The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitro.

doi:10.1128/JVI.67.4.2006-2013.1993

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Article

The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitro.

Journal of virology - 1 Apr 1993

Longnecker R, Miller C L, Miao X Q, Tomkinson B, Kieff E

Abstract excerpt

Specifically mutated Epstein-Barr virus (EBV) recombinants which truncate latent membrane protein 2A (LMP2A) and LMP2B after 260 of 497 amino acids and after 141 of 378 amino acids, respectively, were constructed. Despite truncation before the last seven transmembrane domains and the carboxy terminus, the mutant recombinants were not altered in initiation of primary B-lymphocyte infection or growth...

Topics

Alleles
Antigens, Viral
B-Lymphocytes
Base Sequence
Cell Transformation, Viral
DNA Mutational Analysis
Genotype
Herpesvirus 4, Human
Humans
In Vitro Techniques

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Oligodeoxyribonucleotides

Polymerase Chain Reaction

Structure-Activity Relationship

Viral Matrix Proteins

Virus Replication

Source

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Identifiers

PMID: 8383224
DOI: 10.1128/JVI.67.4.2006-2013.1993
PMCID: PMC240269

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The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitro.PMID 8383224Read ↗

The only domain which distinguishes Epstein-Barr virus latent membrane protein 2A (LMP2A) from LMP2B is dispensable for lymphocyte infection and growth transformation in vitro; LMP2A is therefore nonessential.Semantic proximity Read ↗

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