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Membranes
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Membrane Proteins: Function, Structure, and Dynamic
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Membrane Proteins: Function, Structure, and Dynamic

A special issue of Membranes (ISSN 2077-0375). This special issue belongs to the section "Biological Membrane Composition and Structures".

Deadline for manuscript submissions: closed (20 June 2023) | Viewed by 32473

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editors

Dr. Yosuke Senju

E-Mail Website
Guest Editor
Research Institute for Interdisciplinary Science (RIIS), Okayama University, Okayama 700-8530, Japan
Interests: protein-lipid interaction; biomimetics; drug delivery system (DDS); biophysics; thermodynamics; synthetic biology; self-assembly; rheology; phase separation; biomembranes; lipid; liposome; cytoskeleton/cell motility; actin; structural biology; drug discovery
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Shiro Suetsugu

E-Mail Website
Guest Editor
1. Division of Biological Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, Nara 630-0192, Japan
2. Data Science Center, Nara Institute of Science and Technology, Nara 630-0192, Japan
3. Center for Digital Green-Innovation, Nara Institute of Science and Technology, Nara 630-0192, Japan
Interests: mechanisms of cell shaping and cell fate determination
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We are pleased to invite you to the Special Issue “Membrane Proteins: Function, Structure, and Dynamics.” Many proteins are known to interact with cell and subcellular membranes. These include transmembrane proteins (e.g., ion channels, transmembrane receptors, and transporters), which integrate into the lipid bilayers to transport molecules and ions across membranes, and peripheral membrane proteins, which temporarily associate with the membranes via electrostatic and/or hydrophobic interactions by dividing their amphipathic helix into lipid bilayers. These protein–lipid interactions determine protein conformations and precisely regulate the activation and localization of molecular complexes at their respective membranes. These signaling pathways play vital roles in various cellular processes, such as membrane trafficking and signal transduction. Furthermore, membrane proteins are involved in many diseases, including cancer and Alzheimer’s; thus, their possible applications in drug design should be considered. However, due to the complexity of the abundant lipid–protein/protein–protein interactions at the cell membranes, an exact understanding of the molecular and cellular mechanisms of membrane proteins has yet to be achieved.

This Special Issue aims to present recent advances in the function, structure, and dynamics of membrane proteins from various perspectives. These studies will shed light on the structural and physiological functions of membrane proteins and provide new insights into their fundamental workings.

Both original research articles and reviews are welcome. Areas of interest may include (but are not limited to) the following: cell biology, biochemistry, and biophysics, including structural biology and molecular dynamics (MD) simulations. Multidisciplinary approaches will also be considered. We look forward to receiving your contributions.

Dr. Yosuke Senju
Prof. Dr. Shiro Suetsugu
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Membranes is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • receptors
  • channels
  • transporters
  • lipid–protein interactions
  • signal transduction
  • membrane traffic
  • organelle
  • membrane contact sites
  • allosteric regulation
  • model membranes and liposomes

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Related Special Issue

Published Papers (13 papers)

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Editorial

Jump to: Research, Review

3 pages, 188 KiB  
Editorial
Membrane Proteins: Function, Structure, and Dynamics
by Yosuke Senju and Shiro Suetsugu
Membranes 2023, 13(12), 904; https://doi.org/10.3390/membranes13120904 - 9 Dec 2023
Viewed by 3458
Abstract
Plasma and intracellular membranes are characterized by different lipid compositions that enable proteins to localize to distinct subcellular compartments [...] Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)

Research

Jump to: Editorial, Review

17 pages, 14177 KiB  
Article
Cholesterol in Class C GPCRs: Role, Relevance, and Localization
by Ugochi H. Isu, Shadi A Badiee, Ehsaneh Khodadadi and Mahmoud Moradi
Membranes 2023, 13(3), 301; https://doi.org/10.3390/membranes13030301 - 3 Mar 2023
Cited by 7 | Viewed by 2843
Abstract
G-protein coupled receptors (GPCRs), one of the largest superfamilies of cell-surface receptors, are heptahelical integral membrane proteins that play critical roles in virtually every organ system. G-protein-coupled receptors operate in membranes rich in cholesterol, with an imbalance in cholesterol level within the vicinity [...] Read more.
G-protein coupled receptors (GPCRs), one of the largest superfamilies of cell-surface receptors, are heptahelical integral membrane proteins that play critical roles in virtually every organ system. G-protein-coupled receptors operate in membranes rich in cholesterol, with an imbalance in cholesterol level within the vicinity of GPCR transmembrane domains affecting the structure and/or function of many GPCRs, a phenomenon that has been linked to several diseases. These effects of cholesterol could result in indirect changes by altering the mechanical properties of the lipid environment or direct changes by binding to specific sites on the protein. There are a number of studies and reviews on how cholesterol modulates class A GPCRs; however, this area of study is yet to be explored for class C GPCRs, which are characterized by a large extracellular region and often form constitutive dimers. This review highlights specific sites of interaction, functions, and structural dynamics involved in the cholesterol recognition of the class C GPCRs. We summarize recent data from some typical family members to explain the effects of membrane cholesterol on the structural features and functions of class C GPCRs and speculate on their corresponding therapeutic potential. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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16 pages, 2246 KiB  
Article
Effect of Cytochrome C on the Conductance of Asolectin Membranes and the Occurrence of Through Pores at Different pHs
by Andrey Anosov, Elizaveta Borisova, Elena Smirnova, Eugenia Korepanova and Anatoly Osipov
Membranes 2023, 13(3), 268; https://doi.org/10.3390/membranes13030268 - 24 Feb 2023
Cited by 2 | Viewed by 1179
Abstract
The study of the electrical parameters of asolectin bilayer lipid membranes in the presence of cytochrome c (cyt c) at various concentrations showed that an increase in the concentration of cyt c leads to an increase in the membrane conductance and the appearance [...] Read more.
The study of the electrical parameters of asolectin bilayer lipid membranes in the presence of cytochrome c (cyt c) at various concentrations showed that an increase in the concentration of cyt c leads to an increase in the membrane conductance and the appearance of through pores. The studied membranes did not contain cardiolipin, which is commonly used in studying the effect of cyt c on membrane permeability. In the presence of cyt c, discrete current fluctuations were recorded. The occurrence of these fluctuations may be associated with the formation of through pores. The diameter of these pores was ~0.8 nm, which is smaller than the size of the cyt c globule (~3 nm). Measurements carried out at pH values from 6.4 to 8.4 showed that the concentration dependence of the membrane conductance increases with increasing pH. To assess the binding of cyt c to the bilayer, we measured the concentration and pH dependences of the difference in surface potentials induced by the unilateral addition of cyt c. The amount of bound cyt c at the same concentrations decreased with increasing pH, which did not correspond to the conductance trend. An analysis of conductance traces leads to the conclusion that an increase in the integral conductance of membranes is associated with an increase in the lifetime of pores. The formation of “long-lived” pores, of which the residence time in the open state is longer than in the closed state, was achieved at various combinations of pHs and cyt c concentrations: the higher the pH, the lower the concentration at which the long-lived pores appeared and, accordingly, a higher conductance was observed. The increase in conductance and the formation of transmembrane pores are not due to the electrostatic interaction between cyt c and the membrane. We hypothesize that an increase in pH leads to a weakening of hydrogen bonds between lipid heads, which allows cyt c molecules to penetrate into the membrane. This disrupts the order of the bilayer and leads to the occurrence of through pores. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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12 pages, 3330 KiB  
Article
Borate Transporters and SLC4 Bicarbonate Transporters Share Key Functional Properties
by Jean L. Beltran, Lila G. McGrath, Sophia Caruso, Richara K. Bain, Claire E. Hendrix, Hana Kamran, Hartlee G. Johnston, Rebecca M. Collings, Menkara-Chinua N. Henry, Tsega-Ab L. Abera, Valeria A. Donoso, Erin C. Carriker and Bryan H. Thurtle-Schmidt
Membranes 2023, 13(2), 235; https://doi.org/10.3390/membranes13020235 - 15 Feb 2023
Cited by 2 | Viewed by 2088
Abstract
Borate transporters are membrane transport proteins that regulate intracellular borate levels. In plants, borate is a micronutrient essential for growth but is toxic in excess, while in yeast, borate is unnecessary for growth and borate export confers tolerance. Borate transporters share structural homology [...] Read more.
Borate transporters are membrane transport proteins that regulate intracellular borate levels. In plants, borate is a micronutrient essential for growth but is toxic in excess, while in yeast, borate is unnecessary for growth and borate export confers tolerance. Borate transporters share structural homology with human bicarbonate transporters in the SLC4 family despite low sequence identity and differences in transported solutes. Here, we characterize the S. cerevisiae borate transporter Bor1p and examine whether key biochemical features of SLC4 transporters extend to borate transporters. We show that borate transporters and SLC4 transporters share multiple properties, including lipid-promoted dimerization, sensitivity to stilbene disulfonate-derived inhibitors, and a requirement for an acidic residue at the solute binding site. We also identify several amino acids critical for Bor1p function and show that disease-causing mutations in human SLC4A1 will eliminate in vivo function when their homologous mutations are introduced in Bor1p. Our data help elucidate mechanistic features of Bor1p and reveal significant functional properties shared between borate transporters and SLC4 transporters. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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13 pages, 4630 KiB  
Article
Stabilization of Cereibacter sphaeroides Photosynthetic Reaction Center by the Introduction of Disulfide Bonds
by Georgii Selikhanov, Anastasia Atamas, Diana Yukhimchuk, Tatiana Fufina, Lyudmila Vasilieva and Azat Gabdulkhakov
Membranes 2023, 13(2), 154; https://doi.org/10.3390/membranes13020154 - 25 Jan 2023
Cited by 2 | Viewed by 2036
Abstract
The photosynthetic reaction center of the purple nonsulfur bacterium Cereibacter sphaeroides is a useful model for the study of mechanisms of photoinduced electron transfer and a promising component for photo-bio-electrocatalytic systems. The basic research and technological applications of this membrane pigment-protein complex require [...] Read more.
The photosynthetic reaction center of the purple nonsulfur bacterium Cereibacter sphaeroides is a useful model for the study of mechanisms of photoinduced electron transfer and a promising component for photo-bio-electrocatalytic systems. The basic research and technological applications of this membrane pigment-protein complex require effective approaches to increase its structural stability. In this work, a rational design approach to genetically modify the reaction centers by introducing disulfide bonds is used. This resulted in significantly increasing the thermal stability of some of the mutant pigment-protein complexes. The formation of the S-S bonds was confirmed by X-ray crystallography as well as SDS-PAGE, and the optical properties of the reaction centers were studied. The genetically modified reaction centers presented here preserved their ability for photochemical charge separation and could be of interest for basic science and biotechnology. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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23 pages, 57566 KiB  
Article
Mechanism of Action and Structure–Activity Relationships of Tetracyclic Small Molecules Acting as Universal Positive Allosteric Modulators of the Cholecystokinin Receptor
by Daniela G. Dengler, Kaleeckal G. Harikumar, Alice Yen, Eduard A. Sergienko and Laurence J. Miller
Membranes 2023, 13(2), 150; https://doi.org/10.3390/membranes13020150 - 24 Jan 2023
Cited by 1 | Viewed by 1576
Abstract
As part of an ongoing effort to develop a drug targeting the type 1 cholecystokinin receptor (CCK1R) to help prevent and/or treat obesity, we recently performed a high throughput screening effort of small molecules seeking candidates that enhanced the action of the natural [...] Read more.
As part of an ongoing effort to develop a drug targeting the type 1 cholecystokinin receptor (CCK1R) to help prevent and/or treat obesity, we recently performed a high throughput screening effort of small molecules seeking candidates that enhanced the action of the natural agonist, CCK, thus acting as positive allosteric modulators without exhibiting intrinsic agonist action. Such probes would be expected to act in a temporally finite way to enhance CCK action to induce satiety during and after a meal and potentially even modulate activity at the CCK1R in a high cholesterol environment present in some obese patients. The current work focuses on the best scaffold, representing tetracyclic molecules identified through high throughput screening we previously reported. Extensive characterization of the two top “hits” from the previous effort demonstrated them to fulfill the desired pharmacologic profile. We undertook analog-by-catalog expansion of this scaffold using 65 commercially available analogs. In this effort, we were able to eliminate an off-target effect observed for this scaffold while retaining its activity as a positive allosteric modulator of CCK1R in both normal and high cholesterol membrane environments. These insights should be useful in the rational medicinal chemical enhancement of this scaffold and in the future development of candidates to advance to pre-clinical proof-of-concept and to clinical trials. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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13 pages, 2827 KiB  
Article
Investigation of Phosphatidylserine-Transporting Activity of Human TMEM16C Isoforms
by Hanggu Kim, Eunyoung Kim and Byoung-Cheol Lee
Membranes 2022, 12(10), 1005; https://doi.org/10.3390/membranes12101005 - 17 Oct 2022
Cited by 8 | Viewed by 1956
Abstract
Lipid scrambling is a rapid process that dissipates the asymmetrical distribution of phospholipids in the plasma membrane. It is involved in various physiological functions such as blood coagulation and apoptosis. Many TMEM16 members are recognized as Ca2+-activated phospholipid scramblases, which transport [...] Read more.
Lipid scrambling is a rapid process that dissipates the asymmetrical distribution of phospholipids in the plasma membrane. It is involved in various physiological functions such as blood coagulation and apoptosis. Many TMEM16 members are recognized as Ca2+-activated phospholipid scramblases, which transport phospholipids between the two leaflets of the plasma membrane nonspecifically and bidirectionally; among these, TMEM16C is abundant in the brain, especially in neuronal cells. We investigated the scrambling activity of three human TMEM16C isoforms with different N-terminus lengths. After optimizing conditions to minimize endogenous scrambling activity, an annexin V-based imaging assay was used to detect phosphatidylserine (PS) scrambling in 293T cells. Unlike previous results, our data showed that human TMEM16C isoform 1 and isoform 3 exposed PS to the cell surface. A surface biotinylation assay showed that the surface expression of isoform 2, which did not show scrambling activity, was ~5 times lower than the other isoforms. In contrast to other TMEM16 proteins, flux assays and electrophysiology recording showed TMEM16C does not possess ion-transporting activity. We conclude that the N-terminus of TMEM16C determines whether TMEM16C can translocate to the plasma membrane and facilitate scrambling activity; membrane-localized TMEM16C isoforms 1 and 3 transport PS to the outer leaflet. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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20 pages, 3408 KiB  
Article
Precise Detection and Visualization of Nanoscale Temporal Confinement in Single-Molecule Tracking Analysis
by Manon Westra and Harold D. MacGillavry
Membranes 2022, 12(7), 650; https://doi.org/10.3390/membranes12070650 - 24 Jun 2022
Cited by 3 | Viewed by 2985
Abstract
The plasma membrane consists of a diverse mixture of molecules that dynamically assemble into a highly non-random organization. The formation of nanoscale domains in the membrane is of particular interest as these domains underlie critical cellular functions. Single-molecule tracking is a powerful method [...] Read more.
The plasma membrane consists of a diverse mixture of molecules that dynamically assemble into a highly non-random organization. The formation of nanoscale domains in the membrane is of particular interest as these domains underlie critical cellular functions. Single-molecule tracking is a powerful method to detect and quantify molecular motion at high temporal and spatial resolution and has therefore been instrumental in understanding mechanisms that underlie membrane organization. In single-molecule trajectories, regions of temporal confinement can be determined that might reveal interesting biophysical interactions important for domain formation. However, analytical methods for the detection of temporal confinement in single-molecule trajectories depend on a variety of parameters that heavily depend on experimental factors and the influence of these factors on the performance of confinement detection are not well understood. Here, we present elaborate confinement analyses on simulated random walks and trajectories that display transient confined behavior to optimize the parameters for different experimental conditions. Furthermore, we demonstrate a heatmap visualization tool that allows spatial mapping of confinement hotspots relative to subcellular markers. Using these optimized tools, we reliably detected subdiffusive behavior of different membrane components and observed differences in the confinement behavior of two types of glutamate receptors in neurons. This study will help in further understanding the dynamic behavior of the complex membrane and its role in cellular functioning. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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Review

Jump to: Editorial, Research

12 pages, 14107 KiB  
Review
Interfacial Enzymes Enable Gram-Positive Microbes to Eat Fatty Acids
by Christopher D. Radka
Membranes 2023, 13(4), 423; https://doi.org/10.3390/membranes13040423 - 10 Apr 2023
Cited by 4 | Viewed by 1974
Abstract
Exogenous fatty acid (eFA) activation and utilization play key roles in bacterial physiology and confer growth advantages by bypassing the need to make fatty acids for lipid synthesis. In Gram-positive bacteria, eFA activation and utilization is generally carried out by the fatty acid [...] Read more.
Exogenous fatty acid (eFA) activation and utilization play key roles in bacterial physiology and confer growth advantages by bypassing the need to make fatty acids for lipid synthesis. In Gram-positive bacteria, eFA activation and utilization is generally carried out by the fatty acid kinase (FakAB) two-component system that converts eFA to acyl phosphate, and the acyl-ACP:phosphate transacylase (PlsX) that catalyzes the reversible conversion of acyl phosphate to acyl–acyl carrier protein. Acyl–acyl carrier protein is a soluble format of the fatty acid that is compatible with cellular metabolic enzymes and can feed multiple processes including the fatty acid biosynthesis pathway. The combination of FakAB and PlsX enables the bacteria to channel eFA nutrients. These key enzymes are peripheral membrane interfacial proteins that associate with the membrane through amphipathic helices and hydrophobic loops. In this review, we discuss the biochemical and biophysical advances that have established the structural features that drive FakB or PlsX association with the membrane, and how these protein–lipid interactions contribute to enzyme catalysis. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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18 pages, 2358 KiB  
Review
Dimerization of Transmembrane Proteins in Cancer Immunotherapy
by Lei Li and Jingying Li
Membranes 2023, 13(4), 393; https://doi.org/10.3390/membranes13040393 - 30 Mar 2023
Cited by 2 | Viewed by 2288
Abstract
Transmembrane proteins (TMEMs) are integrated membrane proteins that span the entire lipid bilayer and are permanently anchored to it. TMEMs participate in various cellular processes. Some TMEMs usually exist and perform their physiological functions as dimers rather than monomers. TMEM dimerization is associated [...] Read more.
Transmembrane proteins (TMEMs) are integrated membrane proteins that span the entire lipid bilayer and are permanently anchored to it. TMEMs participate in various cellular processes. Some TMEMs usually exist and perform their physiological functions as dimers rather than monomers. TMEM dimerization is associated with various physiological functions, such as the regulation of enzyme activity, signal transduction, and cancer immunotherapy. In this review, we focus on the dimerization of transmembrane proteins in cancer immunotherapy. This review is divided into three parts. First, the structures and functions of several TMEMs related to tumor immunity are introduced. Second, the characteristics and functions of several typical TMEM dimerization processes are analyzed. Finally, the application of the regulation of TMEM dimerization in cancer immunotherapy is introduced. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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14 pages, 6715 KiB  
Review
Molecular Dynamics Simulations of the Proteins Regulating Synaptic Vesicle Fusion
by Maria Bykhovskaia
Membranes 2023, 13(3), 307; https://doi.org/10.3390/membranes13030307 - 6 Mar 2023
Cited by 2 | Viewed by 2027
Abstract
Neuronal transmitters are packaged in synaptic vesicles (SVs) and released by the fusion of SVs with the presynaptic membrane (PM). An inflow of Ca2+ into the nerve terminal triggers fusion, and the SV-associated protein Synaptotagmin 1 (Syt1) serves as a Ca2+ [...] Read more.
Neuronal transmitters are packaged in synaptic vesicles (SVs) and released by the fusion of SVs with the presynaptic membrane (PM). An inflow of Ca2+ into the nerve terminal triggers fusion, and the SV-associated protein Synaptotagmin 1 (Syt1) serves as a Ca2+ sensor. In preparation for fusion, SVs become attached to the PM by the SNARE protein complex, a coiled-coil bundle that exerts the force overcoming SV-PM repulsion. A cytosolic protein Complexin (Cpx) attaches to the SNARE complex and differentially regulates the evoked and spontaneous release components. It is still debated how the dynamic interactions of Syt1, SNARE proteins and Cpx lead to fusion. This problem is confounded by heterogeneity in the conformational states of the prefusion protein–lipid complex and by the lack of tools to experimentally monitor the rapid conformational transitions of the complex, which occur at a sub-millisecond scale. However, these complications can be overcome employing molecular dynamics (MDs), a computational approach that enables simulating interactions and conformational transitions of proteins and lipids. This review discusses the use of molecular dynamics for the investigation of the pre-fusion protein–lipid complex. We discuss the dynamics of the SNARE complex between lipid bilayers, as well as the interactions of Syt1 with lipids and SNARE proteins, and Cpx regulating the assembly of the SNARE complex. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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18 pages, 2254 KiB  
Review
Entamoeba histolytica: Membrane and Non-Membrane Protein Structure, Function, Immune Response Interaction, and Vaccine Development
by Nurhana Jasni, Syazwan Saidin, Wong Weng Kin, Norsyahida Arifin and Nurulhasanah Othman
Membranes 2022, 12(11), 1079; https://doi.org/10.3390/membranes12111079 - 31 Oct 2022
Cited by 4 | Viewed by 3495
Abstract
Entamoeba histolytica is a protozoan parasite that is the causative agent of amoebiasis. This parasite has caused widespread infection in India, Africa, Mexico, and Central and South America, and results in 100,000 deaths yearly. An immune response is a body's mechanism for eradicating [...] Read more.
Entamoeba histolytica is a protozoan parasite that is the causative agent of amoebiasis. This parasite has caused widespread infection in India, Africa, Mexico, and Central and South America, and results in 100,000 deaths yearly. An immune response is a body's mechanism for eradicating and fighting against substances it sees as harmful or foreign. E. histolytica biological membranes are considered foreign and immunogenic to the human body, thereby initiating the body's immune responses. Understanding immune response and antigen interaction are essential for vaccine development. Thus, this review aims to identify and understand the protein structure, function, and interaction of the biological membrane with the immune response, which could contribute to vaccine development. Furthermore, the current trend of vaccine development studies to combat amoebiasis is also reviewed. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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22 pages, 614 KiB  
Review
The Role of Outer Membrane Proteins in UPEC Antimicrobial Resistance: A Systematic Review
by Inês C. Rodrigues, Sílvia C. Rodrigues, Filipe V. Duarte, Paula M. da Costa and Paulo M. da Costa
Membranes 2022, 12(10), 981; https://doi.org/10.3390/membranes12100981 - 10 Oct 2022
Cited by 12 | Viewed by 2837
Abstract
Uropathogenic Escherichia coli (UPEC) are one of the most common agents of urinary tract infection. In the last decade, several UPEC strains have acquired antibiotic resistance mechanisms and some have become resistant to all classes of antibiotics. UPEC outer membrane proteins (OMPs) seem [...] Read more.
Uropathogenic Escherichia coli (UPEC) are one of the most common agents of urinary tract infection. In the last decade, several UPEC strains have acquired antibiotic resistance mechanisms and some have become resistant to all classes of antibiotics. UPEC outer membrane proteins (OMPs) seem to have a decisive role not only in the processes of invasion and colonization of the bladder mucosa, but also in mechanisms of drug resistance, by which bacteria avoid killing by antimicrobial molecules. This systematic review was performed according to the PRISMA guidelines, aiming to characterize UPEC OMPs and identify their potential role in antimicrobial resistance. The search was limited to studies in English published during the last decade. Twenty-nine studies were included for revision and, among the 76 proteins identified, seven were associated with antibiotic resistance. Indeed, OmpC was associated with β-lactams resistance and OmpF with β-lactams and fluoroquinolone resistance. In turn, TolC, OmpX, YddB, TosA and murein lipoprotein (Lpp) were associated with fluoroquinolones, enrofloxacin, novobiocin, β-lactams and globomycin resistances, respectively. The clinical implications of UPEC resistance to antimicrobial agents in both veterinary and human medicine must propel the implementation of new strategies of administration of antimicrobial agents, while also promoting the development of improved antimicrobials, protective vaccines and specific inhibitors of virulence and resistance factors. Full article
(This article belongs to the Special Issue Membrane Proteins: Function, Structure, and Dynamic)
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