期刊
VIROLOGY
卷 421, 期 2, 页码 253-265出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2011.09.012
关键词
HIV-1 capsid protein; HIV-1 assembly; HIV-1 cores; VSV-G pseudotyping; Interdomain linker; In vitro assembly; TRIM5 proteins; Host restriction; Virus disassembly; Reverse transcription
类别
资金
- National Institutes of Health (Eunice Kennedy Shriver National Institute of Child Health and Human Development)
- National Cancer Institute, Center for Cancer Research
- Office of Science and Health Coordination, Food and Drug Administration, National Heart, Lung, and Blood Institute, National Institutes of Health
- National Cancer Institute, National Institutes of Health [HHSN261200800001E]
- SAIC-Frederick, Inc.
The HIV-1 capsid protein consists of two independently folded domains connected by a flexible peptide linker (residues 146-150), the function of which remains to be defined. To investigate the role of this region in virus replication, we made alanine or leucine substitutions in each linker residue and two flanking residues. Three classes of mutants were identified: (i) S146A and T148A behave like wild type (WT); (ii) Y145A, 1150A, and L151A are noninfectious, assemble unstable cores with aberrant morphology, and synthesize almost no viral DNA; and (iii) P147L and S149A display a poorly infectious, attenuated phenotype. Infectivity of P147L and S149A is rescued specifically by pseudotyping with vesicular stomatitis virus envelope glycoprotein. Moreover, despite having unstable cores, these mutants assemble WT-like structures and synthesize viral DNA, although less efficiently than WT. Collectively, these findings demonstrate that the linker region is essential for proper assembly and stability of cores and efficient replication. Published by Elsevier Inc.
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