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Article ; Online: Evaluation of Phenol-Substituted Diphyllin Derivatives as Selective Antagonists for Ebola Virus Entry.

Plescia, Caroline B / Lindstrom, Aaron R / Quintero, Maritza V / Keiser, Patrick / Anantpadma, Manu / Davey, Robert / Stahelin, Robert V / Davisson, V Jo

ACS infectious diseases

2022 Volume 8, Issue 5, Page(s) 942–957

Abstract: Ebola virus (EBOV) is an aggressive filoviral pathogen that can induce severe hemorrhagic fever in humans with up to 90% fatality rate. To date, there are no clinically effective small-molecule drugs for postexposure therapies to treat filoviral ... ...

Abstract	Ebola virus (EBOV) is an aggressive filoviral pathogen that can induce severe hemorrhagic fever in humans with up to 90% fatality rate. To date, there are no clinically effective small-molecule drugs for postexposure therapies to treat filoviral infections. EBOV cellular entry and infection involve uptake via macropinocytosis, navigation through the endocytic pathway, and pH-dependent escape into the cytoplasm. We report the inhibition of EBOV cell entry via selective inhibition of vacuolar (V)-ATPase by a new series of phenol-substituted derivatives of the natural product scaffold diphyllin. In cells challenged with Ebola virus, the diphyllin derivatives inhibit viral entry dependent upon structural variations to low nanomolar potencies. Mechanistically, the diphyllin derivatives had no effect on uptake and colocalization of viral particles with endocytic marker LAMP1 but directly modulated endosomal pH. The most potent effects were reversible exhibiting higher selectivity than bafilomycin or the parent diphyllin. Unlike general lysosomotrophic agents, the diphyllin derivatives showed no major disruptions of endocytic populations or morphology when examined with Rab5 and LAMP1 markers. The dilated vacuole phenotype induced by apilimod treatment or in constitutively active Rab5 mutant Q79L-expressing cells was both blocked and reversed by the diphyllin derivatives. The results are consistent with the action of the diphyllin scaffold as a selective pH-dependent viral entry block in late endosomes. Overall, the compounds show improved selectivity and minimal cytotoxicity relative to classical endosomal acidification blocking agents.
MeSH term(s)	Benzodioxoles/pharmacology ; Ebolavirus ; Hemorrhagic Fever, Ebola/drug therapy ; Humans ; Lignans ; Phenol/pharmacology ; Phenol/therapeutic use ; Virus Internalization
Chemical Substances	Benzodioxoles ; Lignans ; Phenol (339NCG44TV) ; diphyllin (W4PN5LDP26)
Language	English
Publishing date	2022-03-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2373-8227
ISSN (online)	2373-8227
DOI	10.1021/acsinfecdis.1c00474
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Article ; Online: Characterization of the Relationship between the Chaperone and Lipid-Binding Functions of the 70-kDa Heat-Shock Protein, HspA1A.

Smulders, Larissa / Daniels, Amanda J / Plescia, Caroline B / Berger, Devon / Stahelin, Robert V / Nikolaidis, Nikolas

International journal of molecular sciences

2020 Volume 21, Issue 17

Abstract: HspA1A, a molecular chaperone, translocates to the plasma membrane (PM) of stressed and cancer cells. This translocation results in HspA1A's cell-surface presentation, which renders tumors radiation insensitive. To specifically inhibit the lipid-driven ... ...

Abstract	HspA1A, a molecular chaperone, translocates to the plasma membrane (PM) of stressed and cancer cells. This translocation results in HspA1A's cell-surface presentation, which renders tumors radiation insensitive. To specifically inhibit the lipid-driven HspA1A's PM translocation and devise new therapeutics it is imperative to characterize the unknown HspA1A's lipid-binding regions and determine the relationship between the chaperone and lipid-binding functions. To elucidate this relationship, we determined the effect of phosphatidylserine (PS)-binding on the secondary structure and chaperone functions of HspA1A. Circular dichroism revealed that binding to PS resulted in minimal modification on HspA1A's secondary structure. Measuring the release of inorganic phosphate revealed that PS-binding had no effect on HspA1A's ATPase activity. In contrast, PS-binding showed subtle but consistent increases in HspA1A's refolding activities. Furthermore, using a Lysine-71-Alanine mutation (K71A; a null-ATPase mutant) of HspA1A we show that although K71A binds to PS with affinities similar to the wild-type (WT), the mutated protein associates with lipids three times faster and dissociates 300 times faster than the WT HspA1A. These observations suggest a two-step binding model including an initial interaction of HspA1A with lipids followed by a conformational change of the HspA1A-lipid complex, which accelerates the binding reaction. Together these findings strongly support the notion that the chaperone and lipid-binding activities of HspA1A are dependent but the regions mediating these functions do not overlap and provide the basis for future interventions to inhibit HspA1A's PM-translocation in tumor cells, making them sensitive to radiation therapy.
MeSH term(s)	Adenosine Triphosphate/metabolism ; Amino Acid Substitution ; Animals ; Circular Dichroism ; HSP70 Heat-Shock Proteins/chemistry ; HSP70 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; Liposomes/chemistry ; Liposomes/metabolism ; Lysine/genetics ; Mice ; Molecular Chaperones/metabolism ; Mutation ; Phosphatidylcholines/metabolism ; Phosphatidylserines/chemistry ; Phosphatidylserines/metabolism ; Protein Binding ; Protein Refolding ; Protein Structure, Secondary ; Surface Plasmon Resonance
Chemical Substances	HSP70 Heat-Shock Proteins ; Hsp70.3 protein, mouse ; Liposomes ; Molecular Chaperones ; Phosphatidylcholines ; Phosphatidylserines ; dipalmitoylphosphatidylserine (3036-82-6) ; 1-palmitoyl-2-oleoylglycero-3-phosphoserine (40290-44-6) ; Adenosine Triphosphate (8L70Q75FXE) ; Lysine (K3Z4F929H6)
Language	English
Publishing date	2020-08-20
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21175995
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Article ; Online: Structural Effect on the Cellular Selectivity of an NIR-Emitting Cyanine Probe: From Lysosome to Simultaneous Nucleus and Mitochondria Selectivity with Potential for Monitoring Mitochondria Dysfunction in Cells.

Abeywickrama, Chathura S / Bertman, Keti A / Plescia, Caroline B / Stahelin, Robert V / Pang, Yi

ACS applied bio materials

2019 Volume 2, Issue 11, Page(s) 5174–5181

Abstract: Bright red to NIR emitting cyanine ... ...

Abstract	Bright red to NIR emitting cyanine probes
Language	English
Publishing date	2019-11-07
Publishing country	United States
Document type	Journal Article
ISSN	2576-6422
ISSN (online)	2576-6422
DOI	10.1021/acsabm.9b00810
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Article ; Online: Phosphatidylserine clustering by the Ebola virus matrix protein is a critical step in viral budding.

Husby, Monica L / Amiar, Souad / Prugar, Laura I / David, Emily A / Plescia, Caroline B / Huie, Kathleen E / Brannan, Jennifer M / Dye, John M / Pienaar, Elsje / Stahelin, Robert V

EMBO reports

2022 Volume 23, Issue 11, Page(s) e51709

Abstract: Phosphatidylserine (PS) is a critical lipid factor in the assembly and spread of numerous lipid-enveloped viruses. Here, we describe the ability of the Ebola virus (EBOV) matrix protein eVP40 to induce clustering of PS and promote viral budding in vitro, ...

Abstract	Phosphatidylserine (PS) is a critical lipid factor in the assembly and spread of numerous lipid-enveloped viruses. Here, we describe the ability of the Ebola virus (EBOV) matrix protein eVP40 to induce clustering of PS and promote viral budding in vitro, as well as the ability of an FDA-approved drug, fendiline, to reduce PS clustering and subsequent virus budding and entry. To gain mechanistic insight into fendiline inhibition of EBOV replication, multiple in vitro assays were run including imaging, viral budding and viral entry assays. Fendiline lowers PS content in mammalian cells and PS in the plasma membrane, where the ability of VP40 to form new virus particles is greatly lower. Further, particles that form from fendiline-treated cells have altered particle morphology and cannot significantly infect/enter cells. These complementary studies reveal the mechanism by which EBOV matrix protein clusters PS to enhance viral assembly, budding, and spread from the host cell while also laying the groundwork for fundamental drug targeting strategies.
MeSH term(s)	Animals ; Hemorrhagic Fever, Ebola/metabolism ; Ebolavirus/physiology ; Phosphatidylserines/metabolism ; Fendiline/metabolism ; Viral Matrix Proteins/metabolism ; Virus Assembly ; Cluster Analysis ; Mammals/metabolism
Chemical Substances	Phosphatidylserines ; Fendiline (S253D559A8) ; Viral Matrix Proteins
Language	English
Publishing date	2022-09-12
Publishing country	England
Document type	Journal Article
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.202051709
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Article ; Online: A pyrene-based two-photon excitable fluorescent probe to visualize nuclei in live cells.

Abeywickrama, Chathura S / Wijesinghe, Kaveesha J / Plescia, Caroline B / Fisher, Lloyd S / Goodson, Theodore / Stahelin, Robert V / Pang, Yi

Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology

2020 Volume 19, Issue 9, Page(s) 1152–1159

Abstract: The two-photon absorption properties of a pyrene-pyridinium dye (1) were studied for potential application in two-photon spectroscopy. When probe 1 was used in cellular two-photon fluorescence microscopy imaging, it allowed the visualization of nuclei in ...

Abstract	The two-photon absorption properties of a pyrene-pyridinium dye (1) were studied for potential application in two-photon spectroscopy. When probe 1 was used in cellular two-photon fluorescence microscopy imaging, it allowed the visualization of nuclei in live cells with a relatively low probe concentration (such as 1 μM). Spectroscopic evidence further revealed that probe 1 interacted with DNA as an intercalator. The proposed DNA intercalation properties of probe 1 were consistent with the experimental findings that suggested that the observed nucleus staining ability is dependent on the substituents on the pyridinium fragment of the probe.
MeSH term(s)	Animals ; COS Cells ; Cattle ; Cell Nucleus/chemistry ; Cell Survival ; Cells, Cultured ; Chlorocebus aethiops ; DNA/chemistry ; Fluorescent Dyes/chemistry ; Microscopy, Fluorescence ; Molecular Structure ; Photons ; Pyrenes/chemistry ; Pyridinium Compounds/chemistry
Chemical Substances	Fluorescent Dyes ; Pyrenes ; Pyridinium Compounds ; DNA (9007-49-2) ; calf thymus DNA (91080-16-9) ; pyrene (9E0T7WFW93)
Language	English
Publishing date	2020-07-08
Publishing country	England
Document type	Journal Article
ZDB-ID	2072584-X
ISSN	1474-9092 ; 1474-905X
ISSN (online)	1474-9092
ISSN	1474-905X
DOI	10.1039/d0pp00107d
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Article: SARS-CoV-2 viral budding and entry can be modeled using virus-like particles.

Plescia, Caroline B / David, Emily A / Patra, Dhabaleswar / Sengupta, Ranjan / Amiar, Souad / Su, Yuan / Stahelin, Robert V

bioRxiv : the preprint server for biology

2020

Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China and expeditiously spread across the globe causing a global pandemic. While a select agent designation has not been made for SARS-CoV-2, ... ...

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China and expeditiously spread across the globe causing a global pandemic. While a select agent designation has not been made for SARS-CoV-2, closely related SARS-CoV-1 and MERS coronaviruses are classified as Risk Group 3 select agents, which restricts use of the live viruses to BSL-3 facilities. Such BSL-3 classification make SARS-CoV-2 research inaccessible to the majority of functioning research laboratories in the US; this becomes problematic when the collective scientific effort needs to be focused on such in the face of a pandemic. In this work, we assessed the four structural proteins from SARS-CoV-2 for their ability to form viruslike particles (VLPs) from human cells to form a competent system for BSL-2 studies of SARS-CoV-2. Herein, we provide methods and resources of producing, purifying, fluorescently and APEX2-labeling of SARS-CoV-2 VLPs for the evaluation of mechanisms of viral budding and entry as well as assessment of drug inhibitors under BSL-2 conditions.
Keywords	covid19
Language	English
Publishing date	2020-10-01
Publishing country	United States
Document type	Preprint
DOI	10.1101/2020.09.30.320903
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Article ; Online: SARS-CoV-2 viral budding and entry can be modeled using BSL-2 level virus-like particles.

Plescia, Caroline B / David, Emily A / Patra, Dhabaleswar / Sengupta, Ranjan / Amiar, Souad / Su, Yuan / Stahelin, Robert V

The Journal of biological chemistry

2020 Volume 296, Page(s) 100103

Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China, and expeditiously spread across the globe causing a global pandemic. Research on SARS-CoV-2, as well as the closely related SARS-CoV-1 and ...

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China, and expeditiously spread across the globe causing a global pandemic. Research on SARS-CoV-2, as well as the closely related SARS-CoV-1 and MERS coronaviruses, is restricted to BSL-3 facilities. Such BSL-3 classification makes SARS-CoV-2 research inaccessible to the majority of functioning research laboratories in the United States; this becomes problematic when the collective scientific effort needs to be focused on such in the face of a pandemic. However, a minimal system capable of recapitulating different steps of the viral life cycle without using the virus' genetic material could increase accessibility. In this work, we assessed the four structural proteins from SARS-CoV-2 for their ability to form virus-like particles (VLPs) from human cells to form a competent system for BSL-2 studies of SARS-CoV-2. Herein, we provide methods and resources of producing, purifying, fluorescently and APEX2-labeling of SARS-CoV-2 VLPs for the evaluation of mechanisms of viral budding and entry as well as assessment of drug inhibitors under BSL-2 conditions. These systems should be useful to those looking to circumvent BSL-3 work with SARS-CoV-2 yet study the mechanisms by which SARS-CoV-2 enters and exits human cells.
MeSH term(s)	Biomimetic Materials/chemistry ; Biomimetic Materials/metabolism ; Containment of Biohazards/classification ; Coronavirus Envelope Proteins/genetics ; Coronavirus Envelope Proteins/metabolism ; Gene Expression ; Genes, Reporter ; Government Regulation ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Humans ; Luminescent Proteins/genetics ; Luminescent Proteins/metabolism ; Microscopy, Electron ; Nucleocapsid Proteins/genetics ; Nucleocapsid Proteins/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; SARS-CoV-2/genetics ; SARS-CoV-2/growth & development ; SARS-CoV-2/metabolism ; SARS-CoV-2/ultrastructure ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Viral Matrix Proteins/genetics ; Viral Matrix Proteins/metabolism ; Virion/genetics ; Virion/growth & development ; Virion/metabolism ; Virion/ultrastructure ; Virus Assembly/physiology ; Virus Internalization ; Virus Release/physiology ; Red Fluorescent Protein
Chemical Substances	Coronavirus Envelope Proteins ; Luminescent Proteins ; Nucleocapsid Proteins ; Recombinant Proteins ; Spike Glycoprotein, Coronavirus ; Viral Matrix Proteins ; envelope protein, SARS-CoV-2 ; membrane protein, SARS-CoV-2 ; spike protein, SARS-CoV-2 ; Green Fluorescent Proteins (147336-22-9)
Keywords	covid19
Language	English
Publishing date	2020-11-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.016148
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Article ; Online: Characterization of the Relationship between the Chaperone and Lipid-Binding Functions of the 70-kDa Heat-Shock Protein, HspA1A

Larissa Smulders / Amanda J. Daniels / Caroline B. Plescia / Devon Berger / Robert V. Stahelin / Nikolas Nikolaidis

International Journal of Molecular Sciences, Vol 21, Iss 5995, p

2020 Volume 5995

Abstract: HspA1A, a molecular chaperone, translocates to the plasma membrane (PM) of stressed and cancer cells. This translocation results in HspA1A’s cell-surface presentation, which renders tumors radiation insensitive. To specifically inhibit the lipid-driven ... ...

Abstract	HspA1A, a molecular chaperone, translocates to the plasma membrane (PM) of stressed and cancer cells. This translocation results in HspA1A’s cell-surface presentation, which renders tumors radiation insensitive. To specifically inhibit the lipid-driven HspA1A’s PM translocation and devise new therapeutics it is imperative to characterize the unknown HspA1A’s lipid-binding regions and determine the relationship between the chaperone and lipid-binding functions. To elucidate this relationship, we determined the effect of phosphatidylserine (PS)-binding on the secondary structure and chaperone functions of HspA1A. Circular dichroism revealed that binding to PS resulted in minimal modification on HspA1A’s secondary structure. Measuring the release of inorganic phosphate revealed that PS-binding had no effect on HspA1A’s ATPase activity. In contrast, PS-binding showed subtle but consistent increases in HspA1A’s refolding activities. Furthermore, using a Lysine-71-Alanine mutation (K71A; a null-ATPase mutant) of HspA1A we show that although K71A binds to PS with affinities similar to the wild-type (WT), the mutated protein associates with lipids three times faster and dissociates 300 times faster than the WT HspA1A. These observations suggest a two-step binding model including an initial interaction of HspA1A with lipids followed by a conformational change of the HspA1A-lipid complex, which accelerates the binding reaction. Together these findings strongly support the notion that the chaperone and lipid-binding activities of HspA1A are dependent but the regions mediating these functions do not overlap and provide the basis for future interventions to inhibit HspA1A’s PM-translocation in tumor cells, making them sensitive to radiation therapy.
Keywords	chaperone function ; heat-shock proteins ; lipid binding ; phosphatidylserine ; protein refolding ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	500
Language	English
Publishing date	2020-08-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: The first DEP domain of the RhoGEF P-Rex1 autoinhibits activity and contributes to membrane binding.

Ravala, Sandeep K / Hopkins, Jesse B / Plescia, Caroline B / Allgood, Samantha R / Kane, Madison A / Cash, Jennifer N / Stahelin, Robert V / Tesmer, John J G

The Journal of biological chemistry

2020 Volume 295, Issue 36, Page(s) 12635–12647

Abstract: Phosphatidylinositol (3,4,5)-trisphosphate ( ... ...

Abstract	Phosphatidylinositol (3,4,5)-trisphosphate (PIP
MeSH term(s)	Cell Membrane/chemistry ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Cyclic AMP-Dependent Protein Kinases/chemistry ; Cyclic AMP-Dependent Protein Kinases/genetics ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Guanine Nucleotide Exchange Factors/chemistry ; Guanine Nucleotide Exchange Factors/genetics ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Phosphorylation ; Protein Domains
Chemical Substances	Guanine Nucleotide Exchange Factors ; PREX1 protein, human ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11)
Language	English
Publishing date	2020-07-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA120.014534
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Article ; Online: SARS-CoV-2 viral budding and entry can be modeled using virus-like particles

Plescia, Caroline B. / David, Emily A. / Patra, Dhabaleswar / Sengupta, Ranjan / Amiar, Souad / Su, Yuan / Stahelin, Robert V.

bioRxiv

Abstract	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was first discovered in December 2019 in Wuhan, China and expeditiously spread across the globe causing a global pandemic. While a select agent designation has not been made for SARS-CoV-2, closely related SARS-CoV-1 and MERS coronaviruses are classified as Risk Group 3 select agents, which restricts use of the live viruses to BSL-3 facilities. Such BSL-3 classification make SARS-CoV-2 research inaccessible to the majority of functioning research laboratories in the US; this becomes problematic when the collective scientific effort needs to be focused on such in the face of a pandemic. In this work, we assessed the four structural proteins from SARS-CoV-2 for their ability to form virus-like particles (VLPs) from human cells to form a competent system for BSL-2 studies of SARS-CoV-2. Herein, we provide methods and resources of producing, purifying, fluorescently and APEX2-labeling of SARS-CoV-2 VLPs for the evaluation of mechanisms of viral budding and entry as well as assessment of drug inhibitors under BSL-2 conditions.
Keywords	covid19
Language	English
Publishing date	2020-10-01
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.09.30.320903
Database	COVID19

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