Abstract
Staphylococcus aureus is a successful human and animal pathogen. Its pathogenicity is linked to its ability to secrete a large amount of virulence factors. These secreted proteins interfere with many critical components of the immune system, both innate and adaptive, and hamper proper immune functioning. In recent years, numerous studies have been conducted in order to understand the molecular mechanism underlying the interaction of evasion molecules with the host immune system. Structural studies have fundamentally contributed to our understanding of the mechanisms of action of the individual factors. Furthermore, such studies revealed one of the most striking characteristics of the secreted immune evasion molecules: their conserved structure. Despite high-sequence variability, most immune evasion molecules belong to a small number of structural categories. Another remarkable characteristic is that S. aureus carries most of these virulence factors on mobile genetic elements (MGE) or ex-MGE in its accessory genome. Coevolution of pathogen and host has resulted in immune evasion molecules with a highly host-specific function and prevalence. In this review, we explore how these shared structures and genomic locations relate to function and host specificity. This is discussed in the context of therapeutic options for these immune evasion molecules in infectious as well as in inflammatory diseases.
Abbreviations
- AMP:
-
Antimicrobial peptide
- APC:
-
Antigen-presenting cell
- Aur:
-
Aureolysin
- Bov:
-
Bovine
- CA-MRSA:
-
Community-acquired MRSA
- CHIPS (chp):
-
Chemotaxis inhibitory protein of S. aureus
- DARC:
-
Duffy antigen receptor for chemokines
- EAP (eap):
-
Extracellular adherence protein
- Ecb (ecb):
-
Extracellular complement-binding protein
- Efb (efb):
-
Extracellular fibrinogen-binding protein
- Egc (egc):
-
Enterotoxin gene cluster
- Eq:
-
Equine
- FLIPr (flipr):
-
FPR2 inhibitory protein
- FPR:
-
Formyl peptide receptor
- GPCR:
-
G-protein-coupled receptor
- HLA:
-
Human leukocyte antigen
- Hla (hla):
-
α-hemolysin
- Hlb (hlb):
-
β-hemolysin
- Hlg (hlg):
-
γ-hemolysin
- IEC:
-
Immune evasion cluster
- Ig:
-
Immunoglobulin
- Luk (luk):
-
Leukocidin
- mAb:
-
Monoclonal antibody
- MAC:
-
Membrane attack complex
- MGE:
-
Mobile genetic element
- MHC-II:
-
Major histocompatibility complex II
- MMP-9:
-
Matrix metalloproteinase 9
- MRSA:
-
Methicillin-resistant Staphylococcus aureus
- NET:
-
Neutrophil extracellular trap
- NMR:
-
Nuclear magnetic resonance
- NSP:
-
Neutrophil serine protease
- OB:
-
Oligomer-binding
- Ov:
-
Ovine
- PSGL-1:
-
P-selection glycoprotein ligand-1
- PSM (psm):
-
Phenol-soluble modulin
- PVL (pvl):
-
Panton–Valentine leukocidin
- SAg:
-
Superantigen
- SAK (sak):
-
Staphylokinase
- SaPI:
-
Staphylococcal pathogenicity island
- Sbi (sbi):
-
Second immunoglobulin-binding protein
- SC (coa):
-
Staphylocoagulase
- SCC:
-
Staphylococcal cassette chromosome
- SCIN (scn):
-
Staphylococcal complement inhibitor
- SE (se):
-
Staphylococcal enterotoxin
- SEl (sel):
-
Staphylococcal enterotoxin-like
- SNase (nuc):
-
Staphylococcal nuclease
- SpA (spa):
-
Staphylococcal protein A
- SSL (ssl):
-
Superantigen-like protein
- TCR:
-
T cell receptor
- TLR:
-
Toll-like receptor
- TSST-1 (tst):
-
Toxic shock syndrome toxin-1
- vWbp (vwb):
-
Von Willebrand factor-binding protein
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Acknowledgements
We would like to thank Dr. Carla de Haas, Dr. Daphne Stapels, Dr. Julia Kolata, Dr. Stephen Nutbeam-Tuffs, and Jacques Flores Dourojeanni for useful discussions and critical review of the manuscript. This work was supported by funding from The Dutch Science Foundation NWO (KJK), the ALTANT initiative of the Dutch Ministry of Economic Affairs (MV) H2020, and M.S. Curie (RDG).
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Koymans, K.J., Vrieling, M., Gorham, R.D., van Strijp, J.A.G. (2015). Staphylococcal Immune Evasion Proteins: Structure, Function, and Host Adaptation. In: Bagnoli, F., Rappuoli, R., Grandi, G. (eds) Staphylococcus aureus. Current Topics in Microbiology and Immunology, vol 409. Springer, Cham. https://doi.org/10.1007/82_2015_5017
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