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Structure and Assembly

Second-Site Compensatory Mutations of HIV-1 Capsid Mutations

Colleen M. Noviello, Claudia S. López, Ben Kukull, Henry McNett, Amelia Still, Jacob Eccles, Rachel Sloan, Eric Barklis
Colleen M. Noviello
1Department of Microbiology, Oregon Health & Science University, Mail Code L220, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239-3098
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Claudia S. López
1Department of Microbiology, Oregon Health & Science University, Mail Code L220, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239-3098
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Ben Kukull
1Department of Microbiology, Oregon Health & Science University, Mail Code L220, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239-3098
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Henry McNett
1Department of Microbiology, Oregon Health & Science University, Mail Code L220, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239-3098
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Amelia Still
2Department of Biochemistry, University of Wisconsin, Madison, Wisconsin
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Jacob Eccles
1Department of Microbiology, Oregon Health & Science University, Mail Code L220, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239-3098
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Rachel Sloan
1Department of Microbiology, Oregon Health & Science University, Mail Code L220, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239-3098
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Eric Barklis
1Department of Microbiology, Oregon Health & Science University, Mail Code L220, 3181 SW Sam Jackson Park Road, Portland, Oregon 97239-3098
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  • For correspondence: barklis@ohsu.edu
DOI: 10.1128/JVI.00099-11
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ABSTRACT

The human immunodeficiency virus (HIV) capsid (CA) protein assembles into a hexameric lattice that forms the mature virus core. Contacts between the CA N-terminal domain (NTD) of one monomer and the C-terminal domain (CTD) of the adjacent monomer are important for the assembly of this core. In this study, we have examined the effects of mutations in the NTD region associated with this interaction. We have found that such mutations yielded modest reductions of virus release but major effects on viral infectivity. Cell culture and in vitro assays indicate that the infectivity defects relate to abnormalities in the viral cores. We have selected second-site compensatory mutations that partially restored HIV infectivity. These mutations map to the CA CTD and to spacer peptide 1 (SP1), the portion of the precursor Gag protein immediately C terminal to the CTD. The compensatory mutations do not locate to the molecularly modeled intermolecular NTD-CTD interface. Rather, the compensatory mutations appear to act indirectly, possibly by realignment of the C-terminal helix of the CA CTD, which participates in the NTD-CTD interface and has been shown to serve an important role in the assembly of infectious virus.

  • Copyright © 2011, American Society for Microbiology
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Second-Site Compensatory Mutations of HIV-1 Capsid Mutations
Colleen M. Noviello, Claudia S. López, Ben Kukull, Henry McNett, Amelia Still, Jacob Eccles, Rachel Sloan, Eric Barklis
Journal of Virology Apr 2011, 85 (10) 4730-4738; DOI: 10.1128/JVI.00099-11

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Second-Site Compensatory Mutations of HIV-1 Capsid Mutations
Colleen M. Noviello, Claudia S. López, Ben Kukull, Henry McNett, Amelia Still, Jacob Eccles, Rachel Sloan, Eric Barklis
Journal of Virology Apr 2011, 85 (10) 4730-4738; DOI: 10.1128/JVI.00099-11
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