Analysis of a human immunodeficiency virus type 1 isolate carrying a truncated transmembrane glycoprotein

Virology. 1992 Aug;189(2):534-46. doi: 10.1016/0042-6822(92)90577-c.

Abstract

We have recently reported the isolation of a human immunodeficiency virus type 1 (HIV-1), KB-1gp32 carrying a shorter size (32 kDa) of transmembrane glycoprotein (TMP) from TALL-1 cells persistently infected with KB-1gp41 virus strain (Shimizu et al., 1990a). Endoglycosidase treatments showed that the different size of the TMP between the two strains was due to a truncation of 9 kDa of polypeptide in the KB-1gp32 TMP coding region. Sequence analysis revealed the substitution of a CAG codon to a TAG stop codon just downstream of the putative membrane-spanning domain of the TMP of KB-1gp32. This resulted in a truncation of some 133 amino acids of the cytoplasmic domain of TMP. The data indicate that a premature stop codon in KB-1gp32 has been introduced during adaption of the parental virus to TALL-1 cells. We have constructed two chimeric clones between the env region of a clone pKB-1, derived from KB-1gp32, and an infectious molecular clone pNL-432. We have also constructed a site-directed mutant of pNL-432 carrying a premature stop codon at the same position as the env stop codon of pKB-1. Among the three clones carrying a premature stop codon in env, only one chimeric clone was infectious to TALL-1 but not MT-2 cells. This clone contained the entire tat, rev, vpu, and env genes of pKB-1. The pNL-432 mutant was not infectious. The results suggest that some sequences of pKB-1 might compensate for the truncation of the TMP during replication in TALL-1 cells.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Cytoplasm
  • Genes, env*
  • HIV Envelope Protein gp41 / chemistry*
  • HIV Envelope Protein gp41 / genetics
  • HIV-1 / chemistry*
  • HIV-1 / genetics
  • Lentivirus / chemistry
  • Lentivirus / genetics
  • Membrane Glycoproteins / chemistry*
  • Membrane Glycoproteins / metabolism
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Mutation
  • Oligodeoxyribonucleotides / chemistry
  • Polymerase Chain Reaction
  • Sequence Alignment
  • Transfection

Substances

  • HIV Envelope Protein gp41
  • Membrane Glycoproteins
  • Oligodeoxyribonucleotides

Associated data

  • GENBANK/D01205
  • GENBANK/D01206
  • GENBANK/D01207