Periplasm
The periplasm is a concentrated gel-like
Terminology
Although bacteria are conventionally divided into two main groups—gram-positive and gram-negative, based upon their Gram-stain retention property—this classification system is ambiguous as it can refer to three distinct aspects (staining result, cell-envelope organization, taxonomic group), which do not necessarily coalesce for some bacterial species.[4][5][6][7] In most situations such as in this article, gram-staining reflects the marked differences in the ultrastructure and chemical composition of the two main kinds of bacteria. The usual "gram-positive" type does not have an outer lipid membrane, while the typical "gram-negative" bacterium does. The terms "diderm" and "monoderm", coined to refer to this distinction only, is a more reliable and fundamental characteristic of the bacterial cells.[4][8]
All
Structure
As shown in the figure to the right, the periplasmic space in gram-negative or diderm bacteria is located between the inner and outer membrane of the cell. The periplasm contains peptidoglycan and the membranes that enclose the periplasmic space contain many integral membrane proteins, which can participate in cell signaling. Furthermore, the periplasm houses motility organelles such as the flagellum, which spans both membranes enclosing the periplasm. The periplasm is described as gel-like due to the high abundance of proteins and peptidoglycan. The periplasm occupies 7% to 40% of the total volume of diderm bacteria, and contains up to 30% of cellular proteins.[10][11] The structure of the monoderm periplasm differs from that of diderm bacteria as the so-called periplasmic space in monoderm bacteria is not enclosed by two membranes but is rather enclosed by the cytoplasmic membrane and the peptidoglycan layer beneath.[12] For this reason, the monoderm periplasmic space is also referred to as the inner-wall zone (IWZ). The IWZ serves as the first destination of translocation for proteins being transported across the monoderm bacterial cell wall.[12]
Function
In
The compartmentalization afforded by the periplasmic space gives rise to several important functions. Aside from those previously mentioned, the periplasm also functions in protein transport and quality control, analogous to the endoplasmic reticulum in eukaryotes.[17] Furthermore, the separation of the periplasm from the cytoplasm allows for the compartmentalization of enzymes that could be toxic in the cytoplasm.[17] Some peptidoglycans and lipoproteins located in the periplasm provide a structural support system for the cell that aids in promoting the cell's ability to withstand turgor pressure. Notably, organelles such as the flagellum require the assembly of polymers within the periplasm for proper functioning. As the driveshaft of the flagellum spans the periplasmic space, its length is dictated by positioning of the outer membrane as induced by its contraction, which is mediated by periplasmic polymers.[17] The periplasm also functions in cell signaling, such as in the case of the lipoprotein RcsF, which has a globular domain residing in the periplasm and acts as a stress sensor. When RcsF fails to interact with BamA, such as in the case of an enlarged periplasm, RcsF is not exported to the cell surface and are able to trigger the Rcs signaling cascade. Periplasm size, therefore, plays an important role in stress signaling.[18][17]
Clinical significance
As bacteria are the responsible pathogen for many infections and illnesses, the biochemical and structural components that distinguish disease causing bacterial cells from native eukaryotic cells are of great interest from a clinical perspective.[19] Gram-negative bacteria tend to be more antimicrobial resistant than gram-positive bacteria, and also possess a much more significant periplasmic space between their two membrane bilayers. Since eukaryotes do not possess a periplasmic space, structures and enzymes found in the gram-negative periplasm are attractive targets for antimicrobial drug therapies.[20] Additionally, vital functions such as facilitation of protein folding, protein transport, cell signaling, structural integrity, and nutrient uptake are performed by periplasm components,[17] making it rich in potential drug targets. Aside from enzymes and structural components that are vital to cell function and survival, the periplasm also contains virulence-associated proteins such as DsbA that can be targeted by antimicrobial therapies.[21] Due to their role in catalyzing disulfide bond formation for a variety of virulence factors, the DsbA/DsbB system has been of particular interest as a target for anti-virulence drugs.[22]
The periplasmic space is deeply interconnected with the pathogenesis of disease in the setting of microbial infection. Many of the virulence factors associated with bacterial pathogenicity are secretion proteins, which are often subject to post-translational modification including disulfide bond formation.[23] The oxidative environment of the periplasm contains Dsb (disulfide bond formation) proteins that catalyze such post-translational modifications, and therefore play an important role in establishing virulence factor tertiary and quaternary structure essential for proper protein function.[23] In addition to Dsb proteins found in the periplasm, motility organelles such as the flagellum are also essential for host infection. The flagellum is rooted in the periplasm and is stabilized by interaction with periplasmic structural components,[17][23] and is therefore another pathogenesis-related target for antimicrobial agents. During infection of a host, the cell of a bacterium is subject to many turbulent environmental conditions, which highlights the importance of the structural integrity afforded by the periplasm. In particular, peptidoglycan synthesis is vital to cell wall production, and inhibitors of peptidoglycan synthesis have been of clinical interest for targeting bacteria for many decades.[24][25] Furthermore, the periplasm is also relevant to clinical developments by way of its role in mediating the uptake of transforming DNA.[16]
References
- S2CID 11013569.
- ^ PMID 16952957.
- ISBN 3-540-42608-6.
- ^ PMID 9841678.
- ^ S2CID 30541897.
- PMID 19299134.
- PMID 20637628.
- ^ S2CID 41206658.
- PMID 21717204.
- ISSN 0003-2700.
- .
- ^ PMID 22471582.
- ISBN 0-07-295175-3.
- PMID 4284300.
- PMID 22901060.
- ^ PMID 34126763.
- ^ PMID 29342145.
- PMID 32572278.
- PMID 26343252.
- PMID 32786281.
- PMID 12595484.
- PMID 27438817.
- ^ PMID 17696887.
- PMID 36947615.
- PMID 4202341.
Further reading
- White D (2000). The Physiology and Biochemistry of Prokaryotes (2nd ed.). Oxford: Oxford University Press. p. 22. ISBN 978-0-19-512579-5.