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Article ; Online: Widespread Distribution and Evolution of Poxviral Entry-Fusion Complex Proteins in Giant Viruses.

Kao, Sheng / Kao, Chi-Fei / Chang, Wen / Ku, Chuan

2023 , Page(s) e0494422

Abstract: Poxviruses are known to encode a set of proteins that form an entry-fusion complex (EFC) to mediate virus entry. However, the diversity, evolution, and origin of these EFC proteins remain poorly understood. Here, we identify the EFC protein homologs in ... ...

Abstract	Poxviruses are known to encode a set of proteins that form an entry-fusion complex (EFC) to mediate virus entry. However, the diversity, evolution, and origin of these EFC proteins remain poorly understood. Here, we identify the EFC protein homologs in poxviruses and other giant viruses of the phylum
Language	English
Publishing date	2023-03-13
Publishing country	United States
Document type	Journal Article
ZDB-ID	2807133-5
ISSN	2165-0497 ; 2165-0497
ISSN (online)	2165-0497
ISSN	2165-0497
DOI	10.1128/spectrum.04944-22
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Structural and functional analysis of vaccinia viral fusion complex component protein A28 through NMR and molecular dynamic simulations.

Chi-Fei Kao / Min-Hsin Tsai / Kathleen Joyce Carillo / Der-Lii Tzou / Wen Chang

PLoS Pathogens, Vol 19, Iss 11, p e

2023 Volume 1011500

Abstract: Host cell entry of vaccinia virus (a poxvirus) proceeds through multiple steps that involve many viral proteins to mediate cell infection. Upon binding to cells, vaccinia virus membrane fuses with host membranes via a viral entry fusion protein complex ... ...

Abstract	Host cell entry of vaccinia virus (a poxvirus) proceeds through multiple steps that involve many viral proteins to mediate cell infection. Upon binding to cells, vaccinia virus membrane fuses with host membranes via a viral entry fusion protein complex comprising 11 proteins: A16, A21, A28, F9, G3, G9, H2, J5, L1, L5 and O3. Despite vaccinia virus having two infectious forms, mature and enveloped, that have different membrane layers, both forms require an identical viral entry fusion complex for membrane fusion. Components of the poxvirus entry fusion complex that have been structurally assessed to date share no known homology with all other type I, II and III viral fusion proteins, and the large number of fusion protein components renders it a unique system to investigate poxvirus-mediated membrane fusion. Here, we determined the NMR structure of a truncated version of vaccinia A28 protein. We also expressed a soluble H2 protein and showed that A28 interacts with H2 protein at a 1:1 ratio in vitro. Furthermore, we performed extensive in vitro alanine mutagenesis to identify A28 protein residues that are critical for H2 binding, entry fusion complex formation, and virus-mediated membrane fusion. Finally, we used molecular dynamic simulations to model full-length A28-H2 subcomplex in membranes. In summary, we characterized vaccinia virus A28 protein and determined residues important in its interaction with H2 protein and membrane components. We also provide a structural model of the A28-H2 protein interaction to illustrate how it forms a 1:1 subcomplex on a modeled membrane.
Keywords	Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2023-11-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Structural and functional analysis of vaccinia viral fusion complex component protein A28 through NMR and molecular dynamic simulations.

Kao, Chi-Fei / Tsai, Min-Hsin / Carillo, Kathleen Joyce / Tzou, Der-Lii / Chang, Wen

PLoS pathogens

2023 Volume 19, Issue 11, Page(s) e1011500

Abstract	Host cell entry of vaccinia virus (a poxvirus) proceeds through multiple steps that involve many viral proteins to mediate cell infection. Upon binding to cells, vaccinia virus membrane fuses with host membranes via a viral entry fusion protein complex comprising 11 proteins: A16, A21, A28, F9, G3, G9, H2, J5, L1, L5 and O3. Despite vaccinia virus having two infectious forms, mature and enveloped, that have different membrane layers, both forms require an identical viral entry fusion complex for membrane fusion. Components of the poxvirus entry fusion complex that have been structurally assessed to date share no known homology with all other type I, II and III viral fusion proteins, and the large number of fusion protein components renders it a unique system to investigate poxvirus-mediated membrane fusion. Here, we determined the NMR structure of a truncated version of vaccinia A28 protein. We also expressed a soluble H2 protein and showed that A28 interacts with H2 protein at a 1:1 ratio in vitro. Furthermore, we performed extensive in vitro alanine mutagenesis to identify A28 protein residues that are critical for H2 binding, entry fusion complex formation, and virus-mediated membrane fusion. Finally, we used molecular dynamic simulations to model full-length A28-H2 subcomplex in membranes. In summary, we characterized vaccinia virus A28 protein and determined residues important in its interaction with H2 protein and membrane components. We also provide a structural model of the A28-H2 protein interaction to illustrate how it forms a 1:1 subcomplex on a modeled membrane.
MeSH term(s)	Humans ; Vaccinia virus/metabolism ; Vaccinia ; Molecular Dynamics Simulation ; Viral Fusion Proteins/metabolism ; Poxviridae/metabolism ; Virus Internalization
Chemical Substances	Viral Fusion Proteins
Language	English
Publishing date	2023-11-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1011500
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Investigation of the Role of the Spike Protein in Reversing the Virulence of the Highly Virulent Taiwan Porcine Epidemic Diarrhea Virus Pintung 52 Strains and Its Attenuated Counterpart.

Kao, Chi-Fei / Chang, Hui-Wen

Viruses

2019 Volume 12, Issue 1

Abstract: Porcine epidemic diarrhea virus (PEDV) has continuously caused severe economic losses to the global swine industries; however, no successful vaccine against PEDV has been developed. In this study, we generated four autologous recombinant viruses, ... ...

Abstract	Porcine epidemic diarrhea virus (PEDV) has continuously caused severe economic losses to the global swine industries; however, no successful vaccine against PEDV has been developed. In this study, we generated four autologous recombinant viruses, including the highly virulent iPEDVPT-P5, attenuated iPEDVPT-P96, and two chimeric viruses (iPEDVPT-P5-96S and iPEDVPT-P96-5S) with the reciprocally exchanged
MeSH term(s)	Animals ; Chlorocebus aethiops ; Coronavirus Infections/virology ; Diarrhea/virology ; Feces/virology ; Mutation ; Porcine epidemic diarrhea virus/genetics ; Porcine epidemic diarrhea virus/pathogenicity ; Reverse Genetics ; Spike Glycoprotein, Coronavirus/genetics ; Swine ; Swine Diseases/virology ; Taiwan ; Vaccines, Attenuated/genetics ; Vero Cells ; Viral Vaccines ; Virulence ; Virus Shedding
Chemical Substances	Spike Glycoprotein, Coronavirus ; Vaccines, Attenuated ; Viral Vaccines
Keywords	covid19
Language	English
Publishing date	2019-12-30
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v12010041
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Investigation of the Role of the Spike Protein in Reversing the Virulence of the Highly Virulent Taiwan Porcine Epidemic Diarrhea Virus Pintung 52 Strains and Its Attenuated Counterpart

Kao, Chi-Fei / Chang, Hui-Wen

Viruses. 2019 Dec. 30, v. 12, no. 1

2019

Abstract	Porcine epidemic diarrhea virus (PEDV) has continuously caused severe economic losses to the global swine industries; however, no successful vaccine against PEDV has been developed. In this study, we generated four autologous recombinant viruses, including the highly virulent iPEDVPT-P5, attenuated iPEDVPT-P96, and two chimeric viruses (iPEDVPT-P5-96S and iPEDVPT-P96-5S) with the reciprocally exchanged spike (S) gene, to study the role of the S gene in PEDV pathogenesis. A deeper understanding of PEDV attenuation will aid in the rational design of a live attenuated vaccine (LAV) using reverse genetics system. Our results showed that replacing the S gene from the highly virulent iPEDVPT-P5 led to complete restoration of virulence of the attenuated iPEDVPT-P96, with nearly identical viral shedding, diarrhea pattern, and mortality rate as the parental iPEDVPT-P5. In contrast, substitution of the S gene with that from the attenuated iPEDVPT-P96 resulted in partial attenuation of iPEDVPT-P5, exhibiting similar viral shedding and diarrhea patterns as the parental iPEDVPT-P96 with slightly severe histological lesions and higher mortality rate. Collectively, our data confirmed that the attenuation of the PEDVPT-P96 virus is primarily attributed to mutations in the S gene. However, mutation in S gene alone could not fully attenuate the virulence of iPEDVPT-P5. Gene (s) other than S gene might also play a role in determining virulence.
Keywords	Porcine epidemic diarrhea virus ; diarrhea ; genes ; histology ; live vaccines ; mortality ; mutation ; pathogenesis ; reverse genetics ; viral shedding ; virulence ; viruses ; Taiwan
Language	English
Dates of publication	2019-1230
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v12010041
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Structural and functional analyses of viral H2 protein of the vaccinia virus entry fusion complex.

Kao, Chi-Fei / Liu, Chang-Yi / Hsieh, Chia-Lin / Carillo, Kathleen Joyce D / Tzou, Der-Lii M / Wang, Hao-Ching / Chang, Wen

Journal of virology

2023 Volume 97, Issue 12, Page(s) e0134323

Abstract: Importance: Vaccinia virus infection requires virus-cell membrane fusion to complete entry during endocytosis; however, it contains a large viral fusion protein complex of 11 viral proteins that share no structure or sequence homology to all the known ... ...

Abstract	Importance: Vaccinia virus infection requires virus-cell membrane fusion to complete entry during endocytosis; however, it contains a large viral fusion protein complex of 11 viral proteins that share no structure or sequence homology to all the known viral fusion proteins, including type I, II, and III fusion proteins. It is thus very challenging to investigate how the vaccinia fusion complex works to trigger membrane fusion with host cells. In this study, we crystallized the ectodomain of vaccinia H2 protein, one component of the viral fusion complex. Furthermore, we performed a series of mutational, biochemical, and molecular analyses and identified two surface loops containing
MeSH term(s)	Membrane Fusion ; Vaccinia virus/chemistry ; Vaccinia virus/genetics ; Vaccinia virus/metabolism ; Viral Fusion Proteins/chemistry ; Viral Fusion Proteins/genetics ; Viral Fusion Proteins/metabolism ; Virus Internalization
Chemical Substances	Viral Fusion Proteins
Language	English
Publishing date	2023-11-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01343-23
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Disseminated Candidiasis and Candidemia Caused by

Wang, Wen-Lin / Sun, Pei-Lun / Kao, Chi-Fei / Li, Wen-Ta / Cheng, I-Jiunn / Yu, Pin-Huan

Animals : an open access journal from MDPI

2021 Volume 11, Issue 12

Abstract: A sub-adult green sea turtle ( ...

Abstract	A sub-adult green sea turtle (
Language	English
Publishing date	2021-12-07
Publishing country	Switzerland
Document type	Journal Article
ISSN	2076-2615
ISSN	2076-2615
DOI	10.3390/ani11123480
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Intramuscular Immunization with Chemokine-Adjuvanted Inactive Porcine Epidemic Diarrhea Virus Induces Substantial Protection in Pigs.

Hsueh, Fu-Chun / Chang, Yen-Chen / Kao, Chi-Fei / Hsu, Chin-Wei / Chang, Hui-Wen

Vaccines

2020 Volume 8, Issue 1

Abstract: Intramuscular (IM) immunization is generally considered incapable of generating a protective mucosal immune response. In the swine industry, attempts to develop a safe and protective vaccine for controlling porcine epidemic diarrhea (PED) via an IM route ...

Abstract	Intramuscular (IM) immunization is generally considered incapable of generating a protective mucosal immune response. In the swine industry, attempts to develop a safe and protective vaccine for controlling porcine epidemic diarrhea (PED) via an IM route of administration have been unsuccessful. In the present study, porcine chemokine ligand proteins CCL25, 27, and 28 were constructed and stably expressed in the mammalian expression system. IM co-administration of inactivated PEDV (iPEDV) particles with different CC chemokines and Freund's adjuvants resulted in recruiting CCR9+ and/or CCR10+ inflammatory cells to the injection site, thereby inducing superior systemic PEDV specific IgG, fecal IgA, and viral neutralizing antibodies in pigs. Moreover, pigs immunized with iPEDV in combination with CCL25 and CCL28 elicited substantial protection against a virulent PEDV challenge. We show that the porcine CC chemokines could be novel adjuvants for developing IM vaccines for modulating mucosal immune responses against mucosal transmissible pathogens in pigs.
Keywords	covid19
Language	English
Publishing date	2020-02-24
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines8010102
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Disseminated Candidiasis and Candidemia Caused by Candida palmioleophila in a Green Sea Turtle ( Chelonia mydas )

Wen-Lin Wang / Pei-Lun Sun / Chi-Fei Kao / Wen-Ta Li / I-Jiunn Cheng / Pin-Huan Yu

Animals, Vol 11, Iss 3480, p

2021 Volume 3480

Abstract: A sub-adult green sea turtle ( Chelonia mydas ) was rescued and treated for carapace and plastron shell fractures. The turtle was kept dry-docked for the first 2 months with a placement of a long-term jugular central venous catheter (CVC). Pain ... ...

Abstract	A sub-adult green sea turtle ( Chelonia mydas ) was rescued and treated for carapace and plastron shell fractures. The turtle was kept dry-docked for the first 2 months with a placement of a long-term jugular central venous catheter (CVC). Pain management, aggressive antibiotic and anthelmintic therapy, fluid therapy, force feeding, and wound debridement were provided to manage the shell fractures and control bacteremia. Human albumin was administered to treat severe hypoalbuminemia. On day 59, small budding yeasts were noted on the blood smears. Candidemia was confirmed by blood culture, as the yeasts were identified as Candida palmioleophila by the molecular multi-locus identification method. The CVC was removed, and the patient was treated with itraconazole. Although the carapace and plastron wounds had epithelized by 5.5 months after the rescue, the turtle died unexpectedly by 7.5 months. The postmortem examination revealed numerous necrogranulomas with intralesional yeasts, morphologically compatible with Candida spp., in joints, bones, brain, and lungs, suggestive of disseminated candidiasis. We describe a rare case of candidemia in the veterinary field. To our knowledge, this is the first report of candidiasis caused by C. palmioleophila in a reptile. The present results should improve veterinary medical care and, therefore, enhance the conservation of endangered sea turtle species.
Keywords	Candida palmioleophila ; candidemia ; central venous catheter ; Chelonia mydas ; disseminated candidiasis ; green sea turtle ; Veterinary medicine ; SF600-1100 ; Zoology ; QL1-991
Language	English
Publishing date	2021-12-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Disseminated Candidiasis and Candidemia Caused by Candida palmioleophila in a Green Sea Turtle (Chelonia mydas)

Wang, Wen-Lin / Sun, Pei-Lun / Kao, Chi-Fei / Li, Wen-Ta / Cheng, I-Jiunn / Yu, Pin-Huan

Animals. 2021 Dec. 07, v. 11, no. 12

2021

Abstract: A sub-adult green sea turtle (Chelonia mydas) was rescued and treated for carapace and plastron shell fractures. The turtle was kept dry-docked for the first 2 months with a placement of a long-term jugular central venous catheter (CVC). Pain management, ...

Abstract	A sub-adult green sea turtle (Chelonia mydas) was rescued and treated for carapace and plastron shell fractures. The turtle was kept dry-docked for the first 2 months with a placement of a long-term jugular central venous catheter (CVC). Pain management, aggressive antibiotic and anthelmintic therapy, fluid therapy, force feeding, and wound debridement were provided to manage the shell fractures and control bacteremia. Human albumin was administered to treat severe hypoalbuminemia. On day 59, small budding yeasts were noted on the blood smears. Candidemia was confirmed by blood culture, as the yeasts were identified as Candida palmioleophila by the molecular multi-locus identification method. The CVC was removed, and the patient was treated with itraconazole. Although the carapace and plastron wounds had epithelized by 5.5 months after the rescue, the turtle died unexpectedly by 7.5 months. The postmortem examination revealed numerous necrogranulomas with intralesional yeasts, morphologically compatible with Candida spp., in joints, bones, brain, and lungs, suggestive of disseminated candidiasis. We describe a rare case of candidemia in the veterinary field. To our knowledge, this is the first report of candidiasis caused by C. palmioleophila in a reptile. The present results should improve veterinary medical care and, therefore, enhance the conservation of endangered sea turtle species.
Keywords	Candida ; Chelonia mydas ; albumins ; anthelmintics ; antibiotics ; bacteremia ; blood ; brain ; candidemia ; candidiasis ; central venous catheters ; debridement ; fluid therapy ; forced feeding ; humans ; hypoalbuminemia ; itraconazole ; necropsy ; pain ; patients ; sea turtles
Language	English
Dates of publication	2021-1207
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2606558-7
ISSN	2076-2615
ISSN	2076-2615
DOI	10.3390/ani11123480
Database	NAL-Catalogue (AGRICOLA)

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