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Intracellular proteins moonlighting as bacterial adhesion factors - PubMed

  • ️Mon Jan 01 2018

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Intracellular proteins moonlighting as bacterial adhesion factors

Constance Jeffery. AIMS Microbiol. 2018.

Abstract

Pathogenic and commensal, or probiotic, bacteria employ adhesins on the cell surface to attach to and interact with the host. Dozens of the adhesins that play key roles in binding to host cells or extracellular matrix were originally identified as intracellular chaperones or enzymes in glycolysis or other central metabolic pathways. Proteins that have two very different functions, often in two different subcellular locations, are referred to as moonlighting proteins. The intracellular/surface moonlighting proteins do not contain signal sequences for secretion or known sequence motifs for binding to the cell surface, so in most cases is not known how these proteins are secreted or how they become attached to the cell surface. A secretion system in which a large portion of the pool of each protein remains inside the cell while some of the pool of the protein is partitioned to the cell surface has not been identified. This may involve a novel version of a known secretion system or it may involve a novel secretion system. Understanding the processes by which intracellular/cell surface moonlighting proteins are targeted to the cell surface could provide novel protein targets for the development of small molecules that block secretion and/or association with the cell surface and could serve as lead compounds for the development of novel antibacterial therapeutics.

Keywords: adhesion; moonlighting proteins; multifunctional proteins.

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Conflict of interest statement

Conflict of interest: The author declares no conflict of interest in this paper.

Figures

Figure 1.
Figure 1.. Intracellular enzymes and chaperones can function as adhesins on the bacterial cell surface. An ISMP can function as an enzyme inside of the cell and an adhesin when located on the cell surface. Enolase is found in the cytoplasm in almost all species where it converts 2-phosphoglycerate to phosphoenolpyruvate as the ninth step of glycolysis. In many species of bacteria, it is also found on the cell surface where it can bind to the host's extracellular matrix or airway mucins. For pathogenic bacteria, this attachment can be important for invading host tissues and promoting infection. In most cases, how the intracellular enzyme is transported outside the cell and how it becomes attached to the cell surface are not known (curved arrow). There might be a receptor for the protein on the bacterial cell surface (hexagon), but the nature of the surface attachment is known for only a few ISMPs.

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