The interaction between human papillomavirus type 16 E1 and E2 proteins is blocked by an antibody to the N-terminal region of E2

Eur J Biochem. 1995 Apr 15;229(2):517-25. doi: 10.1111/j.1432-1033.1995.0517k.x.

Abstract

Replication of papillomavirus DNA requires two virally encoded proteins, E1 and E2. We expressed human papillomavirus (HPV) type 16 E1 and E2 in bacteria and showed that purified full-length E2 protein interacted directly with E1, in the absence of HPV16 DNA. It was established that the first 142 amino acids of E1 were not required for binding as E2 protein was able to interact with E1 devoid of this region. The interaction of E2 with E1 could be blocked by a monoclonal antibody that bound E2 in the region of amino acids 18-41 of E2 whereas a monoclonal antibody reactive with a nearby part of the molecule (amino acids 2-17) only partially blocked this interaction. These results suggest that a region in the N-terminus of E2 around amino acids 18-41 is a site of interaction with the E1 protein.

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Amino Acid Sequence
  • Antibodies, Monoclonal / immunology
  • Base Sequence
  • Binding Sites
  • Binding, Competitive
  • DNA-Binding Proteins / metabolism
  • Epitope Mapping
  • Molecular Sequence Data
  • Oligodeoxyribonucleotides / chemistry
  • Oncogene Proteins, Fusion / metabolism*
  • Oncogene Proteins, Viral / immunology
  • Oncogene Proteins, Viral / metabolism*
  • Papillomaviridae / chemistry*
  • Peptides / chemistry
  • Peptides / immunology
  • Protein Binding
  • Recombinant Proteins

Substances

  • Antibodies, Monoclonal
  • DNA-Binding Proteins
  • E1 protein, Human papillomavirus 16
  • E2 protein, Human papillomavirus type 16
  • Oligodeoxyribonucleotides
  • Oncogene Proteins, Fusion
  • Oncogene Proteins, Viral
  • Peptides
  • Recombinant Proteins
  • Adenosine Triphosphatases