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J Virol, May 1998, p. 4403-4407, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Cryoelectron Microscopic Examination of Human Immunodeficiency Virus Type 1 Virions with Mutations in the Cyclophilin A Binding Loop

Lawrence B. Kong,1 DongSung An,2 Bradley Ackerson,3 Jude Canon,3 Osvaldo Rey,3 Irvin S. Y. Chen,2 Paul Krogstad,3 and Phoebe L. Stewart1,*

Department of Molecular and Medical Pharmacology and Crump Institute for Biological Imaging,1 Departments of Microbiology and Immunology and Medicine,2 and Department of Pediatrics,3 UCLA School of Medicine, Los Angeles, California 90095

Received 4 November 1997/Accepted 21 January 1998

The human immunodeficiency virus type 1 capsid protein contains a conserved P217X4PX2PX5P231 motif. Mutation at Pro-222 decreases virion incorporation of cyclophilin A, while mutation at Pro-231 abolishes infectivity. Although viral RNA incorporation and protease cleavage of the Gag precursor were not affected by these mutations, cryoelectron microscopy revealed a loss of virion maturation in P231A particles.

* Corresponding author. Mailing address: Department of Molecular and Medical Pharmacology, A-324 CIBI, Box 951770, UCLA School of Medicine, Los Angeles, CA 90095. Phone: (310) 206-7055. Fax: (310) 206-8975. E-mail: pstewart{at}mail.nuc.ucla.edu.

J Virol, May 1998, p. 4403-4407, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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