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Review
. 2017 Nov 17;8(8):1592-1601.
doi: 10.1080/21505594.2017.1363140. Epub 2017 Aug 25.

Functional and structural characteristics of bacterial proteins that bind host cytokines

Martin Högbom  1 , Riikka Ihalin  2
Affiliations
Review

Functional and structural characteristics of bacterial proteins that bind host cytokines

Martin Högbom et al. Virulence. .

Abstract

Several human pathogens bind and respond to host cytokines, which can be considered a virulence mechanism that communicates defensive actions of the host to the pathogen. This review summarizes the current knowledge of bacterial cytokine-binding proteins, with a particular focus on their functional and structural characteristics. Many bacterial cytokine-binding proteins function in the development of infection and inflammation and mediate adhesion to host cells, suggesting multiple roles in pathogen-host interactions. The regions of the bacterial proteins that interact with host cytokines can display structural similarities to other proteins involved in cytokine signaling. However, there appears to be no central shared structural themes for bacterial cytokine-binding proteins, and they appear to possess structures that are different from the cytokine receptors of the host. Atomic-level information regarding receptor-cytokine interactions is needed to be able to disrupt these interactions and to elucidate the specific consequences of cytokine binding in a pathogen and host.

Keywords: bacterial cytokine-binding proteins; human pathogens; structural biology; virulence factor.

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Figures

Figure 1.
Figure 1.
The 3D structures of bacterial cytokine-binding proteins colored from the N-terminus (blue) to the C-terminus (red). (A) The N-terminal PapC domain of Y. pestis Caf1A (PDB:4BOE), the β, N0 and N1 domains of N. meningitidis PilQ (PDB:4AV2), the N-terminal transmembrane domain (PDB:4RLC), and the C-terminal domain (PDB:5U1H) of P. aeruginosa OprF are located in the outer membrane of gram-negative species. (B) E. coli IrmA (PDB:5EK5) and N. meningitidis PilE (PDB:5JW8) are secreted to and face the extracellular space, respectively. The figures were prepared with PyMol (www.pymol.org).
Figure 2.
Figure 2.
Structural similarities of bacterial cytokine-binding proteins and proteins involved in cytokine signaling. The bacterial proteins are shown in blue. (A) IrmA compared with the N-terminal Ig-fold domain of β-domain of IL-2R (PDB:2B5I), (B) the C-terminal domain of OprF compared with macrophage migration inhibitory factor (MIF) (PDB:4P7M), (C) the N-terminal PapC domain of Caf1A compared with transcription elongation factor b polypeptide 2 (TCEB2) (PDB:2IZV), and (D) the N0 domain of PilQ compared with human granulocyte macrophage colony stimulating factor receptor (GM-CSF) (PDB:5D71) are shown. Superimpositions were performed using the secondary-structure matching (SSM) tool in Coot. The figures were prepared with PyMol (www.pymol.org).
See this image and copyright information in PMC

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