HIV-1 envelope protein gp120 expression by secretion in E. coli: assessment of CD4 binding and use in epitope mapping. Academic Article uri icon

Overview

abstract

  • A non-glycosylated form of the HIV-1 envelope protein gp120 and four truncated derivatives have been expressed as non-fused secreted products in the periplasmic space of E. coli. We show that the full length molecule, whilst folded and soluble, fails to bind to CD4 consistent with other work that suggests an essential role for carbohydrate in gp120 function. In addition, when used in conjunction with the truncated derivatives, rapid epitope mapping of anti-gp120 monoclonal antibodies is achieved using both Western-blot and ELISA formats.

publication date

  • July 1, 1990

Research

keywords

  • Antibodies, Viral
  • CD4 Antigens
  • Epitopes
  • Escherichia coli
  • HIV Envelope Protein gp120
  • HIV-1

Identity

Scopus Document Identifier

  • 0025306463

Digital Object Identifier (DOI)

  • 10.1016/0166-0934(90)90013-6

PubMed ID

  • 1698804

Additional Document Info

volume

  • 29

issue

  • 1