Solution structure of leptospiral LigA4 Big domain

Biochem Biophys Res Commun. 2015 Nov 13;467(2):288-92. doi: 10.1016/j.bbrc.2015.09.170. Epub 2015 Oct 9.

Abstract

Pathogenic Leptospiraspecies express immunoglobulin-like proteins which serve as adhesins to bind to the extracellular matrices of host cells. Leptospiral immunoglobulin-like protein A (LigA), a surface exposed protein containing tandem repeats of bacterial immunoglobulin-like (Big) domains, has been proved to be involved in the interaction of pathogenic Leptospira with mammalian host. In this study, the solution structure of the fourth Big domain of LigA (LigA4 Big domain) from Leptospira interrogans was solved by nuclear magnetic resonance (NMR). The structure of LigA4 Big domain displays a similar bacterial immunoglobulin-like fold compared with other Big domains, implying some common structural aspects of Big domain family. On the other hand, it displays some structural characteristics significantly different from classic Ig-like domain. Furthermore, Stains-all assay and NMR chemical shift perturbation revealed the Ca(2+) binding property of LigA4 Big domain.

Keywords: Big domain; Ca(2+) binding; LigA; NMR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Adhesins, Bacterial / genetics
  • Amino Acid Sequence
  • Calcium / chemistry*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Gene Expression
  • Immunoglobulins / chemistry*
  • Immunoglobulins / genetics
  • Leptospira interrogans / chemistry*
  • Leptospira interrogans / metabolism
  • Models, Molecular
  • Molecular Mimicry
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Sequence Alignment

Substances

  • Adhesins, Bacterial
  • Immunoglobulins
  • Recombinant Proteins
  • Calcium