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 language | English |
|---|---|
| Pages (from-to) | 692-704 |
| Number of pages | 13 |
| Journal | International Journal of Medical Microbiology |
| Volume | 308 |
| Issue number | 6 |
| Early online date | 27 Oct 2017 |
| DOIs | |
| Publication status | Published - Aug 2018 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Lipoproteins
- Protein structure
- Staphylococcus aureus
- Streptococcus pneumoniae
- Virulence
ASJC Scopus subject areas
- Microbiology
- Microbiology (medical)
- Infectious Diseases
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