Identification of a family of BspA like surface proteins of Entamoeba histolytica with novel leucine rich repeats

Mol Biochem Parasitol. 2006 Jan;145(1):111-6. doi: 10.1016/j.molbiopara.2005.08.017. Epub 2005 Sep 16.

Abstract

Leucine rich repeats serve as recognition motifs for surface proteins from bacteria and eukaryotes. The BspA protein from Bacteroides forsythus mediates bacterial binding to fibronectin and contains leucine rich repeats of the Treponema pallidum (TpLRRP) family. Here we show that the protozoan parasite Entamoeba histolytica contains multiple BspA-like proteins, including a family of surface proteins which possess a new form of a leucine rich repeat that differs from the standard Treponema pallidum- like leucine rich repeat (TpLRRP) by possessing two conserved cysteine residues.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Cloning, Molecular
  • Entamoeba histolytica / genetics
  • Entamoeba histolytica / metabolism*
  • Leucine / chemistry*
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Minisatellite Repeats
  • Molecular Sequence Data
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Repetitive Sequences, Nucleic Acid / genetics*
  • Sequence Analysis, DNA

Substances

  • Bacterial Proteins
  • BspA protein, bacteria
  • Membrane Proteins
  • Protozoan Proteins
  • Leucine