Staphylococcal Periscope proteins Aap, SasG, and Pls project noncanonical legume-like lectin adhesin domains from the bacterial surface.
Humans
Adhesins, Bacterial
/ genetics
Bacterial Proteins
/ chemistry
Lectins
/ chemistry
Staphylococcal Infections
/ microbiology
Staphylococcus epidermidis
/ chemistry
Protein Domains
/ physiology
Protein Structure, Tertiary
Models, Molecular
Protein Binding
Staphylococcus aureus
/ chemistry
Recombinant Proteins
/ chemistry
Escherichia coli
Epithelial Cells
/ microbiology
Periscope proteins
adhesin
bacterial adhesion
biofilm
cell surface protein
glycomics
lectin
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
03 2023
03 2023
Historique:
received:
13
11
2022
revised:
08
01
2023
accepted:
18
01
2023
medline:
29
3
2023
pubmed:
27
1
2023
entrez:
26
1
2023
Statut:
ppublish
Résumé
Staphylococcus aureus and Staphylococcus epidermidis are frequently associated with medical device infections that involve establishment of a bacterial biofilm on the device surface. Staphylococcal surface proteins Aap, SasG, and Pls are members of the Periscope Protein class and have been implicated in biofilm formation and host colonization; they comprise a repetitive region ("B region") and an N-terminal host colonization domain within the "A region," predicted to be a lectin domain. Repetitive E-G5 domains (as found in Aap, SasG, and Pls) form elongated "stalks" that would vary in length with repeat number, resulting in projection of the N-terminal A domain variable distances from the bacterial cell surface. Here, we present the structures of the lectin domains within A regions of SasG, Aap, and Pls and a structure of the Aap lectin domain attached to contiguous E-G5 repeats, suggesting the lectin domains will sit at the tip of the variable length rod. We demonstrate that these isolated domains (Aap, SasG) are sufficient to bind to human host desquamated nasal epithelial cells. Previously, proteolytic cleavage or a deletion within the A domain had been reported to induce biofilm formation; the structures suggest a potential link between these observations. Intriguingly, while the Aap, SasG, and Pls lectin domains bind a metal ion, they lack the nonproline cis peptide bond thought to be key for carbohydrate binding by the lectin fold. This suggestion of noncanonical ligand binding should be a key consideration when investigating the host cell interactions of these bacterial surface proteins.
Identifiants
pubmed: 36702253
pii: S0021-9258(23)00068-6
doi: 10.1016/j.jbc.2023.102936
pmc: PMC9999234
pii:
doi:
Substances chimiques
Adhesins, Bacterial
0
Bacterial Proteins
0
Lectins
0
Recombinant Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
102936Subventions
Organisme : British Heart Foundation
ID : PG/17/19/32862
Pays : United Kingdom
Organisme : Wellcome Trust
ID : WT099197/Z/12/Z
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 108430/Z/15/Z
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 218304/Z/19/Z
Pays : United Kingdom
Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.