Three-dimensional structures of Lipoproteins from Streptococcus pneumoniae and Staphylococcus aureus

Sergio G. Bartual, Martín Alcorlo, Siseth Martínez-Caballero, Rafael Molina, Juan A. Hermoso (Lead / Corresponding author)

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

Bacterial lipoproteins (Lpp) compose a large family of surface-exposed proteins that are involved in diverse, but critical, cellular functions spanning from fitness to virulence. All of them present a common signature, a sequence motif, known as LipoBox, containing an invariant Cys residue that allows the protein to be covalently bound to the membrane through a thioether linkage. Despite the abundance and relevance of Lpp, there is a scarcity of structural and functional information for this family of proteins. In this review, the updated structural and functional data for Lpp from two Gram-positive pathogenic model organisms, Staphylococcus aureus and Streptococcus pneumoniae is presented. The available structural information offers a glimpse over the Lpp functional mechanisms. Their relevance in bacterial fitness, and also in virulence and host-pathogen interactions, reveals lipoproteins as very attractive targets for designing of novel antimicrobials, and interesting candidates as novel vaccine antigens.

Original languageEnglish
Number of pages13
JournalInternational Journal of Medical Microbiology
DOIs
Publication statusE-pub ahead of print - 27 Oct 2017

Keywords

  • Lipoproteins
  • Protein structure
  • Staphylococcus aureus
  • Streptococcus pneumoniae
  • Virulence

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