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Article ; Online: How the COVID-19 Overcomes the Battle? An Approach to Virus Structure.

Ahmadpour, Doryaneh / Ahmadpoor, Pedram

2020 Volume 14, Issue 3, Page(s) 167–172

Abstract: Coronaviruses primarily cause zoonotic infections, however in the past few decades several interspecies transmissions have occurred, the last one by SARS-CoV-2, causing COVID-19 pandemic, posing serious threat to global health. The SARS-CoV-2 spike (S) ... ...

Abstract	Coronaviruses primarily cause zoonotic infections, however in the past few decades several interspecies transmissions have occurred, the last one by SARS-CoV-2, causing COVID-19 pandemic, posing serious threat to global health. The SARS-CoV-2 spike (S) protein plays an important role in viral attachment, fusion and entry. However, other structural and non-structural SARS-CoV-2 proteins are potential influencers in virus pathogenicity. Among these proteins; Orf3, Orf8, and Orf10 show the least homology to SARSCoV proteins and therefore should be further studied for their abilities to modulate antiviral and inflammatory responses. Here, we discuss how SARS-COV-2 interacts with our immune system.
MeSH term(s)	Animals ; Betacoronavirus/genetics ; Betacoronavirus/immunology ; COVID-19 ; Coronavirus Infections/immunology ; Coronavirus Infections/virology ; Gene Order ; Genome, Viral/genetics ; Humans ; Immune System/virology ; Pandemics ; Pneumonia, Viral/immunology ; Pneumonia, Viral/virology ; SARS Virus/genetics ; SARS Virus/immunology ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Viral Structures/genetics ; Virus Internalization
Chemical Substances	Spike Glycoprotein, Coronavirus ; Viral Proteins ; spike protein, SARS-CoV-2
Keywords	covid19
Language	English
Publishing date	2020-04-23
Publishing country	Iran
Document type	Journal Article ; Review
ZDB-ID	2388271-2
ISSN	1735-8604 ; 1735-8582
ISSN (online)	1735-8604
ISSN	1735-8582
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Syntaxin 5-dependent phosphorylation of the small heat shock protein Hsp42 and its role in protein quality control.

Ahmadpour, Doryaneh / Kumar, Navinder / Fischbach, Arthur / Chawla, Srishti / Widlund, Per O / Nyström, Thomas

The FEBS journal

2023 Volume 290, Issue 19, Page(s) 4744–4761

Abstract: The small heat shock protein Hsp42 and the t-SNARE protein Sed5 have central roles in the sequestration of misfolded proteins into insoluble protein deposits in the yeast Saccharomyces cerevisiae. However, whether these proteins/processes interact in ... ...

Abstract	The small heat shock protein Hsp42 and the t-SNARE protein Sed5 have central roles in the sequestration of misfolded proteins into insoluble protein deposits in the yeast Saccharomyces cerevisiae. However, whether these proteins/processes interact in protein quality control (PQC) is not known. Here, we show that Sed5 and anterograde trafficking modulate phosphorylation of Hsp42 partially via the MAPK kinase Hog1. Such phosphorylation, specifically at residue S215, abrogated the co-localization of Hsp42 with the Hsp104 disaggregase, aggregate clearance, chaperone activity, and sequestration of aggregates to IPOD and mitochondria. Furthermore, we found that Hsp42 is hyperphosphorylated in old cells leading to a drastic failure in disaggregation. Old cells also displayed a retarded anterograde trafficking, which, together with slow aggregate clearance and hyperphosphorylation of Hsp42, could be counteracted by Sed5 overproduction. We hypothesize that the breakdown of proper PQC during yeast aging may, in part, be due to a retarded anterograde trafficking leading to hyperphosphorylation of Hsp42.
MeSH term(s)	Heat-Shock Proteins/metabolism ; Heat-Shock Proteins, Small/genetics ; Heat-Shock Proteins, Small/metabolism ; HSP70 Heat-Shock Proteins/metabolism ; Phosphorylation ; Protein Aggregates ; Qa-SNARE Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
Chemical Substances	Heat-Shock Proteins ; Heat-Shock Proteins, Small ; HSP70 Heat-Shock Proteins ; Protein Aggregates ; Qa-SNARE Proteins ; Saccharomyces cerevisiae Proteins ; HSP42 protein, S cerevisiae ; Sed5 protein, S cerevisiae ; HsP104 protein, S cerevisiae (143012-44-6)
Language	English
Publishing date	2023-06-20
Publishing country	England
Document type	Journal Article
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.16886
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Article ; Online: Calcineurin stimulation by Cnb1p overproduction mitigates protein aggregation and α-synuclein toxicity in a yeast model of synucleinopathy.

Chawla, Srishti / Ahmadpour, Doryaneh / Schneider, Kara L / Kumar, Navinder / Fischbach, Arthur / Molin, Mikael / Nystrom, Thomas

Cell communication and signaling : CCS

2023 Volume 21, Issue 1, Page(s) 220

Abstract: The calcium-responsive phosphatase, calcineurin, senses changes in ... ...

Abstract	The calcium-responsive phosphatase, calcineurin, senses changes in Ca
MeSH term(s)	Humans ; Synucleinopathies ; alpha-Synuclein ; Protein Aggregates ; Calcineurin ; Saccharomyces cerevisiae ; Parkinson Disease ; DNA-Binding Proteins ; Transcription Factors ; Saccharomyces cerevisiae Proteins
Chemical Substances	alpha-Synuclein ; Protein Aggregates ; Calcineurin (EC 3.1.3.16) ; CRZ1 protein, S cerevisiae ; DNA-Binding Proteins ; Transcription Factors ; Saccharomyces cerevisiae Proteins
Language	English
Publishing date	2023-08-24
Publishing country	England
Document type	Video-Audio Media ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126315-2
ISSN	1478-811X ; 1478-811X
ISSN (online)	1478-811X
ISSN	1478-811X
DOI	10.1186/s12964-023-01242-w
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Article ; Online: Impact of Circulating SARS-CoV-2 Mutant G614 on the COVID-19 Pandemic.

Ahmadpour, Doryaneh / Ahmadpoor, Pedram / Rostaing, Lionel

Iranian journal of kidney diseases

2020 Volume 14, Issue 5, Page(s) 331–334

Abstract: Coronavirus family has caused several human illnesses, the latest caused by SARS-CoV-2, has led to COVID-19 pandemic posing serious threat to global health. A SARS-CoV-2 variant encoding a D614G mutation in the viral spike (S) protein has now become the ... ...

Abstract	Coronavirus family has caused several human illnesses, the latest caused by SARS-CoV-2, has led to COVID-19 pandemic posing serious threat to global health. A SARS-CoV-2 variant encoding a D614G mutation in the viral spike (S) protein has now become the most prevalent form of the virus worldwide, suggesting a fitness advantage for the mutant. The G614 variant is associated with higher upper respiratory tract viral load, higher infectivity, increased total S protein incorporation into the virion, reduced S1 shedding and a conformational change leading to a more ACE2- binding and fusion- competent state. However, it does not seem to be correlated to increased disease severity or escape neutralizing antibodies.
MeSH term(s)	Betacoronavirus ; COVID-19 ; Coronary Artery Bypass ; Coronavirus Infections ; Humans ; Length of Stay ; Pandemics ; Peptidyl-Dipeptidase A ; Pneumonia, Viral ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Water-Electrolyte Balance
Chemical Substances	Spike Glycoprotein, Coronavirus ; Peptidyl-Dipeptidase A (EC 3.4.15.1)
Keywords	covid19
Language	English
Publishing date	2020-09-17
Publishing country	Iran
Document type	Journal Article
ZDB-ID	2388271-2
ISSN	1735-8604 ; 1735-8582
ISSN (online)	1735-8604
ISSN	1735-8582
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Hitchhiking on vesicles: a way to harness age-related proteopathies?

Ahmadpour, Doryaneh / Babazadeh, Roja / Nystrom, Thomas

The FEBS journal

2020 Volume 287, Issue 23, Page(s) 5068–5079

Abstract: Central to proteopathies and leading to most age-related neurodegenerative disorders is a failure in protein quality control (PQC). To harness the toxicity of misfolded and damaged disease proteins, such proteins are either refolded, degraded by temporal ...

Abstract	Central to proteopathies and leading to most age-related neurodegenerative disorders is a failure in protein quality control (PQC). To harness the toxicity of misfolded and damaged disease proteins, such proteins are either refolded, degraded by temporal PQC, or sequestered by spatial PQC into specific, organelle-associated, compartments within the cell. Here, we discuss the impact of vesicle trafficking pathways in general, and syntaxin 5 in particular, as key players in spatial PQC directing misfolded proteins to the surface of vacuole and mitochondria, which facilitates their clearance and detoxification. Since boosting vesicle trafficking genetically can positively impact on spatial PQC and make cells less sensitive to misfolded disease proteins, we speculate that regulators of such trafficking might serve as therapeutic targets for age-related neurological disorders.
MeSH term(s)	Aging/metabolism ; Aging/pathology ; COP-Coated Vesicles/metabolism ; Humans ; Mitochondria/metabolism ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neurodegenerative Diseases/therapy ; Protein Folding ; Protein Transport ; Proteins/chemistry ; Proteins/metabolism
Chemical Substances	Proteins
Language	English
Publishing date	2020-05-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.15345
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Article ; Online: Extracellular Vesicles Slow Down Aβ(1-42) Aggregation by Interfering with the Amyloid Fibril Elongation Step.

Halipi, Vesa / Sasanian, Nima / Feng, Julia / Hu, Jing / Lubart, Quentin / Bernson, David / van Leeuwen, Daniel / Ahmadpour, Doryaneh / Sparr, Emma / Esbjörner, Elin K

ACS chemical neuroscience

2024 Volume 15, Issue 5, Page(s) 944–954

Abstract: Formation of amyloid-β (Aβ) fibrils is a central pathogenic feature of Alzheimer's disease. Cell-secreted extracellular vesicles (EVs) have been suggested as disease modulators, although their exact roles and relations to Aβ pathology remain unclear. We ... ...

Abstract	Formation of amyloid-β (Aβ) fibrils is a central pathogenic feature of Alzheimer's disease. Cell-secreted extracellular vesicles (EVs) have been suggested as disease modulators, although their exact roles and relations to Aβ pathology remain unclear. We combined kinetics assays and biophysical analyses to explore how small (<220 nm) EVs from neuronal and non-neuronal human cell lines affected the aggregation of the disease-associated Aβ variant Aβ(1-42) into amyloid fibrils. Using thioflavin-T monitored kinetics and seeding assays, we found that EVs reduced Aβ(1-42) aggregation by inhibiting fibril elongation. Morphological analyses revealed this to result in the formation of short fibril fragments with increased thicknesses and less apparent twists. We suggest that EVs may have protective roles by reducing Aβ(1-42) amyloid loads, but also note that the formation of small amyloid fragments could be problematic from a neurotoxicity perspective. EVs may therefore have double-edged roles in the regulation of Aβ pathology in Alzheimer's disease.
MeSH term(s)	Humans ; Amyloid/metabolism ; Alzheimer Disease/metabolism ; Amyloid beta-Peptides/metabolism ; Peptide Fragments/metabolism ; Extracellular Vesicles/metabolism
Chemical Substances	amyloid beta-protein (1-42) ; Amyloid ; Amyloid beta-Peptides ; Peptide Fragments
Language	English
Publishing date	2024-02-26
Publishing country	United States
Document type	Journal Article
ISSN	1948-7193
ISSN (online)	1948-7193
DOI	10.1021/acschemneuro.3c00655
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: How the COVID-19 Overcomes the Battle? An Approach to Virus Structure

Ahmadpour, Doryaneh / Ahmadpoor, Pedram

Iran J Kidney Dis

Abstract	Coronaviruses primarily cause zoonotic infections, however in the past few decades several interspecies transmissions have occurred, the last one by SARS-CoV-2, causing COVID-19 pandemic, posing serious threat to global health. The SARS-CoV-2 spike (S) protein plays an important role in viral attachment, fusion and entry. However, other structural and non-structural SARS-CoV-2 proteins are potential influencers in virus pathogenicity. Among these proteins; Orf3, Orf8, and Orf10 show the least homology to SARSCoV proteins and therefore should be further studied for their abilities to modulate antiviral and inflammatory responses. Here, we discuss how SARS-COV-2 interacts with our immune system.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #32361692
Database	COVID19

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Article ; Online: Inventory study of an early pandemic COVID-19 cohort in South-Eastern Sweden, focusing on neurological manifestations.

Ahmadpour, Doryaneh / Kristoffersson, Anna / Fredrikson, Mats / Huang-Link, Yumin / Eriksson, Anne / Iacobaeus, Ellen / Landtblom, Anne-Marie / Haghighi, Sara

PloS one

2023 Volume 18, Issue 1, Page(s) e0280376

Abstract: Background: Neurological manifestations in patients with COVID-19 have been reported previously as outcomes of the infection. The purpose of current study was to investigate the occurrence of neurological signs and symptoms in COVID-19 patients, in the ... ...

Abstract	Background: Neurological manifestations in patients with COVID-19 have been reported previously as outcomes of the infection. The purpose of current study was to investigate the occurrence of neurological signs and symptoms in COVID-19 patients, in the county of Östergötland in southeastern Sweden. Methods: This is a retrospective, observational cohort study. Data were collected between March 2020 and June 2020. Information was extracted from medical records by a trained research assistant and physician and all data were validated by a senior neurologist. Results: Seventy-four percent of patients developed at least one neurological symptom during the acute phase of the infection. Headache (43%) was the most common neurological symptom, followed by anosmia and/or ageusia (33%), confusion (28%), hallucinations (17%), dizziness (16%), sleep disorders in terms of insomnia and OSAS (Obstructive Sleep Apnea) (9%), myopathy and neuropathy (8%) and numbness and tingling (5%). Patients treated in the ICU had a higher male presentation (73%). Several risk factors in terms of co-morbidities, were identified. Hypertension (54.5%), depression and anxiety (51%), sleep disorders in terms of insomnia and OSAS (30%), cardiovascular morbidity (28%), autoimmune diseases (25%), chronic lung diseases (24%) and diabetes mellitus type 2 (23%) founded as possible risk factors. Conclusion: Neurological symptoms were found in the vast majority (74%) of the patients. Accordingly, attention to neurological, mental and sleep disturbances is warranted with involvement of neurological expertise, in order to avoid further complications and long-term neurological effect of COVID-19. Furthermore, risk factors for more severe COVID-19, in terms of possible co-morbidities that identified in this study should get appropriate attention to optimizing treatment strategies in COVID-19 patients.
MeSH term(s)	Humans ; Male ; COVID-19/epidemiology ; COVID-19/complications ; Sleep Initiation and Maintenance Disorders/epidemiology ; Sleep Initiation and Maintenance Disorders/complications ; Sweden/epidemiology ; Cohort Studies ; Pandemics ; Sleep Apnea, Obstructive/complications
Language	English
Publishing date	2023-01-13
Publishing country	United States
Document type	Observational Study ; Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0280376
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Impact of Circulating SARS-CoV-2 Mutant G614 on the COVID-19 Pandemic

Ahmadpour, Doryaneh / Ahmadpoor, Pedram / Rostaing, Lionel

Iran J Kidney Dis

Abstract	Coronavirus family has caused several human illnesses, the latest caused by SARS-CoV-2, has led to COVID-19 pandemic posing serious threat to global health. A SARS-CoV-2 variant encoding a D614G mutation in the viral spike (S) protein has now become the most prevalent form of the virus worldwide, suggesting a fitness advantage for the mutant. The G614 variant is associated with higher upper respiratory tract viral load, higher infectivity, increased total S protein incorporation into the virion, reduced S1 shedding and a conformational change leading to a more ACE2- binding and fusion- competent state. However, it does not seem to be correlated to increased disease severity or escape neutralizing antibodies.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #777018
Database	COVID19

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Article ; Online: Using reporters of different misfolded proteins reveals differential strategies in processing protein aggregates.

Schneider, Kara L / Ahmadpour, Doryaneh / Keuenhof, Katharina S / Eisele-Bürger, Anna Maria / Berglund, Lisa Larsson / Eisele, Frederik / Babazadeh, Roja / Höög, Johanna L / Nyström, Thomas / Widlund, Per O

The Journal of biological chemistry

2022 Volume 298, Issue 11, Page(s) 102476

Abstract: The accumulation of misfolded proteins is a hallmark of aging and many neurodegenerative diseases, making it important to understand how the cellular machinery recognizes and processes such proteins. A key question in this respect is whether misfolded ... ...

Abstract	The accumulation of misfolded proteins is a hallmark of aging and many neurodegenerative diseases, making it important to understand how the cellular machinery recognizes and processes such proteins. A key question in this respect is whether misfolded proteins are handled in a similar way regardless of their genetic origin. To approach this question, we compared how three different misfolded proteins, guk1-7, gus1-3, and pro3-1, are handled by the cell. We show that all three are nontoxic, even though highly overexpressed, highlighting their usefulness in analyzing the cellular response to misfolding in the absence of severe stress. We found significant differences between the aggregation and disaggregation behavior of the misfolded proteins. Specifically, gus1-3 formed some aggregates that did not efficiently recruit the protein disaggregase Hsp104 and did not colocalize with the other misfolded reporter proteins. Strikingly, while all three misfolded proteins generally coaggregated and colocalized to specific sites in the cell, disaggregation was notably different; the rate of aggregate clearance of pro3-1 was faster than that of the other misfolded proteins, and its clearance rate was not hindered when pro3-1 colocalized with a slowly resolved misfolded protein. Finally, we observed using super-resolution light microscopy as well as immunogold labeling EM in which both showed an even distribution of the different misfolded proteins within an inclusion, suggesting that misfolding characteristics and remodeling, rather than spatial compartmentalization, allows for differential clearance of these misfolding reporters residing in the same inclusion. Taken together, our results highlight how properties of misfolded proteins can significantly affect processing.
MeSH term(s)	Humans ; Protein Aggregates ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Neurodegenerative Diseases/metabolism ; Protein Folding ; Heat-Shock Proteins/metabolism ; Guanylate Kinases/metabolism
Chemical Substances	Protein Aggregates ; Saccharomyces cerevisiae Proteins ; HsP104 protein, S cerevisiae (143012-44-6) ; Heat-Shock Proteins ; Guk1 protein, S cerevisiae ; Guanylate Kinases (EC 2.7.4.8)
Language	English
Publishing date	2022-09-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102476
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