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Article ; Online: Pathogenic prion structures at high resolution.

Caughey, Byron / Standke, Heidi G / Artikis, Efrosini / Hoyt, Forrest / Kraus, Allison

2022 Volume 18, Issue 6, Page(s) e1010594

MeSH term(s)	Humans ; PrPSc Proteins/chemistry ; Prion Diseases ; Prions/chemistry
Chemical Substances	PrPSc Proteins ; Prions
Language	English
Publishing date	2022-06-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010594
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Replication of Coxiella burnetii in a Lysosome-Like Vacuole Does Not Require Lysosomal Hydrolases.

Miller, Heather E / Hoyt, Forrest H / Heinzen, Robert A

Infection and immunity

2019 Volume 87, Issue 11

Abstract: ... Coxiella ... ...

Abstract	Coxiella burnetii
MeSH term(s)	Amino Acids/administration & dosage ; Amino Acids/pharmacology ; Cathepsin D ; Cell Proliferation ; Cholesterol/metabolism ; Coxiella burnetii ; Culture Media ; HeLa Cells ; Humans ; Hydrogen-Ion Concentration ; Hydrolases/metabolism ; Lysosomes ; Macrolides/pharmacology ; Microbial Viability
Chemical Substances	Amino Acids ; Culture Media ; Macrolides ; bafilomycin A1 (88899-55-2) ; Cholesterol (97C5T2UQ7J) ; Hydrolases (EC 3.-) ; Cathepsin D (EC 3.4.23.5)
Language	English
Publishing date	2019-10-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.00493-19
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: High-resolution structure and strain comparison of infectious mammalian prions

Kraus, Allison / Hoyt, Forrest / Schwartz, Cindi L. / Hansen, Bryan / Artikis, Efrosini / Hughson, Andrew G. / Raymond, Gregory J. / Race, Brent / Baron, Gerald S. / Caughey, Byron

Molecular cell. 2021 Nov. 04, v. 81, no. 21

2021

Abstract: Within the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼10⁹ lethal doses per milligram). The structures of such lethal assemblies of PrP molecules have been poorly understood. ...

Abstract	Within the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼10⁹ lethal doses per milligram). The structures of such lethal assemblies of PrP molecules have been poorly understood. Here we report a near-atomic core structure of a brain-derived, fully infectious prion (263K strain). Cryo-electron microscopy showed amyloid fibrils assembled with parallel in-register intermolecular β sheets. Each monomer provides one rung of the ordered fibril core, with N-linked glycans and glycolipid anchors projecting outward. Thus, single monomers form the templating surface for incoming monomers at fibril ends, where prion growth occurs. Comparison to another prion strain (aRML) revealed major differences in fibril morphology but, like 263K, an asymmetric fibril cross-section without paired protofilaments. These findings provide structural insights into prion propagation, strains, species barriers, and membrane pathogenesis. This structure also helps frame considerations of factors influencing the relative transmissibility of other pathologic amyloids.
Keywords	amyloid ; cryo-electron microscopy ; glycolipids ; mammals ; pathogenesis ; polysaccharides ; prions
Language	English
Dates of publication	2021-1104
Size	p. 4540-4551.e6.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2021.08.011
Database	NAL-Catalogue (AGRICOLA)

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Article: Disruption of the Golgi Apparatus and Contribution of the Endoplasmic Reticulum to the SARS-CoV-2 Replication Complex

Hackstadt, Ted / Chiramel, Abhilash I. / Hoyt, Forrest H. / Williamson, Brandi N. / Dooley, Cheryl A. / Beare, Paul A. / de Wit, Emmie / Best, Sonja M. / Fischer, Elizabeth R.

Viruses. 2021 Sept. 09, v. 13, no. 9

2021

Abstract: A variety of immunolabeling procedures for both light and electron microscopy were used to examine the cellular origins of the host membranes supporting the SARS-CoV-2 replication complex. The endoplasmic reticulum has long been implicated as a source of ...

Abstract	A variety of immunolabeling procedures for both light and electron microscopy were used to examine the cellular origins of the host membranes supporting the SARS-CoV-2 replication complex. The endoplasmic reticulum has long been implicated as a source of membrane for the coronavirus replication organelle. Using dsRNA as a marker for sites of viral RNA synthesis, we provide additional evidence supporting ER as a prominent source of membrane. In addition, we observed a rapid fragmentation of the Golgi apparatus which is visible by 6 h and complete by 12 h post-infection. Golgi derived lipid appears to be incorporated into the replication organelle although protein markers are dispersed throughout the infected cell. The mechanism of Golgi disruption is undefined, but chemical disruption of the Golgi apparatus by brefeldin A is inhibitory to viral replication. A search for an individual SARS-CoV-2 protein responsible for this activity identified at least five viral proteins, M, S, E, Orf6, and nsp3, that induced Golgi fragmentation when expressed in eukaryotic cells. Each of these proteins, as well as nsp4, also caused visible changes to ER structure as shown by correlative light and electron microscopy (CLEM). Collectively, these results imply that specific disruption of the Golgi apparatus is a critical component of coronavirus replication.
Keywords	Golgi apparatus ; Severe acute respiratory syndrome coronavirus 2 ; brefeldin A ; electron microscopy ; endoplasmic reticulum ; lipids ; virus replication
Language	English
Dates of publication	2021-0909
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v13091798
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Article ; Online: Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains.

Hoyt, Forrest / Standke, Heidi G / Artikis, Efrosini / Schwartz, Cindi L / Hansen, Bryan / Li, Kunpeng / Hughson, Andrew G / Manca, Matteo / Thomas, Olivia R / Raymond, Gregory J / Race, Brent / Baron, Gerald S / Caughey, Byron / Kraus, Allison

Nature communications

2022 Volume 13, Issue 1, Page(s) 4005

Abstract: Little is known about the structural basis of prion strains. Here we provide a high (3.0 Å) resolution cryo-electron microscopy-based structure of infectious brain-derived fibrils of the mouse anchorless RML scrapie strain which, like the recently ... ...

Abstract	Little is known about the structural basis of prion strains. Here we provide a high (3.0 Å) resolution cryo-electron microscopy-based structure of infectious brain-derived fibrils of the mouse anchorless RML scrapie strain which, like the recently determined hamster 263K strain, has a parallel in-register β-sheet-based core. Several structural motifs are shared between these ex vivo prion strains, including an amino-proximal steric zipper and three β-arches. However, detailed comparisons reveal variations in these shared structural topologies and other features. Unlike 263K and wildtype RML prions, the anchorless RML prions lack glycophosphatidylinositol anchors and are severely deficient in N-linked glycans. Nonetheless, the similarity of our anchorless RML structure to one reported for wildtype RML prion fibrils in an accompanying paper indicates that these post-translational modifications do not substantially alter the amyloid core conformation. This work demonstrates both common and divergent structural features of prion strains at the near-atomic level.
MeSH term(s)	Amyloid ; Animals ; Brain/metabolism ; Cryoelectron Microscopy ; Mice ; Prions/metabolism ; Scrapie ; Sheep
Chemical Substances	Amyloid ; Prions
Language	English
Publishing date	2022-07-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-022-30458-6
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Cryo-EM of prion strains from the same genotype of host identifies conformational determinants.

Hoyt, Forrest / Alam, Parvez / Artikis, Efrosini / Schwartz, Cindi L / Hughson, Andrew G / Race, Brent / Baune, Chase / Raymond, Gregory J / Baron, Gerald S / Kraus, Allison / Caughey, Byron

PLoS pathogens

2022 Volume 18, Issue 11, Page(s) e1010947

Abstract: Prion strains in a given type of mammalian host are distinguished by differences in clinical presentation, neuropathological lesions, survival time, and characteristics of the infecting prion protein (PrP) assemblies. Near-atomic structures of prions ... ...

Abstract	Prion strains in a given type of mammalian host are distinguished by differences in clinical presentation, neuropathological lesions, survival time, and characteristics of the infecting prion protein (PrP) assemblies. Near-atomic structures of prions from two host species with different PrP sequences have been determined but comparisons of distinct prion strains of the same amino acid sequence are needed to identify purely conformational determinants of prion strain characteristics. Here we report a 3.2 Å resolution cryogenic electron microscopy-based structure of the 22L prion strain purified from the brains of mice engineered to express only PrP lacking glycophosphatidylinositol anchors [anchorless (a) 22L]. Comparison of this near-atomic structure to our recently determined structure of the aRML strain propagated in the same inbred mouse reveals that these two mouse prion strains have distinct conformational templates for growth via incorporation of PrP molecules of the same sequence. Both a22L and aRML are assembled as stacks of PrP molecules forming parallel in-register intermolecular β-sheets and intervening loops, with single monomers spanning the ordered fibril core. Each monomer shares an N-terminal steric zipper, three major arches, and an overall V-shape, but the details of these and other conformational features differ markedly. Thus, variations in shared conformational motifs within a parallel in-register β-stack fibril architecture provide a structural basis for prion strain differentiation within a single host genotype.
MeSH term(s)	Animals ; Mice ; Cryoelectron Microscopy ; Genotype ; Prion Proteins/genetics ; Prions/metabolism ; Protein Conformation
Chemical Substances	Prion Proteins ; Prions
Language	English
Publishing date	2022-11-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Intramural
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1010947
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Disruption of the Golgi Apparatus and Contribution of the Endoplasmic Reticulum to the SARS-CoV-2 Replication Complex.

Hackstadt, Ted / Chiramel, Abhilash I / Hoyt, Forrest H / Williamson, Brandi N / Dooley, Cheryl A / Beare, Paul A / de Wit, Emmie / Best, Sonja M / Fischer, Elizabeth R

Viruses

2021 Volume 13, Issue 9

Abstract	A variety of immunolabeling procedures for both light and electron microscopy were used to examine the cellular origins of the host membranes supporting the SARS-CoV-2 replication complex. The endoplasmic reticulum has long been implicated as a source of membrane for the coronavirus replication organelle. Using dsRNA as a marker for sites of viral RNA synthesis, we provide additional evidence supporting ER as a prominent source of membrane. In addition, we observed a rapid fragmentation of the Golgi apparatus which is visible by 6 h and complete by 12 h post-infection. Golgi derived lipid appears to be incorporated into the replication organelle although protein markers are dispersed throughout the infected cell. The mechanism of Golgi disruption is undefined, but chemical disruption of the Golgi apparatus by brefeldin A is inhibitory to viral replication. A search for an individual SARS-CoV-2 protein responsible for this activity identified at least five viral proteins, M, S, E, Orf6, and nsp3, that induced Golgi fragmentation when expressed in eukaryotic cells. Each of these proteins, as well as nsp4, also caused visible changes to ER structure as shown by correlative light and electron microscopy (CLEM). Collectively, these results imply that specific disruption of the Golgi apparatus is a critical component of coronavirus replication.
MeSH term(s)	Animals ; Chlorocebus aethiops ; Coronavirus M Proteins/physiology ; Coronavirus M Proteins/ultrastructure ; Endoplasmic Reticulum/ultrastructure ; Endoplasmic Reticulum/virology ; Golgi Apparatus/ultrastructure ; Golgi Apparatus/virology ; Humans ; Intracellular Membranes/ultrastructure ; Intracellular Membranes/virology ; Microscopy, Electron ; SARS-CoV-2/physiology ; SARS-CoV-2/ultrastructure ; Vero Cells ; Viral Structural Proteins/physiology ; Viral Structural Proteins/ultrastructure ; Virus Replication
Chemical Substances	Coronavirus M Proteins ; M protein, SARS-CoV ; Viral Structural Proteins
Language	English
Publishing date	2021-09-09
Publishing country	Switzerland
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v13091798
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: High-resolution structure and strain comparison of infectious mammalian prions.

Kraus, Allison / Hoyt, Forrest / Schwartz, Cindi L / Hansen, Bryan / Artikis, Efrosini / Hughson, Andrew G / Raymond, Gregory J / Race, Brent / Baron, Gerald S / Caughey, Byron

Molecular cell

2021 Volume 81, Issue 21, Page(s) 4540–4551.e6

Abstract: Within the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼ ... ...

Abstract	Within the extensive range of self-propagating pathologic protein aggregates of mammals, prions are the most clearly infectious (e.g., ∼10
MeSH term(s)	Amyloid/chemistry ; Animals ; Brain/metabolism ; Cryoelectron Microscopy/methods ; Glycolipids/chemistry ; Humans ; Image Processing, Computer-Assisted ; Imaging, Three-Dimensional ; Mice ; Phenotype ; Polysaccharides/chemistry ; Prion Proteins/chemistry ; Prions/chemistry ; Prions/ultrastructure ; Protein Binding ; Protein Structure, Secondary ; Thermodynamics
Chemical Substances	Amyloid ; Glycolipids ; Polysaccharides ; Prion Proteins ; Prions
Language	English
Publishing date	2021-08-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1415236-8
ISSN	1097-4164 ; 1097-2765
ISSN (online)	1097-4164
ISSN	1097-2765
DOI	10.1016/j.molcel.2021.08.011
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Transcriptomic profiling of the digestive tract of the rat flea, Xenopsylla cheopis, following blood feeding and infection with Yersinia pestis.

Bland, David M / Martens, Craig A / Virtaneva, Kimmo / Kanakabandi, Kishore / Long, Dan / Rosenke, Rebecca / Saturday, Greg A / Hoyt, Forrest H / Bruno, Daniel P / Ribeiro, José M / Hinnebusch, B Joseph

PLoS neglected tropical diseases

2020 Volume 14, Issue 9, Page(s) e0008688

Abstract: Yersinia pestis, the causative agent of plague, is a highly lethal pathogen transmitted by the bite of infected fleas. Once ingested by a flea, Y. pestis establish a replicative niche in the gut and produce a biofilm that promotes foregut colonization ... ...

Abstract	Yersinia pestis, the causative agent of plague, is a highly lethal pathogen transmitted by the bite of infected fleas. Once ingested by a flea, Y. pestis establish a replicative niche in the gut and produce a biofilm that promotes foregut colonization and transmission. The rat flea Xenopsylla cheopis is an important vector to several zoonotic bacterial pathogens including Y. pestis. Some fleas naturally clear themselves of infection; however, the physiological and immunological mechanisms by which this occurs are largely uncharacterized. To address this, RNA was extracted, sequenced, and distinct transcript profiles were assembled de novo from X. cheopis digestive tracts isolated from fleas that were either: 1) not fed for 5 days; 2) fed sterile blood; or 3) fed blood containing ~5x108 CFU/ml Y. pestis KIM6+. Analysis and comparison of the transcript profiles resulted in identification of 23 annotated (and 11 unknown or uncharacterized) digestive tract transcripts that comprise the early transcriptional response of the rat flea gut to infection with Y. pestis. The data indicate that production of antimicrobial peptides regulated by the immune-deficiency pathway (IMD) is the primary flea immune response to infection with Y. pestis. The remaining infection-responsive transcripts, not obviously associated with the immune response, were involved in at least one of 3 physiological themes: 1) alterations to chemosensation and gut peristalsis; 2) modification of digestion and metabolism; and 3) production of chitin-binding proteins (peritrophins). Despite producing several peritrophin transcripts shortly after feeding, including a subset that were infection-responsive, no thick peritrophic membrane was detectable by histochemistry or electron microscopy of rat flea guts for the first 24 hours following blood-feeding. Here we discuss the physiological implications of rat flea infection-responsive transcripts, the function of X. cheopis peritrophins, and the mechanisms by which Y. pestis may be cleared from the flea gut.
MeSH term(s)	Animals ; Biofilms ; Epithelium/microbiology ; Epithelium/pathology ; Female ; Gastrointestinal Tract/microbiology ; Gastrointestinal Tract/pathology ; Gene Expression Profiling ; Insect Vectors/microbiology ; Plague/microbiology ; Plague/veterinary ; Rats ; Sequence Analysis, RNA ; Transcriptome ; Xenopsylla/microbiology ; Yersinia pestis/genetics ; Yersinia pestis/growth & development ; Yersinia pestis/isolation & purification ; Yersinia pestis/metabolism
Language	English
Publishing date	2020-09-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2429704-5
ISSN	1935-2735 ; 1935-2727
ISSN (online)	1935-2735
ISSN	1935-2727
DOI	10.1371/journal.pntd.0008688
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Scanning electron microscopy.

Fischer, Elizabeth R / Hansen, Bryan T / Nair, Vinod / Hoyt, Forrest H / Dorward, David W

Current protocols in microbiology

2012 Volume Chapter 2, Page(s) Unit 2B.2.

Abstract: Scanning electron microscopy (SEM) remains distinct in its ability to allow topographical visualization of structures. Key elements to consider for successful examination of biological specimens include appropriate preparative and imaging techniques. ... ...

Abstract	Scanning electron microscopy (SEM) remains distinct in its ability to allow topographical visualization of structures. Key elements to consider for successful examination of biological specimens include appropriate preparative and imaging techniques. Chemical processing induces structural artifacts during specimen preparation, and several factors need to be considered when selecting fixation protocols to reduce these effects while retaining structures of interest. Particular care for proper dehydration of specimens is essential to minimize shrinkage and is necessary for placement under the high-vacuum environment required for routine operation of standard SEMs. Choice of substrate for mounting and coating specimens can reduce artifacts known as charging, and a basic understanding of microscope settings can optimize parameters to achieve desired results. This unit describes fundamental techniques and tips for routine specimen preparation for a variety of biological specimens, preservation of labile or fragile structures, immune-labeling strategies, and microscope imaging parameters for optimal examination by SEM.
MeSH term(s)	Biomedical Research/instrumentation ; Biomedical Research/methods ; Image Processing, Computer-Assisted/methods ; Microscopy, Electron, Scanning/instrumentation ; Microscopy, Electron, Scanning/methods ; Specimen Handling/methods
Language	English
Publishing date	2012-05-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Intramural
ZDB-ID	2213675-7
ISSN	1934-8533 ; 1934-8525
ISSN (online)	1934-8533
ISSN	1934-8525
DOI	10.1002/9780471729259.mc02b02s25
Database	MEDical Literature Analysis and Retrieval System OnLINE

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