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.
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 transformation, in expression of nuclear protein 1 or 2 or LMP1, or in induction of lytic EBV replication. Cells transformed by mutant virus recombinants were not different from wild-type virus transformants in initial or long-term outgrowth, sensitivity to limiting cell dilution, serum requirement, or clonogenic growth in soft agar. Together with similar analyses of a mutation stopping translation of the LMP2A amino-terminal cytoplasmic domain, these results indicate that LMP2 is not required for primary B-lymphocyte infection in vitro.
Longnecker
R
R
Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115.
Miller
C L
CL
Miao
X Q
XQ
Tomkinson
B
B
Kieff
E
E
D000483:Alleles; D000956:Antigens, Viral / Q000235:genetics*; D001402:B-Lymphocytes / Q000382:microbiology*; D001483:Base Sequence; D002472:Cell Transformation, Viral; D004252:DNA Mutational Analysis; D005838:Genotype; D004854:Herpesvirus 4, Human / Q000254:growth & development*; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D016133:Polymerase Chain Reaction; D013329:Structure-Activity Relationship; D014763:Viral Matrix Proteins / Q000235:genetics*; D014779:Virus Replication
D000956:Antigens, Viral; C037662:EBV-associated membrane antigen, Epstein-Barr virus; D009838:Oligodeoxyribonucleotides; D014763:Viral Matrix Proteins