The interactions of peripheral membrane proteins with biological membranes

Whited, Allison M.; Johs, Alexander

doi:10.1016/j.chemphyslip.2015.07.015

Cited by 83 publications

(60 citation statements)

References 119 publications

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“…This suggests that though mVP40 and eVP40 both rely heavily on electrostatic interactions for membrane association, there is a fundamental difference between the two proteins' mechanism of assembly at the plasma membrane. Many peripheral proteins rely on more than electrostatic interactions for membrane targeting (75), and while it is quite possible the mVP40 dimer electrostatic interactions with the plasma membrane are sufficient to drive NTD displacement and mVP40 oligomerization, further biophysical analysis is warranted to understand the mechanisms of lipid-protein and protein-protein interactions that regulate the mVP40 matrix assembly.…”

Section: Discussionmentioning

confidence: 99%

Investigation of the Lipid Binding Properties of the Marburg Virus Matrix Protein VP40

Wijesinghe

Stahelin

2016

J Virol

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Marburg virus (MARV), which belongs to the virus family Filoviridae, causes hemorrhagic fever in humans and nonhuman primates that is often fatal. MARV is a lipid-enveloped virus that during the replication process extracts its lipid coat from the plasma membrane of the host cell it infects. MARV carries seven genes, one of which encodes its matrix protein VP40 (mVP40), which regulates the assembly and budding of the virions. Currently, little information is available on mVP40 lipid binding properties. Here, we have investigated the in vitro and cellular mechanisms by which mVP40 associates with lipid membranes. mVP40 associates with anionic membranes in a nonspecific manner that is dependent upon the anionic charge density of the membrane. These results are consistent with recent structural determination of mVP40, which elucidated an mVP40 dimer with a flat and extensive cationic lipid binding interface. IMPORTANCEMarburg virus (MARV) is a lipid-enveloped filamentous virus from the family Filoviridae. MARV was discovered in 1967, and yet little is known about how its seven genes are used to assemble and form a new viral particle in the host cell it infects. The MARV matrix protein VP40 (mVP40) underlies the inner leaflet of the virus and regulates budding from the host cell plasma membrane. In vitro and cellular assays in this study investigated the mechanism by which mVP40 associates with lipids. The results demonstrate that mVP40 interactions with lipid vesicles or the inner leaflet of the plasma membrane are electrostatic but nonspecific in nature and are dependent on the anionic charge density of the membrane surface. Small molecules that can disrupt lipid trafficking or reduce the anionic charge of the plasma membrane interface may be useful in inhibiting assembly and budding of MARV. Marburg virus (MARV) and Ebola virus (EBOV) are members of the virus family Filoviridae that are characterized by their filamentous lipid -enveloped morphology (1). Electron microscopy studies revealed that MARV particles have a uniform diameter of approximately 80 nm, with an average particle length of 740 nm (2, 3). MARV harbors a negative-sense RNA genome 19.1 kb in length that includes seven genes (4). The glycoprotein (GP) is a transmembrane protein present in the viral envelope, and it mediates viral entry into the host cell. VP40 is the major matrix protein (mVP40) and completely underlies the lipid envelope of the virus. VP40 alone is sufficient to produce virus-like particles (VLPs) from mammalian cells that are nearly indistinguishable from virions (5-8). In addition to interacting with the host cell membrane and mediating budding, VP40 interacts with the nucleocapsid, which consists of nucleoprotein, VP24, VP30, VP35, and the L protein (9). VP40 also plays other essential roles, such as immunosuppression (10), regulation of viral transcription, and/or replication (11,12), and is also able to interact with GP, coexpression of which leads to GP enrichment at sites of mVP40 budding (13). mVP40 is a peripheral ...

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Section: Discussionmentioning

confidence: 99%

Investigation of the Lipid Binding Properties of the Marburg Virus Matrix Protein VP40

Wijesinghe

Stahelin

2016

J Virol

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“…Different membrane proteins are localized in the plasma membrane of spermatozoa. These proteins have some important functions, for example serving as receptors, ion channels, structural proteins and enzymes (Flesch & Gadella, 2000;Whited & Johs, 2015).…”

Section: Matur Ati On Of S Permatozoa In the Epid Idymismentioning

confidence: 99%

Canine spermatozoa—What do we know about their morphology and physiology? An overview

Chłopik

Wysokińska

2019

Reprod Domestic Animals

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Spermatozoa are unique cells because of their morphological and physiological characteristics. They are produced during the process called spermatogenesis. Spermatogenesis consists of three phases: spermatocytogenesis, spermiogenesis and spermiation, during which spermatozoa undergo several changes. Spermatogenesis takes place within the seminiferous tubules containing two types of cells—the germ cells and the Sertoli cells—that alongside the Leydig cells, which play an important role when it comes to normal fertility. Everything is regulated by the hypothalamic–pituitary–gonadal axis and specific hormones due to multi‐hormonal feedback systems. Spermatozoa possess morphological and physiological features, which are sometimes completely different from what is observed in various somatic cells. What is more, canine spermatozoa have specific characteristics making them special compared to the spermatozoa of other mammalian species. The metabolic energy production, which is crucial for the appropriate functioning of spermatozoa, can be fuelled by different metabolic pathways utilizing different chemical substrates. Inseparable from the oxidative phosphorylation process is the production of reactive oxygen species, which are both essential and toxic to spermatozoa. Furthermore, epididymis is a very important structure, responsible for the transport and maturation of spermatozoa, which are then stored in the last segment of epididymis—the epididymal cauda. Moreover, the retrieval of spermatozoa from the epididymides is crucial for the development of assisted reproduction techniques and sperm cryopreservation methods. The information gained from the research on domestic dogs might be transferred to their wild relatives, especially those species categorized as endangered.

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“…Nowhere is this clearer than for peripheral membrane proteins, a subset of membrane proteins whose principal membrane interactions to the headgroups of membrane lipids. These structurally diverse peripheral proteins[10] are indispensable to cellular signaling [11, 12]. Beyond coupling, peripheral proteins also detoxify small molecules [13], and initiate important biological processes to human health such as the blood coagulation cascade [14] or viral fusion [15].…”

Section: Complementing Experiments With Simulation At the Membrane mentioning

confidence: 99%

“…The proteins studied with the HMMM so far interact with the membrane periphery, and therefore the protein–membrane interactions are accurately captured by the HMMM model [76]. Given the increasing awareness of the importance of lipid–protein interactions in modulating protein function [170, 171] and the ubiquity of peripheral proteins on the membrane surface, simply applying the model to similar systems is an important contribution to the field, supplying mechanistic details to the broad body of evidence suggesting that the function of these proteins is tightly regulated by their interaction with the membrane [11, 171, 172]. …”

Section: Perspectives On Future Hmmm Applicationmentioning

confidence: 99%

Atomic-level description of protein–lipid interactions using an accelerated membrane model

Baylon

Vermaas

Müller

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Peripheral membrane proteins are structurally diverse proteins that are involved in fundamental cellular processes. Their activity of these proteins is frequently modulated through their interaction with cellular membranes, and as a result techniques to study the interfacial interaction between peripheral proteins and the membrane are in high demand. Due to the fluid nature of the membrane and the reversibility of protein–membrane interactions, the experimental study of these systems remains a challenging task. Molecular dynamics simulations offer a suitable approach to study protein–lipid interactions; however, the slow dynamics of the lipids often prevents sufficient sampling of specific membrane–protein interactions in atomistic simulations. To increase lipid dynamics while preserving the atomistic detail of protein–lipid interactions, in the highly mobile membrane-mimetic (HMMM) model the membrane core is replaced by an organic solvent, while short-tailed lipids provide a nearly complete representation of natural lipids at the organic solvent/water interface. Here, we present a brief introduction and a summary of recent applications of the HMMM to study different membrane proteins, complementing the experimental characterization of the presented systems, and we offer a perspective of future applications of the HMMM to study other classes of membrane proteins.

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The interactions of peripheral membrane proteins with biological membranes

Cited by 83 publications

References 119 publications

Investigation of the Lipid Binding Properties of the Marburg Virus Matrix Protein VP40

Investigation of the Lipid Binding Properties of the Marburg Virus Matrix Protein VP40

Canine spermatozoa—What do we know about their morphology and physiology? An overview

Atomic-level description of protein–lipid interactions using an accelerated membrane model

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