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

Sergio G Bartual, Martín Alcorlo, Siseth Martínez-Caballero, Rafael Molina, Juan A Hermoso

7 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
JournalInternational Journal of Medical Microbiology
Volume308
Issue number6
Pages (from-to)692-704
Number of pages13
ISSN1438-4221
DOIs
Publication statusPublished - Aug 2018
Externally publishedYes

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