840. Phone: (406) 363-9339. Fax: (406) 363-9286. E-mail: jportis{at}nih.gov.

Journal of Virology, November 2001, p. 11239-11243, Vol. 75, No. 22
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.22.11239-11243.2001


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