A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein.

A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Research Abstract Details 

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A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Abstract Text:

Shixing Tang,Sherimay Ablan,Megan Dueck,Wilfredo ,Brenda Soto,Margaret Caplan,Kunio Nagashima,Indira K Hewlett,Eric O Freed,Judith G Levin,

The HIV-1 capsid (CA) protein plays an important role in virus assembly and infectivity. Previously, we showed that Ala substitutions in the N-terminal residues Trp23 and Phe40 cause a severely defective phenotype. In searching for mutations at these positions that result in a non-lethal phenotype, we identified one candidate, W23F. Mutant virions contained aberrant cores, but unlike W23A, also displayed some infectivity in a single-round replication assay and delayed replication kinetics in MT-4 cells. Following long-term passage in MT-4 cells, two second-site mutations were isolated. In particular, the W23F/V26I mutation partially restored the wild-type phenotype, including production of particles with conical cores and wild-type replication kinetics in MT-4 cells. A structural model is proposed to explain the suppressor phenotype. These findings describe a novel occurrence, namely suppression of a mutation in a hydrophobic residue that is critical for maintaining the structural integrity of CA and proper core assembly.

A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Publishing Authors By Initials

S Tang,S Ablan,M Dueck,W ,B Soto,M Caplan,K Nagashima,IK Hewlett,EO Freed,JG Levin,

For similar biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus replication research abstracts see: biological phenomena, cell phenomena, and immunity: biological phenomena: microbiologic phenomena: viral physiology: virus replication research

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A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Intr

Journal: Virology

VOLUME: 359

Page Numbers: 105-15

Journal Abbreviation: Virology

ISSN: 0042-6822

DAY: 19

MONTH: 10

YEAR: 2006

A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Information

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LANGUAGE: eng

NlmUniqueID: 110674

A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Keywords Mesh Terms:

KEYWORDS: Virus Replication

MESH TERMS: ultrastructure

Chemical & Substance for Abstract: A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein. Information

Substance Name: RNA-Directed DNA Polymerase

Registry Number: EC 2.7.7.49

Grant and Affiliation Information for A second-site suppressor significantly improves the defective phenotype imposed by mutation of an aromatic residue in the N-terminal domain of the HIV-1 capsid protein.

AFFILIATION: Viral Gene Regulation Section, Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health, Building 6B, Room 216, Bethesda, MD 20892-2780, USA.

Country: United States

AGENCY: United States NICHD

GRANT: Z01 HD000069-33

ACRONYM: HD

MEDLINETA: Virology

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